Nonlinear Procedures Applied to Formation Flight Strategies for Spacecraft.
Nonlinear Methodologies Applied to Formation Flight About The Earth.
Càlcul de l'Escissió de Separatrius Usant Tècniques de Matching Complex i Ressurgència, 10/07/2006, UPC.
The Role of Invariant Manifolds in the Formation of Arms and Rings in Barred Galaxies, 12/02/2007, UPC.
On the Meromorphic Non-Integrability of Some Problems in Celestial Mechanics, 09/07/2007, UB.
Contributions to Libration Orbit Mission Design using Hyperbolic Invariant Manifolds, 24/07/2007, UPC.
Analytical and Numerical Tools for the Study of Normally Hyperbolic Invariant Manifolds in Hamiltonian Systems and Their Associated Dynamics, 27/11/2007, UPC.
Differential Galois Theory and Lie-Vessiot Systems, 07/07/2008, UPC.
The Role of Hyperbolic Invariant Objects: From Arnold Diffusion to Biological Clocks, 16/10/2008, UPC.
Galoisian approach to supersymmetric quantum mechanics, 02/07/2009, UPC.
Analytic and Numerical Tools for the Study of QuasiPeriodic Motions in Hamiltonian Systems, 12/01/2010, UPC.
Proximity Maneuvering of Libration Point Orbit Formations Using Adapted Finite Element Methods, 04/02/2010, UPC.
From Non-smooth to Analytic Dynamical Systems: Low Codimension Bifurcations and Exponentially Small Splitting of Separatrices, 19/07/2010, UPC.
The Role and Usage of Libration Point Orbits in the Earth-Moon System, 4/10/2010, UB.
Cálculo de la Escisión de Separatrices y Regiones de Estabilidad Usando Multiprecisión: El Microtrón y la Singularidad Hopfzero, 21/07/2011, UPC.
Haar Wavelets-Based Methods for Credit Risk Portfolio Modelling, 24/11/2011, UPC.
Explicit Integration of Some Integrable Systems of Classical Mechanics, 28/03/2012, UPC.
Noise-induced Reversals in Bistable Visual Perception, 06/06/2012, UPF.
Local and Global Phenomena in Piecewisedefined Systems: From Big Bang Bifurcations to Splitting of Heteroclinic Manifolds, 17/09/2012, UPC.
Homoclinic Phenomena in Conservative Systems, 29/04/2013, UPC.
Global Instability in the Elliptic Restricted Three Body Problem, 16/06/2014, UPC.
Diffusion Through Non-transverse Heteroclinic Chains: A Long-time Instability for the NLS, 06/07/2015, UPC.
Singular Phenomena in the Length Spectrum of Analytic Convex Curves, 06/07/2015, UPC.
Study of Invariant Manifolds in Two Different Problems: the Hopf-zero Singularity and Neural Synchrony, 16/07/2015, UPC.
Dynamical Transport Mechanisms in Celestial Mechanics and Astrodynamics Problems, 30/11/2015, UB.
Bifurcaçoes de Familias a tres paràmetros de Sistemas Planares de Filippov, 27/11/2015, U. Campinas.
Estimació de Connectivitat entre Neurones i Reproducció via Sistemes Lineals a Trossos de Components Neuronals, 2016, UIB.


text:
Buckcherry adds Billy Rowe as second guitarist
Mitch Lafon interviewed Buckcherry guitarist Stevie D. today (August 26, 2020) and Stevie announced that Buckcherry's new guitarist is Jetboy guitarist Billy Rowe.
Rowe replaces Kevin Roentgen who announced his departure from the band earlier this week.
Stevie commented that Rowe and Buckcherry come from the same scene, are close in age, and that Rowe would add a lot to the band since he comes from the same roots as Buckcherry - AC/DC, Rolling Stones, and elements of Punk. Stevie added that Rowe was also a great slide guitar player and that was a plus.
Rowe has been writing and recording new music with Buckcherry and there are plans to tour once Covid is under control.

redpajama_set_name: RedPajamaCommonCrawl


text:
Q: How can I convert a simple java swing code into javafx code using netbeans 7.3.1 IDE Is there any way by which I can convert a simple java swing application which I have already developed in simple java swing using JFrameForm into javaFX? is there
any library or something?

redpajama_set_name: RedPajamaStackExchange


text:
Bg Staffing
(NYSE: BGSF)
SIC-7363 Services-Help Supply Services
BGSF	 -1.74%	 +4.63%	 -3.55%
BG Staffing Acquires L.J. Kushner & Associates, a
BusinessWire via COMTEX - Mon Dec 16, 08:55AM EST
BG Staffing, Inc. (NYSE: BGSF), a growing national provider of workforce solutions, announced that on December 13, 2019, the Company completed the acquisition of substantially all of the assets of L.J. Kushner & Associates, LLC, a(full story)
BGSF: 21.45 (-0.38)
BG Staffing's President and CEO Beth Garvey Recognized
BusinessWire via COMTEX - Wed Dec 11, 08:55AM EST
BG Staffing, Inc. (NYSE: BGSF), a growing national provider of professional temporary staffing services, proudly announces that President and CEO Beth Garvey has been recognized as a leader and named to three significant industry (full story)
BG Staffing, Inc. Announces Transfer Listing of its
BusinessWire via COMTEX - Mon Nov 11, 08:55AM EST
BG Staffing, Inc. (NYSE American: BGSF), a growing national provider of professional temporary staffing services, today announced that it has chosen to transfer the listing of its common stock from the NYSE American to the New Yor(full story)
BG Staffing, Inc. Announces Q3 and Nine-Month 2019
BusinessWire via COMTEX - Tue Nov 05, 08:55AM EST
BG Staffing, Inc. (NYSE American: BGSF), a growing national provider of professional temporary staffing services, today reported record financial results for its third quarter and nine months ended September 29, 2019.(full story)
BG Staffing, Inc. Declares $0.30 Per Share Quarterly
PR Newswire via COMTEX - Tue Oct 29, 04:16PM EDT
BG Staffing, Inc. (NYSE American: BGSF), a growing national provider of professional temporary staffing services, today announced that its Board of Directors has declared a quarterly cash dividend of $0.30 per share of common stoc(full story)


HP Promoting Private Clouds With CloudStart - InternetNews.
For all the exuberance about the benefits of cloud computing, the logistical transition can be a real headache for businesses, often entailing unforeseen costs and delays.
With its new CloudStart product, HP is looking to ease the process, offering businesses a portfolio of software, hardware and consulting services that promises to set up a private cloud within 30 days. Datamation takes a look.
While there is a lot of interest in cloud computing for its potential cost savings and more flexible IT infrastructure advantages, enterprises don't necessarily know how transitioning to the cloud will cost and how long it could take.
On Monday, HP (NYSE: HPQ) announced CloudStart, a package of products and services designed to address those concerns by simplifying private cloud deployments.


Sankt Ingbert is 258 m above sea level and located at 49.28° N 7.12° E. Sankt Ingbert has a population of 38697. Local time in Sankt Ingbert is CEST.
Mostly dry. Warm (max 20°C on Fri afternoon, min 9°C on Fri morning). Wind will be generally light.
Mostly dry. Warm (max 21°C on Wed afternoon, min 8°C on Sun night). Wind will be generally light.
Light rain (total 6mm), mostly falling on Sat night. Warm (max 25°C on Fri afternoon, min 12°C on Wed night). Wind will be generally light.
* NOTE: not all weather stations near Sankt Ingbert update at the same time and we only show reports from the nearest stations that are deemed current. Weather reports submitted by any ship (SYNOP) that is close to Sankt Ingbert within an acceptable time window are also included.
11 km Mostly dry. Mostly dry. Light rain (total 7mm), mostly falling on Sat night.
16 km Mostly dry. Mostly dry. Light rain (total 5mm), mostly falling on Sat night.
19 km Mostly dry. Mostly dry. Light rain (total 7mm), mostly falling on Sat night.
19 km Mostly dry. Mostly dry. Light rain (total 4mm), mostly falling on Sat night.


The last time I wrote a blog it became a book. Well stay tuned for what ever it is I will write but in the meantime check out my book called "My Camino Dream" a fun and thoughtful account of my walk across Northern Spain on the Camino de Santiago. Available at Bookpoint in Dunoon (Signed copies) Amazon, Amazon Kindle, iBooks, LuLu.com and any other great book place.


We hope you can find what you need here. We always effort to show a picture with HD resolution or at least with perfect images. Extraordinary Spider Man Into The Verse Images SPIDER MAN INTO THE SPIDERVERSE Three Villains Revealed And Jake can be beneficial inspiration for those who seek an image according specific categories; you can find it in this site. Finally all pictures we have been displayed in this site will inspire you all..


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Dalit Mahila Vikas Mandal (DMVM) was formed in 1990 by Adv. Varsha Deshpande in Satara. As a first step, we conducted a survey to identify Women who had been deserted by their families in Satara city. Such Women were identified. We collectivised these women and met with the local Collector and demanded that such women be issued separate ration cards and also provided livelihood skills. The district administration issued ration cards to these women. The success of this campaign motivated us to conduct a survey of deserted women across Satara district. Around 5000 women who were deserted by their husbands/families were identified and registered. Self Help Groups (SHG) of these women were formed at the village level. The women were also provided certain vocational skills to make a living. Simultaneously, we initiated a "Zunka Bhakri Kendra" at the State Transport bus stand employing the most vulnerable women. The Zunka Bhakri Kendra has been functional ever since and helps deserted women make a living by cooking and supplying food to bus travellers. We realised that one of the main reasons for desertion of women was alcoholism of their husbands and widespread sale of illicit liquor. Through a series of campaigns and movements, we emphasised on the District Administration to close down illicit liquor shops & bars.
Self Help Groups of women that were constituted continue to function as credit societies and have effectively mobilised resources/finances through district cooperative banks for initiating small enterprises and for various other needs. DMVM is in the process of trying to federate these groups and initiate a milk cooperative society. As part of our work, we also initiated a counselling and free legal aid cell to counsel women survivors of violence. The cell has also been functional since 1990. In 2001, it got affiliated to the Maharashtra State legal resources authority and in 2007; we were designated as a service providing organisation under the PWDV Act 2005.
During our interactions with SHG women, we realised that the practice of sex selection was becoming rampant and several women were being forced to go in for sex determination and pre-birth elimination of female fetuses. This motivated us to begin work on the issue of the girl child in general and sex selection in particular.
We began undertaking various campaigns on the issue of sex selection and improving the value of the girl child.
We also worked on sensitising and creating awareness amongst a range of stakeholders on the issue of sex selection. These included women, youth, elected representatives, media etc. Simultaneously, in order to catch erring doctors, we initiated sting operations by taking decoy clients to doctors in the garb of having sex determination. So far, we have already conducted 47 sting operations all over Maharashtra.
We have also worked with the key implementing authorities – the appropriate authorities and advisory committees to improve implementation of PCPNDT Act.
Our Secretary, Adv Varsha Deshpande was and continues to be a member of various task forces under the PCPNDT Act like the Central Supervisory Board, The National inspection and monitoring committee etc. She is also a key trainer identified by UNFPA and the State Government for capacity building of various actors involved in the implementation of PCPNDT Act like judicial officers, prosecutors, Members of Advisory Committees, Appropriate Authorities etc.
In order to strengthen our work on PCPNDT Act implementation, we undertook an analysis of all cases where there had been an acquittal with support from Action Aid so as to help appropriate authorities plug these loopholes.
UNFPA supported us to build capacities of Village Health Nutrition and Sanitation Committee (VHNSC) members under the Government's flagship program Beti Bachao Beti Padhao. As part of this, we trained around 12500 VHNSC members in Beed. We also built capacities of Master trainers in nine other districts to, in turn, train VHNSC members to address issues of women's health, well-being and sex selection in their areas.
We also work extensively with adolescents and Youth on the issue of gender equality and sex selection because we believe that reaching out to this group can impact their entire life ahead and in turn impact overall development of the country.
Through our journey, we have filled various PIL's, appeared in interviews for cases under the PCPNDT Act. Currently, with support from UNFPA, we are actively working on a program to build the social, health and economic assets of adolescent girls by empowering them with information and skills so that they can fulfil their aspirations and make informed and responsible choices in decisions related to their health and well-being. This project is being undertaken in Shirur Kasar block of Beed district.
Made By Pratul R


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← Kate Tattersall, Victorian Adventuress Extraordinaire
Early Victorian Handguns; Part 1, a time of great change →
Kate Tattersall; a little bio
Posted on: 02 . 9 . 12 by R.S. Fleming
If you enjoy this website, and would like to see it remain open, please purchase Kate Tattersall Adventures in China.
Kate (Katelyn Elizabeth Beaufort) was born on the 11th of January 1834, her mother died a few days later. Her father was an earl, and she had five older brothers, but only two who survived infancy, and only one who survived childhood; the first-born, who was sixteen years her senior and therefore not any kind of a playmate. She was raised by a nanny, then a governess, and her father who treated her like a boy, spending most of her childhood in the Quantock Hills of Somerset. It seems to have been a somewhat lonely existence, her best friend a hound named Cinders, then a black retriever named Ebony. When Kate tried to join in games with lower-class children from the nearby village they often treated her unkindly, calling her names, pushing her into puddles, and generally excluding her from fair participation. Her education consisted of languages, geography, some natural sciences, classical history, and countless hours of committing poetry, quotes, and Bible verses to memory. She enjoyed drawing, playing piano, harp, and guitar. While wealthy people of the era all learned to ride, she went beyond most girls and actually straddled her horse and participated in wild steeplechase races. Still a tomboy at the age of twelve, but tall and graceful, she started receiving quite alarming attention from men. For a while she had a society tutor (decorum matron) who taught her a great deal, but also delivered some savage beatings. When she was fourteen her father remarried and Kate's step-mother spent a year teaching her to act as a proper aristocratic lady. She then started taking a greater interest in fashion, honed her skills in sewing and knitting, and designed outfits that were tailor made to her specifications by an elite and very expensive dress-maker.
A 1/9th plate daguerreotype, increased about four times.
Engaged, married and widowed all at sixteen, she had her daughter (Elizabeth Josephine) about a fortnight after turning seventeen. It was the untimely death of her husband which led to her becoming a dedicated operative in the British Secret Service. As was common at the time, she often left her infant daughter to the care of a nursemaid, then a nanny, then later with a governess.
We only have this image that we suspect is Kate. It was found with her diaries and other items. It is a very small 1/9th daguerreotype* (2×2.5", 5×6 cm) plate probably taken in the Summer of 1853 when she was nineteen. It is housed in a battered leather case and brass frame. By this time she would have no longer been in mourning, although some widows remained all in black longer, or only went into half mourning after two years. The photo was hand tinted but has faded; there is pink on her cheeks and the flower, and perhaps some slight blue colouring on her dress. Her wedding band is visible on her left hand, and she is wearing another ring on her right middle finger. She wrote of having long unruly black hair, so here it appears to be carefully oiled for control, the front tresses curled and looped back, and tied with the rest at the back of her head. Large bright eyes, fair complexion, a long straight nose, thin face and slender body are all words she used to describe herself.
When I first looked at this photo I didn't think much of it. We managed to scan and enlarge it so we could see her better. This is quite tricky with a daguerreotype because they are like mirrors in direct light. Dust often got trapped behind the glass and caused the speckling seen here. Unfortunately air and damp has also leaked in between the glass and frame. The pink tinting for her face may have removed some of the details. However, it is still a decent image, and looking at other photos from the era, and comparing them to Kate, we realized she must have been very attractive. At 5'6" (168 cm) she stood taller than most women of her times, in fact that was the height of the average English man in the mid 1800s, but there are records of many members of both sexes being six feet tall or taller. Naturally healthy with an agile athletic physique, wearing the finest of clothes, she certainly would have turned heads effortlessly as she strode confidently and gracefully through posh London neighbourhoods.
A fashion aficionado examined this image and suggested that Kate may not be wearing a corset, because her bosom would be flattened and pushed up higher. She probably has on some kind of simple stays, and there could be support (boning) built into the dress, that is tailored to fit tight on her midriff. The layers under her dress would include at least a chemise, stays or corset, and shirt bodice (chemisette). Women also wore little waistcoats to swathe their breasts, made of various materials, and known as camisoles, bosom friends, under vests, modesty wraps, or covers. While it's true that these undergarments did lessen the details of a bosom, it also added volume to a small-breasted girl's figure, which was a body image issue Kate wrote and worried about. (She may be wearing a corset with an under vest.) The lacy flared shirt sleeves which are visible, known as engageantes, were separate items worn with elastic above the elbows or tacked into the dress sleeves and removed for laundering. The sloping shoulders with dropped arm's eye (armscye), neat little collar, cut of the sleeves, and flat pleating are all typical of the late 1840s to the mid 1850s. Women of that era desired an appearance of hardly any shoulders, and this dress certainly achieves such an effect. Also typical of the early 1850s is the centre parting and side ringlets. Women wanted their waists to appear about as big around as their heads, but Kate isn't quite achieving that fashion trend. It was common for women to wear pads on the sides of their heads, hidden within their hair, then lace their corsets tight, and thereby produce an even balance in the width of their heads and waists.
In this pastel rendering of Kate by Mia Lane, based on the daguerreotype, we get an idea of what she may have looked like in the Spring of 1850, sixteen years old and newly wed. Her hair would have been tied at the back of her head, and a bit of eye paint and red lip salve was fashionable. Her adornments are conservative; large tear-drop pearl earrings and a cameo tied at her throat on a silk ribbon. During this era sects of some faiths believed any cosmetics or jewellery was sinful, and revealed a lack of modesty, but not generally amongst the peerage. It seems the wealthy gentry, the growing upper-middle-class, were far more prone to strict puritanical beliefs, and that women should be home-bound "guardians of the hearth" waiting to fulfil their husband's every whim. Kate certainly never fit such a description, her fondness for travel and adventure too great, but she did strive to be a devoted, caring, loving wife and mother.
*The daguerreotype process creates a direct positive image on a silver plated copper plate, producing a mirror effect and is unstable; it can easily be rubbed off and will oxidise in the air, so daguerreotypes are mounted in sealed cases with a glass cover. Our image of Kate has unfortunately degraded.
Kate Tattersall Adventures in China, Spring to Autumn 1849.
Available for purchase from these fine vendors:
Amazon.ca (Canada)
Amazon.co.jp (Japan)
Amazon.com (USA)
Amazon.co.uk (UK)
Amazon.de (Germany)
Amazon.fr (France)
Barnes & Noble Nook Edition (USA)
Chapters Indigo (Canada) and the Kobo Edition
Daum Books (Korea)
Fishpond (Australia)
Krisostomus (Estonia)
McNally Robinson (Canada)
Powell's Books (USA)
And book sellers near you. Look for this sensational penny dreadful styled cover.
Please consider purchasing the adventures from a local independent bookshop.
Congratulations on having one of the most sophisticated blogs I've come across in some time! Kate's story is very interesting.
Enid V
Hey there! I'm a 19th century English lit fan, and this reads fantastic! Will your books be available in the US?
03 . 2 . 13
R.S. Fleming
@ Enid V, the e books will be available everywhere, and the printed books will certainly be available through the mail, if not at your local bookshop.
I am really loving the theme/design of your site. I looked carefully at the photo. I think it has some yellow in the middle of the flower. Kate's build and pose looks like the famous photo of Emily Dickinson; both slender with really long necks.
@ Reggie. I think you're right about the bit of yellow on the silk(?) flower. It appears to be a button or ring, probably pinning the flower in place. Part of Kate's neck is hidden by her collar and the "sloped shoulder" cut of her bodice. I looked at the daguerreotype of Emily Dickinson and agree, they are quite similar. Emily's was taken in 1846 or 47, and is in very good condition. Thanks for your observation.
I like Kate as a heroine. You really make her come to life.
I wish there were sites like this for all my favourite novel characters. Thanks!


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Q: How to add mdframed in footer? I am working on fancyhdr in report generation. Currently I am using fancyhdr which produces one line and I can add left, center and right footers below to this line. But I need an mdframed as footer and need to add right, left and middle text inside it.
Below is sample mdframed which need to be added as footer.

Please help me out.

A: You can use something like the following:
\documentclass{article}
\usepackage[framemethod=tikz]{mdframed}
\usepackage{fancyhdr}
\usepackage{lipsum}

\pagestyle{fancy}
\fancyhead{}
\fancyfoot{}
\fancyfoot[C]{%
\begin{mdframed}[linecolor=blue!60,roundcorner=3pt]
\parbox[t]{0.333\textwidth}{\raggedright Text on the left}%
\parbox[t]{0.333\textwidth}{\centering Text on the center}%
\parbox[t]{0.333\textwidth}{\raggedleft Text on the right}
\end{mdframed}%
}

\begin{document}
\lipsum[1-12]
\end{document}

The idea is to place an mdframed environment centered in the footer; inside this environment, three \parboxes of equal length are used to place the footer contents. An image of the footer on the first page:

A: The tcolorbox package is another option to to produce rounded corner boxes, even in the footer:

\documentclass{article}
\usepackage{fancyhdr}% http://ctan.org/pkg/fancyhdr
\usepackage{lipsum}% http://ctan.org/pkg/lipsum
\usepackage{tcolorbox}% http://ctan.org/pkg/tcolorbox
\pagestyle{fancy}
  \fancyhf{}% Clear headers/footers
  \fancyfoot[C]{%
    \begin{tcolorbox}[width=\linewidth]
      \makebox[0pt][l]{Text on the left}\hfill%
      \makebox[0pt][c]{Text on the center}\hfill%
      \makebox[0pt][r]{Text on the right}%
    \end{tcolorbox}%
}
\begin{document}
\lipsum[1-12]
\end{document}


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Home / Dr. Bill Freeman, Director & Chair of the Master of Public Health -The Chicago School of Professional Psychology
Dr. Bill Freeman, Director & Chair of the Master of Public Health -The Chicago School of Professional Psychology
Dr. Bill Freeman, Program Director & Chair of the Master of Public Health program at The Chicago School of Professional Psychology joins us today to discuss public health education.
#1 Can you tell us about the M.P.H Programs Offered Online and Onground at The Chicago School?
Built upon The Chicago School's 36-year history of practitioner-focused learning, our Master of Public Health (MPH) is designed for working adults passionate about making a dramatic impact on the health and wellness of others, particularly those representing marginalized and underserved populations.
Our 21st Century curriculum embraces the evolving U.S. healthcare landscape, which has seen dramatic change following the implementation of The Patient Protection and Affordable Care Act, while developing a global mindset to respond to the challenges of a highly interconnected world.
The entire focus of the program is career-facing, preparing graduates to thrive in a dramatically changing public health and healthcare marketplace.
Our rigorous curriculum integrates theory, scientific research, professional practice and innovation – all framed by career-focused community engagement, offering the knowledge and skills drawn from a variety of disciplines.
The M.P.H. is a 42-credit program consisting of 27 credits of core courses; four practical concentrations; engaged fieldwork; and a practical capstone project.
Our commitment is to graduate true agents of change. Through coursework, concentrations and field experiences, students are empowered with the competencies required to meaningfully contribute to local public health needs while remaining focused on our ever-present responsibility as global citizens.
Substantial public health challenges at the national and global level await our students as they prepare to bring both head and heart to a world in deep need. With our MPH program, they will be equal to these challenges as The Chicago School partners with them for every step of their academic journey.
#2 How long does a typical M.P.H. Program take at The Chicago School? What is the maximum and minimum time of completion?
Whether online or onground, our M.P.H. Program has been designed for the working adult. The average time to completion for our online program is 27 months with students taking one, eight-week course consecutively. The average time to completion for the on-ground program is about 27 months with students taking two 15-week courses simultaneously during the Fall, Spring, and Summer terms.
There is no minimum time to completion; ambitious students, working with their advisor, can complete their program sooner than 27 months. Maximum time to graduation is 5 years.
#3 What do you think makes The Chicago School's M.P.H. stand out from other online and on ground MPH programs?
Based on our long-standing experience of training outstanding health practitioners, our M.P.H. Program s designed to prepare engaged public health and healthcare professionals with both the head and heart to respond to the needs of a dramatically changing healthcare environment.
From our core courses and engaged concentrations, to our domestic and international fieldwork culminating in an applied research project, our M.P.H. is a promise to graduate community-based change agents with the skills and experience required to succeed in the dynamic multicultural, stakeholder-diverse health marketplace.
International Practicum: As part of our steadfast commitment to prepare globally responsible and locally responsive leaders, all students participate in a 10-day international field experience examining the unique and common health challenges faced by a diverse, yet connected world.
Career Concentrations: Following the completion of core courses, students select one of four concentrations geared toward in-demand public health and health-related employment: Mental & Behavioral Aspects of Public Health; Public Policy Development & Advocacy; Health Informatics: and Senior Services Administration. A number of our concentrations involve 4-day residence intensives with practitioner thought leaders.
Each concentration includes three courses, followed by a 15-week related field experience, all of which culminates in the development of a practical applied research project based on each student's area of interest.
#4 How important would you say accreditation is when choosing an online or on-ground M.P.H. Program?
The Chicago School of Professional Psychology is regionally accredited by the WASC Senior College and University Commission (WSCUC). The last review in 2011 resulted in an accreditation term of five years (2016).
Our M.P.H. Program has been designed based on the highest national standards of the Association of School and Programs of Public Health and the Council on Education for Public Health (CEPH).
#5 How does The Chicago School ensure that the quality of its M.P.H. Program, whether delivered online or onground, meets the needs of a dramatically changing public health and healthcare marketplace?
We are not the traditional M.P.H. Program. Our program has been completely redesigned to respond to the realities of a dramatically changing public health and healthcare marketplace. Based on these new realities, our program is career-facing, competency-focused and concentration-rich.
We have developed an integrated, high-quality program, whether delivered online or on ground.
#6 What are the advantages to earning a M.P.H. degree in general?
The M.P.H. is the doorway into the exploding public health and healthcare job market. According to the U.S. Bureau of Labor Statistics, U.S. Department of Labor, Occupational Outlook Handbook, 2014-15 Edition, the nation is projected to add 250,000 public health jobs and grow by 37% over the next five years. Our graduates are prepared to deliver outstanding professional services, excel as community leaders with the skill-sets to respectfully engage as collaborative partners in multi-cultural and stakeholder-diverse local and international settings.
Our graduates will be fully prepared to pursue careers in a range of public and private settings including: Government agencies—local, state or federal health departments; healthcare provider organizations (hospitals, clinics, ambulatory-care centers); health insurance companies; pharmaceutical companies; corporate wellness centers; community-based organizations; advocacy organizations and many others.
The M.P.H. is a "degree with legs" and our program is uniquely designed to prepared gradates with the skills and experiences they need to thrive in the public health and healthcare world of today and tomorrow.
#7 Does The Chicago School offer job placement for students who graduate in public health?
Yes, but we also do much, much more. For us, job placement isn't a near-to-graduation afterthought.
Our entire program is career focused, ideal for the currently employed health or healthcare worker needing a graduate degree for career advancement or those not currently employed in the health marketplace and looking for a degree with the flexibility to enter the public or private sector job market.
From your first course through the completion of your program, our focus is on employment. All of our faculty are healthcare practitioners both global and domestic experience who bring that real-world perspective essential to job success.
We have relationships with hundreds of domestic and international public and private public health and service providers including established relationships with 22 countries. Our domestic and international field placements and practicum are second-to-none offering students the rounded education experience and skills demanded by an evolving workplace.
With laser focus, we work with students to prepare for and secure the job that best aligns to their passion, skills and interests as committed agents of change.
#8 What type of financial aid packages are available for students in public health? Are there any fellowships, grants and scholarships available?
The Chicago School offers need -and merit-based scholarships. Details are available on our Admissions website. We also offer a professional tuition rate for those employed in mental or behavioral health professions, which is valued at approximately 10% off our standard tuition costs. A special tuition rate is also available for individuals who work in law enforcement. Additionally, students who qualify for veteran benefits may use them at The Chicago School, and we offer a limited number of Yellow Ribbon scholarship awards. Lastly, we have limited scholarship offerings for international students. For more information, individuals can call (800) 721-8072.
#9 Do you have any advice for students enrolling in an M.P.H. Program, whether online or on ground?
Ask yourself, "What is my passion? What brings meaning and purpose to my life? Where do I want to take a stand?" And based on my passion, which program will best allow me to ensure that it's realized?
For those with an interest in research and science, there are great programs at other schools. We aren't that program.
But for those passionate about becoming true agents of change, working mindfully in a post-Affordable Care Act world in communities to make lives better, our program is the perfect match.
Our passion – reflected in our rich history of training engaged practitioners – is preparing individuals committed to work collaboratively and respectfully with diverse communities with both a local and a global lens to improve the health and well-being of others.
#10 Why would I want to get an M.P.H. from a psychology school?
The Chicago School of Professional Psychology was part of an activist movement in the 1970s to improve the training of psychologists with a goal to produce highly effective, community-focused, multi-cultural healers. Thirty-six years later, we are recognized as a leader in training mental health professionals across the U.S. and internationally.
Over the past five years, our mission has expanded to preparing effective leaders in health and wellness. It's a natural progression.
Our M.P.H. Program stands on the shoulders of our rich heritage with a solid commitment to prepare public heath and healthcare leaders to work as effective community change agents amide a dramatically changing health care environment. We are the M.P.H. for the 21st Century.
For more information on the M.P.H. Program offered at The Chicago School, visit www.TheChicagoSchool.edu/MPH.
Thank you Dr. Freeman for sharing and participating in this piece.


text:
Waiouru is a small town in the centre of the North Island of New Zealand. It is located on the North Island Volcanic Plateau at a height of 815 metres above sea level, 25 kilometres to the southeast of Mount Ruapehu.
North of Waiouru is the section of State Highway 1 called the Desert Road. This runs for 35 km through the Rangipo Desert to Turangi, at the southern end of Lake Taupo. Waiouru is a military town that has grown up in conjuction with the New Zealand Army Training Group, which is responsible for the training of recruits and other soldiers. The Desert Road immediately north of Waiouru runs through the 868.18 km2 army training area, which lies mainly to the east of the road.
The main attraction of Waiouru is the Queen Elizabeth II Army Memorial Museum, which features static displays of New Zealand's military heritage. The rest of the township consists of a small cluster of hotels, tearooms and service stations along the highway.
Seven kilometres to the west of Waiouru is the small settlement of Tangiwai, which is the site of New Zealand's worst railway disaster. On December 24, 1953 the overnight express between Wellington and Auckland passed over the Tangiwai Railway Bridge. The bridge, which had just minutes earlier been weakened by a lahar from Mount Ruapehu, collapsed, sending the train into the Whangaehu River, killing 151 people.
1.1 The sheep years
1.2 The military camp
The sheep years
Merino sheep had a big part to play in the siting of an Army training camp at Waiouru.
In 1855, missionary Tom Grace brought merinos from Taupo to graze on the tussock lands in the Waiouru area. The flock was eaten by Te Kooti's warriors in the early 1870s, and 4000 more merinos were brought over the mountains from Hawke's Bay.
By the 1890s there were 40,000 merinos on the tussock lands between Karioi bush and the Kaimanawa Ranges, and pack-tracks were formed to get the hundreds of tons of wool to Napier (The Gentle Annie track), and later to Lake Taupo (The Desert Road) or down to Wanganui (Hales' Track and Field's Track). These tracks were later developed into roads for wool wagons. By 1897 there was a coaching house at Waiouru for mail-coach passengers on the Napier-Taupo run.
The North Island Main Trunk Railway came through in 1907 but not much wool was sent by rail as overgrazing by the sheep at this time had led to a plague of rabbits, and by the 1930s no sheep at all could be grazed on Waiouru sheep station.
The military camp
When the Government needed a training area in the North Island for its Territorial Forces in the 1930s, Waiouru sheep station was thus ideal, with vast areas of cheap open land, and also ready road or rail access to all the North Island coastline.
Artillerymen were first soldiers to use Waiouru. In 1937 Waiouru farmhand, Cedric Arthur, wrote:
The Military (artillery) Camp is here again for its annual big shoot, so Waiouru is exceedingly busy with huge lorries, tractors, guns and horses, not to mention soldiers galore.... It has been rumoured around here that the Minister of Defence has bought 15 miles of Waiouru to make a permanent Camp here. (Arthur 1984)
The rumour was correct. A month after war was declared in 1939, the majority of the leasehold Waiouru run was taken back by the Crown.
At the beginning of winter 1940, eight hundred construction workers from the Ministry of Works Work started building a camp at Waiouru for training 7000 Territorals at a time.
Arthur, P.M. (1984). Waiouru, Land of the Tussock, 1935-40.
Moss, G.R. (1956).The Waiouru Tussock Lands, in "New Zealand Journal of Agriculture", 16 July 1956.
Retrieved from "http://clipart.academickids.com/encyclopedia/index.php/Waiouru"
Categories: Cities and towns in New Zealand | Central North Island, New Zealand


text:
НЧ/ВЧ (Музыкально-художественное любительское объединение «Низкие частоты / высокие частоты») (или иначе Клуб «НЧ/ВЧ», иногда «НЧ-ВЧ») — клуб художников, рок-музыкантов, кинематографистов, театральных актеров и режиссёров и писателей, созданный в Санкт-Петербурге осенью 1986 по инициативе Олега Михайловича Сумарокова (также известного как «Папа ОМ»).

Клуб берёт своё название от хеви-метал группы «НЧ/ВЧ», в которой играл сын Папы ОМа Алексей, а также принимал участие лидер «Автоматических удовлетворителей» Свин.

В разное время клуб располагался по различным адресам:
 1986—1988 — сквот в проходном дворе между домами по Чайковского, 20 и Каляева, 5.
 1988—1990 — ул. Каляева, дома 29 и 31.
 c 1990 — «Египетский дом» на Каляева, 23 (с 1991 улица вновь становится Захарьевской).

Клуб официально зарегистрирован Управлением культуры 10 июля 1987. Деятельность клуба продолжалась до середины 90-х, после чего постепенно сошла на нет. Архивы клуба переданы в Российскую национальную библиотеку, а также в Библиотеку ПАиБНИ Арт-центра «Пушкинская, 10».

Деятельность

Рок-клуб
На заре существования клуб выступал в качестве пристанища для музыкальных коллективов, не ставших ещё членами ленинградского Рок-клуба. В разные годы здесь выступают «НЧ/ВЧ», «Аукцыон», «Трубный зов», «Время любить», «Луна», «Младшие братья», «Автоматические удовлетворители», «Wine», «Юго-запад», «Выход», «Ноль», Гарик Сукачёв

На базе клуба возник проект Олега Сумарокова «Преображение», в записи которого участвовал Николай Рубанов и другие участники из групп «АукцЫон», «Время любить», «Маньяки» и «Ноль». Единственный альбом проекта вышел в виниле в Продюсерском центре Представительства Евангелическо-лютеранских приходов России Андрея Тропилло.

Прочая деятельность
В клубе функционировали кино- и фото- студии, галерея и Музей творческих содружеств, выпускались самиздатские журналы («Свет», «Рок-Революция», «Психоделическая Революция»). В 1990—1991 на базе редакции журнала «Рок-Революция» проходили регулярные литературные чтения, в которых принимали участие поэты и писатели мистического реализма и фэнтези. В одном из чтений принимал участие писатель Владимир Сорокин. Одно время в клубе жил Орден Алхимиков из Прибалтики. Одним из наиболее значимых событий была проведённая в 1988 по инициативе Клуба друзей Маяковского выставка, посвящённая 95-летию со дня рождения Владимира Владимировича Маяковского.

В деятельности клуба участвуют митёк Олег Григорьев, некрореалисты Олег Котельников и Евгений Юфит, художник-нонконформист Борис Кошелохов, основатель Новой Академии Изящных Искусств Тимур Новиков.

Деятельность художников близких к клубу нашла своё отражение в культовом фильме 80-х «Асса»: картины «Новых художников» висят на стенах квартиры Бананана, роль которого исполняет председатель Клуба друзей Маяковского Сергей Бугаев, а в одном из эпизодов в качестве участника группы «Кино» появляется Тимур Новиков, художник, открывший в 1980 галерею «АССА».

Ссылки
 «НЧ/ВЧ» в Энциклопедии «Санкт-Петербург»
 Газета «Смена», N74, 22.04.1994. «ПАПА ОМ преобразился.»
 Из истории сквотов и сквотерского движения.

Примечания

Творческие объединения Санкт-Петербурга
Творческие объединения писателей
Творческие объединения кинематографистов

redpajama_set_name: RedPajamaWikipedia


Conjugate heat transfer refers to the coupled analysis of the thermal interactions between fluids and solids. Earlier methods relied on an empirical constant, the heat transfer coefficient, which lumps together all the unknown information regarding the heat transfer process. Conjugation consists of solving the temperature and heat flux distributions at the fluid-solid interfaces as a coupled problem, without assuming a heat transfer coefficient. The purpose of this thesis is to implement a partitioned approach to perform conjugate heat transfer analysis, where separate fluid and solid solvers operate on their own domains, and the interface values are exchanged and solved for in an iterative way. The coupling is done with the multiphysics coupling library preCICE. The tasks of this thesis mainly involve the implementation of the adapter codes, which are in charge of steering the respective fluid and solid solvers, and exchanging coupling data by calls to the preCICE library. The implementation will then be validated and an application will be presented.
This page was last modified on 11 July 2016, at 14:12.


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Few things let digital publishers address their users more effectively than a well-made video. Whether it's to promote a new app or address a community, videos pack lots of information into digestible, user-friendly chunks that get noticed. Though they can be more expensive than static ads to produce, video campaigns can be among the highest ROI projects any team undertakes, made more so by the possibilities available to modern digital marketing teams. With the recent release of Upsight's video campaign tools, we thought we'd share a few creative ways for publishers to use in-app video to engage their users.
This week we're shipping two new improvements to our marketing tools that improve efficiency for digital marketers and streamline the milestone management process.
We're always looking for ways to help our partners get more done in a day. To that effect, we're rolling out three new time-saving features for anyone using Upsight to track their analytics, deliver push notifications, or manage their app settings.
The digital world runs on video. Modern users expect premium communications wherever possible and they won't waste time or attention on anything less. That's why we're proud to announce that Upsight customers can now leverage videos in their in-app marketing.
With the end of summer in sight, we're rolling out a few helpful product updates that will make it even easier to parse your data and customize visualizations to suit your team's needs. Here's what we've been up to.


Do your team have a plethora of good ideas but struggle to make themselves heard in the context of a meeting? Having your ideas ignored or misunderstood can be frustrating. If this is the case, there are practical ways your team members can each make their own personal impact.
By developing the correct approach to making a point, your team can completely transform the way they are perceived. After all many people have good ideas but when energy and eagerness are at peak, ideas are vulnerable to being overlooked or being misinterpreted.
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By the end of our How to Get Heard in Meetings workshop, you will be able to communicate with confidence and understand how different vocal techniques and body language changes how you're received.
Communicate your ideas: Speak confidently and manage interruptions.
This workshop will be tailored to suit your business objectives with your team in mind. At City Academy, all our workshops make use of practical exercises relevant to the industry and individual taking part in the workshop. Throughout and at the end of your training, you will be provided with extensive feedback on your work to ensure you can continue developing your skills.


husband for Christmas this year?
-A house! A house with a big yard so he could build a huge shed where we can store all of our moon bounces and all the other equipment. (This way, we wouldn't have to rent out storage space for the company.) Of course the house would have a mancave!
-A week long honeymoon to an island or a cruise... doesn't matter. Just to get away!
-A boat to go fishing on with his man friends.


Oct 13, 1976 - Pfizer Inc.
Functional protein is prepared by heat denaturing impure natural protein selected from whey, microbial and vegetable protein and subjecting the separated denatured protein to enzymatic proteolysis for a period of up to 30 minutes at 20 to 65.degree. C using at least a designated minimum amount of enzyme. Because of its high degree of functionality and its lack of bitter taste, the modified protein has a wide application in food compositions, primarily as a replacement for nonfat dry milk, sodium caseinate, gelatin and egg albumin.
This invention relates to proteins. More specifically, it relates to the modification of natural proteins to improve their functionality and thereby enhance their utility in food compositions.
Nutritional value is a primary concern in the world's quest for new sources of protein, but consideration must also be given to the protein's functional and flavor characteristics. For while nutritionally balanced foods may be prepared from a wide variety of sources, acceptability of such foods depends upon their sensory properties such as taste and texture. A protein substituted for traditional proteins should therefore maintain or improve the quality and acceptability of the food products in which it is incorporated. This requires that the new protein not only possess satisfactory nutritional properties, but also acceptable flavor, color and additional functional properties, such as solubility, thermal stability, emulsifying, foaming and texturizing characteristics.
At the same time, the food industry is seeking less expensive proteins for use in the preparation of modern convenience foods. In such uses, the protein often must have specific functional characteristics. For example, the protein in a coffee whitener should not precipitate when added to the coffee and a protein for use in carbonated beverages must be acid soluble.
It is therefore a primary objective of the present invention to provide a simple and inexpensive method of preparing functional protein for use in a wide variety of food compositions.
1. Direct enzymatic proteolysis of natural proteins such as taught in U.S. Pat. Nos. 2,489,208 and 3,889,001. This approach normally uses low levels of enzyme for extended reaction times. Yield of soluble functional protein from such processes is usually low and the product generally has poor flavor.
2. Enzymatic treatment of natural protein which has initially been subjected to high shear to modify the protein structure. As exemplified in U.S. Pat. No. 3,694,221, proteolysis of the pretreated protein is accomplished with high levels of enzyme for short reaction times and purportedly gives an easily wettable and dispersable product with good mouthfeel.
3. Enzymatic treatment of heat-treated protein such as disclosed in U.S. Pat. Nos. 3,857,966 and 3,876,806. In U.S. Pat. No. 3,857,966, heat-precipitated and separated protein is initially subjected to alkaline hydrolysis at elevated temperature and then to a sequential proteolytic hydrolysis which utilizes both microbial alkaline and neutral protease plus plant protease over a period of about two hours. U.S. Pat. No. 3,876,806 discloses a process in which an aqueous slurry of defatted vegetable seed protein is initially heat treated to destroy vegetative cells and then subjected to enzymatic proteolysis to produce soluble protein. Separation of water insolubles is made after rather than prior to the proteolysis, and the product therefore contains not only soluble protein but also water-soluble impurities present in the protein source material.
150 Pepsin Units where said enzyme is an animal protease.
In preferred aspects of the invention, the functional protein is derived from whey or from a yeast selected from the group consisting of S. cerevisiae, S. fragilis and C. utilis, and the proteolytic enzyme is derived from B. subtilis or B. licheniformis.
The functional protein of this invention finds wide use in food compositions since it can either supplement a composition or effectively replace a substantial portion of the conventional protein content of the composition, particularly nonfat dry milk, sodium caseinate, gelatin and egg albumin.
The instant process provides a simple and inexpensive means of separating the protein of many natural protein sources from water-soluble constituents and in turn converting the separated protein into a water-soluble form with a high degree of functionality. The elaborate and costly isolation and purification techniques previously used to extract the soluble protein content of these sources are thus avoided, and a protein with improved acid solubility and heat stability is obtained in higher yields than from such techniques.
A number of methods are available to assess the functionality of a given protein intended for food use. Included are those based on solubility, emulsification, foaming, viscosity and gelation properties. The protein of the instant invention is evaluated on the basis of its suitability for use in a coffee whitener formulation. Such use not only gives an indication of the heat stability of a protein under harsh conditions but also relfects its solublity, acid stability, viscosity and emulsification characteristics. The term "functional protein" as used herein is meant to include those proteins which, when incorporated in the test formulation of Example 16 described hereinafter, produces a coffee whitener which shows no feathering (precipitation or coagulation of protein) and a fat separation no greater than that from the control formulation when added to hot coffee as described in that example. In addition, the functional protein has a bland taste with no objectional bitterness or saltiness.
Sources of the functional protein include whey, microbial protein and vegetable protein. By "whey" is meant cheese whey, the watery part of milk that is separated from the curd in the process of making cheese. The whey may be either sweet whey or acid whey and in the form of fresh whey, condensed whey or whey solids. While the present process is particularly applicable to these impure forms of whey protein, partially purified whey such as the concentrates from ultrafiltration (UF), reverse osmosis, electrodialysis or gel filtration may also be used.
The source of microbial protein may be yeast, bacteria or fungi. Preferred yeasts include those of the genera Saccharomyces, Candida, Hansenula and Pichia, especially those of the species S. cerevisiae, S. fragilis and C. utilis. Preferred genera of bacteria are Pseudomonas, Lactobacillus, Streptococcus, Micrococcus, Cellulomonas, Arthrobacter, Bacillus, Hydrogenomonas and Aerobacter, especially those of the species P. methylotropha, L. bulgaricus and S. lactis. Preferred fungi are those of the genera Trichoderma, Fusarium, Penicillium, Aspergillus, Neurospora and Endomycopsis, especially those of the species T. viride, F. solani and A. oryzae. The microbial cells are initially ruptured and the cell protein content separated from the cell debris by conventional techniques prior to processing.
Suitable vegetable protein sources include, for example, soybeans, wheat gluten, cottonseeds, okra, corn gluten, peanuts, potatoes, alfalfa, oats, rice, rapeseeds, sesame seeds and sunflower seeds. Preferred sources are soybeans, wheat gluten and cottonseeds. Especially preferred is soybeans in such forms as soy grits, solvent-extracted soybean flakes, soy flour, alcohol-treated soy flakes, soy concentrate and soy whey. The protein source is usually slurried in water, any undissolved material is separated, and the liquid phase is introduced into the process. Vegetable protein whey, like cheese whey, may be processed directly.
The introductory stream of impure protein in aqueous medium is normally a solution, but may also be a suspension provided a hazy to clear solution results from the subsequent proteolytic hydrolysis step described hereinafter. This stream is adjusted to a desired pH, heated to a temperature of from about 40.degree. to 150.degree. C and held at that temperature until substantial precipitation of denatured protein occurs. By "substantial" is meant at least 50 percent of the ultimate protein precipitation possible at the temperature and pH employed. The protein content of the crude protein is normally about 1 to 60 weight percent on a dry basis while the level of the crude protein in the introductory stream is conveniently from about 1 to 25 weight percent. While the pH during this step is not critical, the precipitation is customarily conducted at a pH of from about 0.5 to 9. Much above pH 9 or below pH 0.5, excessive degradation of the protein may occur. Preferably the precipitation is conducted at about the isoelectric pH of the protein to maximize its recovery. This pH varies with the protein source and is normally from about 4 to 7. The indicated temperature normally results in substantial precipitation in 1 second to 60 minutes. At temperatures much below 40.degree. C, the rate of precipitation is too slow to be practical. At temperatures much above 150.degree. C, the protein may develop off flavor. Preferably the temperature is between about 70.degree. and 95.degree. C, where substantial precipitation occurs in from about two seconds to 10 minutes.
The precipitated heat-denatured protein is separated from the aqueous medium by any convenient method such as filtration or centrifugation, the latter being preferred. The separated precipitate is preferably washed with water to minimize the watersoluble impurities in the precipitate. These impurities include, for example, lactose and salt in the case of whey protein and ribonucleic acid in the case of microbial protein. The separated precipitate may also be washed with a water-soluble food grade alcohol such as ethanol prior to the water wash, if desired. The wet heat-denatured protein solids can be dried by conventional means, if desired, or may be used directly in the next step of the process.
The heat-denatured protein is slurried in aqueous medium and converted to functional protein with proteolytic enzyme. Any acid, neutral or alkaline protease of microbial, plant or animal origin is suitable. Preferred are microbial proteases of bacterial origin such as those derived from B. subtilis and B. licheniformis and those of fungal origin such as those derived from A. oryzae, A. flavus, A. niger and S. griseus; plant proteases such as papain, ficin and bromelain; and animal proteases such as pepsin, trypsin, chymotrysin and rennin. Particularly suitable are those proteases derived from B. licheniformis and B. subtilis. Combinations of such proteases or proteases with peptidases may also be used. The sole requirement is that the protease be present in sufficient amount to insure conversion of the denatured protein to functional protein within 30 minutes without creating objectionable bitterness in the final protein product.
150 to 750 Pepsin Units for animal protease.
The units used herein to express the activity of the above classes or proteases are well known to the art and are clearly defined in such references as the First Supplement to the Food Chemical Codex, second Edition, 1974.
The concentration of the denatured protein in the aqueous slurry is not critical and is normally from about 1 to 20 weight percent on a dry basis. The temperature and the pH of the hydrolysis will depend upon the nature of the protein hydrolyzed and the proteolytic enzyme employed, and are selected to optimize the conversion of the denatured protein to functional protein. Convenient temperatures range from about 20.degree. to 65.degree. C. Much below 20.degree. C, the hydrolysis proceeds at a rather slow rate, while at temperatures much above 65.degree. C, the enzyme may be deactivated. The optimum temperature is normally about 50.degree. C.
At the completion of the reaction, the resulting hazy to clear functional protein solution is treated for enzyme deactivation. The method of treatment will depend upon the nature of the enzyme, but the deactivation is usually accomplished by heating the reaction solution to from about 80.degree. to 100.degree. C for from about 1 to 20 minutes. Depending upon the enzyme employed, such treatment may be accompanied by pH adjustment.
The functional protein solution following enzyme deactivation is normally cooled to about room temperature, adjusted to pH 6 to 8 and then either used directly in food compositions or dried by conventional means such as spray or freeze drying prior to such use. By "food composition" is meant a composition ingested by animals including humans to satisfy hunger or thirst. Suitable food compositions are those which comprise the functional protein of the process of the instant invention and at least one member selected from the group consisting of carbohydrate, fat, a second souce of protein other than the functional protein, vitamins and minerals.
Functional proteins prepared by the process of the instant invention are useful in such a broad range of food compositions because of their lack of bitterness and their excellent functionality, including solubility over a wide pH range, heat stability, low viscosity in solution, and excellent dispersability, aerating, emulsifying and texturizing properties. While these proteins are suitable as nutritional supplements, where they may be the sole source of protein in a food composition, their principal use is as a replacement for a substantial portion (at least 20 percent by weight) of many of the more costly soluble proteins traditionally used in foods, particularly nonfat dry milk, sodium caseinate, egg albumin and gelatin. In many cases, as shown in the examples, such replacement results in a superior food product.
Thus, we find the functional protein, because of its acid solubility, readily suitable for use in acid food compositions such as carbonated and acidic noncarbonated beverages where traditional proteins cannot be used. The functional protein can replace up to twice its weight of nonfat dry milk in many food compositions including baked goods such as yeast-leavened bread, confections such as frostings and milk nougat, desserts such as puddings and ice cream, instant breakfast foods, processed meats such as meatloaf, dressings such as salad dressing and mayonnaise, and fermented milk products such as yogurt. Sodium caseinate is totally replaced in such food compositions as coffee whiteners, nondairy products such as cream cheese, nondairy processed cheese and nondairy cheese spreads, whipped toppings and sour cream as well as in both milk and citrus type instant breakfasts and in processed meat products. Gelatin may be wholly replaced in such food compositions as instant frozen pudding and bakers marshmallow, while egg albumin is partially to totally replaced in such products as meringues, confections such as soft-centered candies, angel food cake, textured vegetable protein, pasta and noodles. The functional protein can also replace combinations of natural proteins, for example, nonfat dry milk and egg albumin in chemically leavened baked goods such as cakes; nonfat dry milk and egg yolks in salad dressings; nonfat dry milk, egg solids and soy protein in snack foods such as batter-coated onion rings; egg albumin and soy protein in high protein breakfast foods; gelatin and Hyfoama.sup.(1) in bakers marshmallow; and gelatin and soy protein in lemon chiffon.
The following examples merely illustrate the process of the present invention and the use of the functional protein product of the invention in food compositions, and are not to be construed as limiting the invention, the scope of which is defined by the appended claims.
A sample of fresh sweet cheese whey (94.6 liters) was adjusted to pH 5.0, heated to 90.degree. C and held at that temperature for five minutes. The resulting slurry was cooled to room temperature and centrifuged. The centrifuge cake was washed with water to yield 1415 g of wet heat-denatured whey protein solids (436 g dry).
A portion (32.7 g) of the wet heat-denatured whey protein solids (10.1 g dry) was dispersed in 100 ml water. The slurry was adjusted to pH 8.5 and 50.degree. C, 20 mg of Alcalase.sup.(1) S-6 (2970 Delf Units/g protein) was added, and the mixture was stirred at 50.degree. C and pH 8.5 for 30 minutes, the pH being maintained by the addition of 1 N NaOH. The resulting solution was heated to 80.degree. C for two minutes to deactivate the added enzyme. The solution was then cooled to room temperature, adjusted to pH 7.0 with 1 N HCl and freeze dried. The dry product passed the protein functionality test and had acceptable taste with no objectionable bitterness or saltiness.
(1) registered trademark for microbial alkaline protease derived from B. licheniformis supplied by Novo Enzyme Corp., Mamaroneck, N.Y.
The fresh whey may also be adjusted to pH 4.0 and 40.degree. C, or to pH 7.0 and 150.degree. C, pH 0.5 and 100.degree. C or pH 9.0 and 120.degree. C, and held for an appropriate time to substantially precipitate the whey protein solids.
Proteolysis of the heat-denatured whey protein solids may also be run at 20.degree. C or at 65.degree. C, using 2300 Delf Units or more of Alcalase S-6 per gram of dry protein to insure solution of the protein within 30 minutes.
A sample of UF whey concentrate (600 g; 40 weight percent solids) .sup.(1) was diluted to 2400 g with water, adjusted to pH 4.8, heated to 90.degree. C and held at that temperature for two minutes. The resulting slurry was cooled to room temperature and centrifuged. The centrifuge cake was washed with water and freeze dried to yield 112.5 g heat-denatured whey protein solids.
(1) Crowley Cheese Company, Binghamton, N.Y.
A portion (10 g) of the heat-denatured whey protein solids was dispersed in 90 ml water. The slurry was adjusted to pH 9.5 and 50.degree. C, 25 mg Alcalase S-6 (3750 Delf Units/g protein) was added, and the mixture was stirred at 50.degree. C for 15 minutes, the pH being maintained by the addition of 1 N NaOH. The resulting solution was heated to 80.degree. C for two minutes to deactivate the added enzyme and the solution was then cooled to room temperature, adjusted to pH 7.0 with 1 N HCl and freeze dried. The dry product passed the protein functionality test and had acceptable taste with no objectionable bitterness or saltiness.
Use of 7.5 mg Alcalase S-6 (11,250 Delf units)/g protein in the above enzyme treatment likewise resulted in a functional protein with acceptable tase. A comparable product was also obtained when the above process was followed with the exception that the centrifuge cake from the heat precipitation step was washed initially with ethanol and then with water, and the enzyme treatment was with 5.0 mg (7500 Delf Units)/g protein.
The enzyme treatment of Example 2 was repeated on a second l0 g portion of the same heat-denatured whey protein solids but with 15 mg Alcalase S-6 (2250 Delf Units/g protein), running the treatment until the takeup of 1 N NaOH was equal to that when 25 mg Alcalase S-6 was used. This required 36 minutes. The dry product did not pass the protein functionality test and had inferior taste with slightly objectionable bitterness.
The resulting freeze dried product from each of the runs passed the protein functionality test and had good taste with no objectional bitterness or saltiness.
S. cerevisiae yeast cells (800 g wet, 172 g dry) were dispersed in 1000 ml water and the pH of the slurry was adjusted to 9.5 by the addition of 1 N NaOH. The cells were homogenized at 9000 psi (633 kg/cm.sup.2) and 30.degree. C for 80 minutes. The resulting mixture was centrifuged and the supernatant liquor decanted. The residual solids were repulped in 1000 ml water and recentrifuged. The supernatant liquors were combined, adjusted to pH 6.0, heated to 70.degree. C and held at that temperature for 1 minute. The resulting slurry was centrifuged and the centrifuge cake was washed with water to yield 392 g wet heat-denatured yeast protein solids (72 g dry).
A portion (50 g) of the wet heat-denatured yeast protein solids (9.2 g dry) was dispersed in 200 ml water. The slurry was adjusted to pH 8.5 and 50.degree. C, 100 mg subtilsin (16,300 Delf Units/g protein) was added and the mixture was stirred at 50.degree. C and pH 8.5 for 30 minutes, the pH being maintained by the addition of 1 N NaOH. The resulting solution was heated to 80.degree. C for 5 minutes to deactivate the added enzyme, and the solution was then cooled to room temperature, adjusted to pH 7.0 with 1 N HCl and freeze dried. The product passed the protein functionality test and had acceptable taste with no objectional bitterness or saltiness.
The hydrolysis may be repeated using fungal protease.sup.(1) at a level of 240 HUT/g protein at 50.degree. C and pH 5.0 for 30 minutes to yield a functional protein with acceptable taste.
(1) microbial acid protease supplied by Miles Laboratories, Inc., Elkhart, Ind.
Substitution of S. fragilis or C, utilis yield cells, P. methylotropha, L. bulgaricus or S. lactis bacterial cells, or T. viride, F. solani or A. oryzae fungal cells for S. cerevisiae cells in this preparation will also result in a functional protein with acceptable taste.
A sample of 200 g of dry heat-denatured S. cerevisiae yeast protein solids.sup.(1) was slurried in 1000 ml ethanol, filtered and washed with water. The washed filter cake was slurried in 1000 ml water, the slurry was adjusted to pH 8.5 and 50.degree. C, 2.0 g of Alcalase S-6 (15,000 Delf units/g protein) was added and the mixture was stirred at 50.degree. C and pH 8.5 for 30 minutes. The resulting solution was heated to 80.degree. C for 3 minutes to deactivate to added enzyme, and the solution was then cooled to room temperature, adjusted to pH 7.0 with 1 N HCl and freeze dried. The product passed the protein functionality test and had acceptable taste with no objectionable bitterness or saltiness.
A mixture of 100 g of solvent-extracted soybean flakes.sup.(1) and 1400 ml water was stirred for 2 hours at 140.degree. F (60.degree. C) and then filtered over screens. The residual flakes were reslurried in 1100 ml water for 10 minutes at 85.degree. F (29.degree. C) and refiltered over the screens. The combined liquors were clarified by filtration, adjusted to pH 5.0, heated to 95.degree. C and held at that temperature for 10 minutes. The resulting slurry was cooled to room temperature and centrifuged, and the centrifuge cake was washed with water to yield 100 g of wet heat-denatured soy protein solids (25 g dry).
The wet heat-denatured soy protein solids was slurried in 300 ml water. The slurry was adjusted to pH 9.5 and 50.degree. C, 125 mg of Alcalase S-6 (7500 Delf Units/g protein) was added and the mixture was stirred at 50.degree. C and pH 9.5 for 15 minutes, the pH being maintained by the addition of 1 N NaOH. The resulting solution was heated to 85.degree. C for 2 minutes to deactivate the added enzyme and the solution was then cooled to room temperature, adjusted to pH 7.0 and freeze dried. The dry product passed the protein functionality test and had acceptable taste with no objectionable bitterness or saltiness.
(1) Central Soya Inc., Chicago, Ill.
The solvent-extracted soybean flakes may be replaced by soy flour, alcohol-treated soy flakes, soy concentrate or soy grits.
A 50 g sample of dry soy whey solids.sup.(1) was dissolved in 150 ml water. The solution was adjusted to pH 5.0, heated to 95.degree. C and held at that temperature for 5 minutes. The resulting slurry was cooled to room temperature and centrifuged, and the centrifuge cake was washed with water to yield 32 g of wet heat-denatured soy whey protein solids (8 g dry). The wet cake was reslurried in 75 ml water. The slurry was adjusted to pH 9.0 and 50.degree. C, 50 mg of Alcalase S-6 (9375 Delf Units/g protein) was added, and the mixture was stirred at 50.degree. C and pH 9.0 for 15 minutes, the pH being maintained by the addition of 1N NaOH. The resulting solution was heated to 80.degree. C for 3 minutes to deactivate the added enzyme, and the solution was then cooled to room temperature, adjusted to pH 7.0 and freeze dried. The dry product passed the protein functionality test and had acceptable test with no objectional bitterness or saltiness.
The ingredients of each formulation were blended and the resulting dough was transferred to greased pans, allowed to rise for 5 hours at 60.degree. C and baked at 430.degree. F (221.degree. C).
Test formulations in which the protein replacement was either functional whey protein solids or 1:1 functional whey protein solids:heat-denatured whey protein solids resulted in good quality bread with superior taste, texture and loaf volume. Replacement with heat-denatured whey protein solids alone gave a bread with taste comparable to the control but with poorer texture and lower loaf volume.
Functional yeast protein solids, prepared as in Example 8, may be substituted for functional whey protein solids in this recipe.
The starch of each formulation was combined with the water and vinegar in a blender operating at medium speed. The remaining dry ingredients, previously blended, were added, followed by the egg yolk, vegetable oil and finally the blue cheese. The mixture was blended to a smooth consistency and refrigerated.
The test formulation in which the protein replacement was functional whey protein solids resulted in a good quality salad dressing with improved taste, viscosity and resistance to water separation. The replacement with heat-denatured whey protein gave a dressing with poorer taste and reduced viscosity which also showed water separation.
Preparation of a dressing as indicated in which 3.5 g of functional whey protein solids replaced both the 5.0 g of NFDM and 1.0 of egg yolk in the control formulation resulted in a product of improved viscosity and enhanced flavor with no indication of water separation.
The boiling water was added to the preblended dry ingredients and the mixture was whipped (15-20 minutes) until the desired overrun was obtained. The resulting frosting was stored under refrigeration.
The test formulation in which the protein replacement was functional whey protein solids resulted in a good quality chocolate frosting with improved taste. The replacement with heat-denatured whey protein also gave a good quality frosting but with poorer taste.
A blend of functional whey protein solids with gelatin was prepared in which 2.1 g of gelatin was dissolved in 200 ml of water at 50.degree. C and the solution was combined with 43.7 g of the functional whey protein solids, 3.4 g sodium hexametaphosphate and 1.7 g potassium aluminum sulfate, adjusted to pH 5.0 and freeze dried. Use of this blend as the protein replacement in the test formulation resulted in a superior chocolate frosting with highly improved taste, spreadability, gloss dryness and peak characteristics.
The gelatin was dissolved in a small portion of the water at 145.degree.-150.degree. F (63.degree.-66.degree. C) and added with constant stirring to the previously blended remaining ingredients, except flavoring, at that temperature. The resulting mixture was pasteurized for 20-30 minutes at 165.degree. F (74.degree. C) and the flavoring added. The mixture was then homogenized through a 2-stage homogenizer, rapidly cooled to 40.degree. F (4.degree. C) and frozen by standard ice cream freezing techniques.
The test formulation in which the protein replacement was functional whey protein solids resulted in a good quality ice cream with superior overrun, taste, texture and mouthfeel. The replacement with heat-denatured whey protein solids gave an ice cream with inferior overrun, taste, texture and mouthfeel.
The water and shortening were heated to 140.degree. F (60.degree. C) and the sodium caseinate or its protein replacement followed by the previously melted emulsifiers, the carrageenan and the corn syrup solids were added with mixing. The mixture was then heated to 160.degree. F (71.degree. C), homogenized hot through a 2-stage homogenizer, adjusted to pH 7.0 if necessary, cooled and stored at 40.degree. F (4.degree. C).
Each resulting liquid coffee whitener was evaluated by adding 10 ml of the whitener to 80 ml of a solution of 2 weight percent freeze dried coffee in water at 165.degree. F (74.degree. C) and then heating the resulting mixture to 195.degree. F (91.degree. C).
The test formulation in which the protein replacement was functional whey protein performed similarly to the control in that both the control and test coffees were free of feathering (protein coagulation or precipitation) and showed only slight oil separation during the heating from 165.degree. to 195.degree. F. By contrast, the coffee utilizing heat-denatured whey protein solids in the test formulation showed considerable feathering and oil separation during the heating.
Functional yeast and bacteria protein solids, prepared as in Examples 8 and 9, and functional soy protein solids, prepared as in Examples 10 and 11, replaced the functional whey protein solids in this formulation with comparable results.
The ingredients of each formulation were combined and the resulting mixture was pasteurized at 60.degree. C for 10 minutes, homogenized in a 2-stage homogenizer and freeze dried.
Instant breakfasts were prepared by adding 5 g of the chocolate mix solids to 100 ml of milk and the same level of the orange mix solids to orange juice.
Good quality instant breakfasts obtained with both chocolate and orange test formulations using functional whey protein solids.
Functional yeast protein solids, prepared as in Example 8, may be substituted for functional whey protein solids in these recipes.
______________________________________ Ingredient, grams Control Test ______________________________________ Sodium caseinate 9.5 -- Functional or denatured whey protein -- 9.5 Corn syrup solids 3.8 3.8 Salt 0.15 0.15 Atmos.sup.(1) 150 0.40 0.40 Agar 2.00 2.00 Vegetable shortening 30.5 30.5 Water 54.0 54.0 ______________________________________ .sup.(1) registered trademark for emulsifier supplied by ICI United States, Inc.
The dry ingredients were blended with the water. The melted shortening and emulsifier were added and the mixture was then adjusted to pH 4.0-5.0, pasteurized at 65.degree. C for 15 minutes, homogenized in a single-stage homogenizer and cooled to 40.degree. F (4.degree. C).
The test formulation in which the protein replacement was functional whey protein solids resulted in an excellent cream cheese with superior texture and mouthfeel. Both the control formulation with sodium caseinate and the test formulation with heat-denatured whey protein solids as the protein replacement failed to give a suitable cheese because the acidic mixture curdled during pasteurization.
Repetition of the preparations substituting functional yeast protein solids and heat-denatured yeast protein solids, prepared as in Example 9, gave comparable results.
The ingredients were mixed, transferred to a loaf pan and baked at 375.degree. F (191.degree. C) for 45 minutes.
The test formulation in which the protein replacement was functional whey protein solids resulted in a better textured meatloaf with enhanced flavor. Replacement with heat-denatured whey protein solids gave a poorer meatloaf with inferior taste.
Sausages and frankfurters may be prepared using appropriate recipes and similar procedures.
Functional yeast protein solids, prepared as in Example 8, may be substituted for functional whey protein solids in this recipe and in appropriate recipes for other processed meats, such as sausages and frankfurters, wherein the modified whey protein solids may replace the NFDM or sodium caseinate content of the processed meat.
The water and vegetable shortening were combined, heated to 160.degree. F (71.degree. C) and mixed with the sodium caseinate or its replacement. The combined carrageenan, guar gum, Polysorbate 60 and Span 60 were heated to 120.degree. F (49.degree. C) and added to the mixture. The sugar and flavor were then added and the resulting mixture was homogenized hot through a 2-stage homogenizer, cooled to 50.degree. F (10.degree. C) and stored at 40.degree. F (4.degree. C) for 4 hours. The chilled mixture was whipped to 150-250 percent overrun using a high-speed mixer with nitrogen injection, and the whipped product was packaged and frozen.
The test formulation in which the protein replacement was functional whey protein solids gave excellent whipped topping with improved overrun, while that in which the replacement was heat-denatured whey protein solids failed to whip, having an overrun of less than 50 percent.
The topping preparation was repeated using functional yeast protein solids and heat-denatured yeast protein solids, prepared as in Example 8. The overrun was even higher with the functional protein while the formulation with the denatured protein again failed to whip.
The dry ingredients were blended in a mixer, the boiling water was added slowly in parts and with mixing to the blend, and the resulting mixture was packaged and frozen.
The test formulation in which the protein replacement was functional whey protein solids resulted in a good quality frozen dessert with improved taste. Replacement with heat-denatured whey protein solids gave a dessert of poorer taste. A test formulation in which the protein replacement was a blend of functional whey protein solids and gelatin prepared as in Example 14 gave an excellent frozen dessert with superior taste.
Functional yeast protein solids, prepared as in Example 8, may be substituted for the functional whey protein solids in this recipe.
The ingredients of Part A were mixed and beat into a stiff foam. The gelatin or its replacement was dissolved in the water of Part B and the solution was added with mixing to Part A. The ingredients of Part C were combined, brought to a boil and blended with combined Parts A and B. The resulting mixture was beaten until the desired peaks were formed.
Test formulations in which the protein replacement was either functional whey protein solids or functional yeast protein solids resulted in good quality marshmallow of comparable taste. Replacement with heat-denatured whey protein solids gave a product that failed to whip and with highly inferior taste. A test formulation in which the protein replacement was a blend of functional whey protein solids and gelatin prepared as in Example 14 gave an excellent marshmallow with a superior taste.
The egg white, or its replacement, was beaten until frothy. The cream of tartar, sugar and vanilla were added with whipping, and the whipping continued until strong peaks developed. The meringue was then spread on top of lemon filling in a precooked pie crust and the pie was baked at 400.degree. F (204.degree. C) for 5-10 minutes.
Test formulations in which the protein replacement was either functional whey protein solids or functional yeast protein solids resulted in good quality meringues with similar taste, improved texture and no water syneresis. Replacement with heat-denatured whey or yeast protein solids failed to produce a meringue.
The flour and half the sugar were preblended. The egg whites, cream of tartar and salt were combined and beaten until foamy. The second half of sugar was then slowly added and the beating continued until a stiff meringue developed. The flavorings followed by the flour-sugar blend were gently folded into the meringue and the resulting batter was transferred to an ungreased tube pan and baked.
The test formulation in which the protein replacement was functional yeast protein solids resulted in a good quality angel food cake of slightly poorer taste. Replacement with the heat-denatured yeast protein solids also gave a cake of slightly poorer taste and also of lower cake volume.
The ingredients were combined, cooked to 238.degree. F (114.degree. C), whipped hot to maximum overrun and cooled.
The test formulation in which the protein replacement was functional whey protein solids resulted in a good quality mazetta with improved fluff and slightly poorer taste than the control. Replacement with heat-denatured whey protein solids gave a mazetta with above the same fluff as the control but with much poorer taste.
The hydrated textured soy protein was prepared by blending 125 g textured soy protein, 300 g water, 25 g meat flavor, 8 g monosodium glutamate, 12.5 g salt and 0.5 g white pepper and allowing the blend to stand at room temperature overnight.
The vegetable shortening was melted and combined with the water, egg albumin or its replacement, soy flour and wheat gluten. This mixture was then blended with 100 g of the hydrated textured soy protein. The blend was allowed to stand 1-3 hours and was then made into meat patties and broiled at 375.degree. F (191.degree. C) for 15 minutes.
The test formulation in which the protein replacement was functional whey protein solids resulted in a good quality broiled patty similar to the control in binding, emulsification and sensory characteristics. Replacement with heat-denatured whey protein solids gave a poorer patty with inferior binding, emulsification and sensory characteristics.
Functional bacteria protein solids, prepared as in Example 8, may be substituted for functional whey protein solids in this recipe or in a recipe in which the protein replacement is for the soy flour or the wheat gluten content of the textured protein product.
The effectiveness of functional and heat-denatured whey protein solids, prepared as in Example 2, in fortifying carbonated beverages was tested by adding 0.5 to 2 g of the solids to 100 ml of a commercial carbonated orange soda or ginger ale. Addition of the functional whey protein solids did not affect the clarity or the taste of the soda. Addition of the heat-denatured whey protein solids destroyed the soda clarity with protein precipitation occurring.
Functional yeast protein solids, prepared as in Example 8, or functional soy protein solids, prepared as in Example 10 or 11, may be substituted for the functional whey protein solids in fortifying such carbonated beverages.
The ingredients were blended, pasteurized at 65.degree. C for 10 minutes, homogenized in a 2-stage homogenizer and cooled to 40.degree. F (4.degree. C).
The test formulation in which the protein replacement was functional whey protein solids resulted in a good quality chocolate milk with only slightly poorer taste than that of the control. Replacement with heat-denatured whey protein solids was ineffective since the solids did not dissolve.
Functional yeast protein solids, prepared as in Example 8, may be substituted for functional whey protein solids in this formulation.
______________________________________ Ingredient, grams Control Test ______________________________________ NFDM 8.0 -- Functional or denatured whey protein -- 7.2 Soy protein 2.2 -- Wheat flour 32.6 32.6 Salt 0.78 0.78 Egg solids 0.30 0.15 Vegetable shortening 2.33 2.33 1:1 Atmos 300:Tween.sup.(1) 60 0.30 0.30 Water 54.0 54.0 ______________________________________ .sup.(1) registered trademark for emulsifier supplied by ICI United States, Inc.
All ingredients except the emulsifiers and shortening were thoroughly blended. The emulsifiers and shortening were combined, melted and added to the blend. Sliced onion rings were dipped in the resulting batter and fried in vegetable oil at 325.degree. F (163.degree. C).
The test formulation in which the protein replacement was functional whey protein solids resulted in improved quality onion rings which were crisp and had a light fat taste and good flavor. Replacement with heat-denatured whey protein solids gave rings of about the same quality as the control.
150 Pepsin Units where said enzyme is an animal protease, said impure protein being such that in in an aqueous medium a solution or suspension is formed and said suspension must be such that a hazy or clear solution results from said proteolytic hydrolysis.
2. The process of claim 1 wherein said functional protein is derived from whey.
3. The process of claim 1 wherein the source of said microbial protein is a yeast selected from the group consisting of S. cerevisiae, S. fragilis and C. utilis.
4. The process of claim 1 wherein in step (a) said temperature is about 70.degree. to 95.degree. C and the pH of said aqueous medium is about 4 to 7.
5. The process of claim 1 wherein said proteolytic enzyme is derived from B. subtilis or B. licheniformis.
6. A functional protein prepared by the process of claim 1.
7. The functional protein of claim 6 wherein said protein is derived from whey.
8. A food composition comprising a functional protein prepared by the process of claim 1 and at least one member selected from the group consisting of carbohydrate, fat, a second source of protein other than said functional protein, vitamins and minerals.
9. The food composition of claim 8 wherein said functional protein is the sole source of protein in said food composition.
10. The food composition of claim 8 containing said second source of protein, the functional protein constituting at least 20% by weight of the total protein content of said food composition.
11. The food composition of claim 10 wherein said second source of protein is nonfat dry milk, sodium caseinate, gelatin or egg albumin.
2457642 December 1948 Butterfield et al.
2802738 August 1957 Anson et al.
3725075 April 1973 Muroi et al.
3761353 September 1973 Hoe et al.
3857966 December 1974 Feldman et al.
3970520 July 20, 1976 Feldman et al.


text:
Arnold and Marion Clark
A memorial concert in honor of Marion Clark was held in the multipurpose room of East Avenue Middle School, 3951 East Avenue, in Livermore, on the afternoon of Saturday February 5, 2011. As her friend Ursula Goldstein put it, "I can't think of a more appropriate location for the memorial." That's because the school is not only the regular venue for LAS rehearsals, it is also the site at which Clark had volunteered most. An original member of the Livermore-Amador Symphony, Clark continued as an active member of the orchestra until mid-October 2010, when a harrowing fall and subsequent hip surgery prevented her from playing viola. Until her accident in October, Clark aided and coached the young string players at East Avenue regularly, assisting music teacher and LAS member Kathy Boster. And on most weekdays for years, Marion and Arnold Clark walked hand-in-hand to the school, on their way to volunteer together.
Arnold Clark, Marion Clark's spouse of fifty years, died on November 13, 2009, and Marion died January 2, 2011. Both of them were active musically (and in other areas as well, like hiking and bird watching). They taught, promoted, and participated in music. Three examples, of many: a) They hosted weekly chamber music groups in their home; a quartet comprised of Arnold and Marion, Ursula Goldstein, and Al Oliver (also a longtime member of LAS) was the most frequent grouping. b) They proudly followed the developing career of granddaughter Meredith Clark, a professional harpist who moved to the Bay Area in 2010. c) When the Symphony rehearsed in places where music stands weren't available and players needed to supply their own, they brought a bag of collapsible stands—typically and thoughtfully, just in case someone forgot.
Player Profiles: The Clarks
The text below is from
the Livermore-Amador Symphony concert program booklet of
March 1990.
Marion and Arnold Clark of Livermore are charter members of the Livermore-Amador Symphony, both having played since the first season in 1963. Currently a member of the first violin section, Arnold began as principal second violin and has also played viola and cello at various times. Marion has been principal viola for most of her years here and was often the only viola player at Symphony rehearsals.
Before there was a symphony in the Valley, Marion recalls, their musical activities consisted of playing with the Diablo Light Opera in Walnut Creek and playing chamber music with other local musicians, which they still do. The first auditions for players were held at the Clarks' house, and they also remember the first conducting outing here of the young Stanford graduate student Arthur Barnes.
A physicist at Lawrence Livermore National Laboratory for 30 years, Arnold grew up in Madison, Wisconsin, and began violin at age 9. "I began viola," he adds, "at age 16, cello at age 45, and bass at age 68." He attended Swarthmore College, and received his Ph.D. from Indiana University in 1941. Now retired, he continues with consulting work at the Lab, and for the past 6 years has served as a volunteer with the string program in Livermore public schools.
Marion is an Indiana native who began violin at age 10 and viola in high school, where she played in the school orchestra. She attended Stevens College and graduated from Purdue University with a B.S. degree, and received an M.S. in Medical Microbiology from the University of Wisconsin. It was in Madison that she met the Clark family, when she played quartets with Arnold's sister. Marion has also played in the University of Iowa, Iowa City, Symphony, and she taught violin and viola in Livermore for many years. For the past 15 years, she has also served as a volunteer with school string programs, particularly at East Avenue Middle School, and now at Mendenhall, Sunset, Joe Michell, and Emma Smith schools.
One of six married couples on the Symphony roster, Marion and Arnold plan to spend their retirement together with "more of the same"—that is, Symphony rehearsals and helping string players in the schools.
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