Egg Consumption and Human Health
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Impact of Steam Treatment on Protein Quality Indicators of Full Fat Soybeans from Different Origins
Impact of steam treatment on protein quality indicators of full fat soybeans from different origins Pieter Bos 20-10-2019 1 Wageningen University ASG - Animal Nutrition Group Impact of steam treatment on protein quality indicators of full fat soybeans from different origins Author : Bos, P. Registration nr. : 940221104030 Code : ANU-80436 Supervisor(s) : A.F.B. van der Poel, G. Bosch Wageningen, Oktober 2018 2 Copyright Niets uit dit verslag mag worden verveelvoudigd en/of openbaar gemaakt door middel van druk, fotokopie, microfilm of welke andere wijze ook, zonder voorafgaande schriftelijke toestemming van de hoogleraar van de leerstoelgroep Diervoeding van Wageningen Universiteit. No part of this publication may be reproduced or published in any form or by any means, electronic, mechanical, photocopying, recording or otherwise, without prior written permission of the head of the Animal Nutrition Group of Wageningen University, The Netherlands. 3 Summary The production of soybeans in the EU-28 in 2016 was 2.4 million tons, which is only 0.7% of the global production. From a social perspective, there is a stimulus in the Netherlands to a protein transition in which regional proteins are used for livestock farming. Heat-treated full-fat soybeans (FFSB) can be an important protein source. Due to the gap in knowledge about European soybeans, more research can provide clarity about protein quality of European FFSB. In this study, raw GMO- free, unprocessed soybeans from European zone (France, FFSBFR; Netherlands, FFSBNL ) and common used beans (Ukraine, FFSBUKR; Brazil, FFSBBR) were steam-toasted for 9 different time- temperature combinations, and analysed on different in-vitro protein quality indicators: Trypsin inhibitor activity (TIA), total and reactive lysine (rLys, tLys), crude protein (CP), pH-stat digestibility at 10 minutes (DH10) and 120 minutes (DH120), and protein dispersibility index (PDI). -
Breeding for Quality Protein Maize (QPM) Varieties: a Review
agronomy Review Breeding for Quality Protein Maize (QPM) Varieties: A Review Liliane N. Tandzi 1,2,*, Charles S. Mutengwa 1, Eddy L. M. Ngonkeu 2,3, Noé Woïn 2 and Vernon Gracen 4 1 Department of Agronomy, Faculty of Science and Agriculture, University of Fort Hare, P. Bag X1314, Alice 5700, South Africa; [email protected] 2 Institute of Agricultural Research for Development (IRAD), P.O. Box 2123, Messa, Yaounde, Cameroon; [email protected] (E.L.M.N.); [email protected] (N.W.) 3 Department of Plant Biology and Physiology, Faculty of Science, University of Yaounde I, Yaounde, Cameroon 4 West Africa Centre for Crop Improvement (WACCI), College of Basic and Applied Sciences, University of Ghana, Legon PMB LG 30, Accra 999064, Ghana; [email protected] * Correspondence: [email protected] or [email protected]; Tel.: +27-063-459-4323 Received: 28 August 2017; Accepted: 19 October 2017; Published: 28 November 2017 Abstract: The nutritional evaluation of quality protein maize (QPM) in feeding trials has proved its nutritional superiority over non-QPM varieties for human and livestock consumption. The present paper reviews some of the most recent achievements in development of QPM varieties using both conventional and molecular breeding under stressed and non-stressed environments. It is evident that numerous QPM varieties have been developed and released around the world over the past few decades. While the review points out some gaps in information or research efforts, challenges associated with adoption QPM varieties are highlighted and suggestions to overcome them are presented. The adoption of released varieties and challenges facing QPM production at the farmer level are also mentioned. -
Sources of Carotenoids and Their Uses As Animal Feed
Scientific Papers. Series D. Animal Science. Vol. LXI, Number 2, 2018 ISSN 2285-5750; ISSN CD-ROM 2285-5769; ISSN Online 2393-2260; ISSN-L 2285-5750 important role in molecular processes of cell molecules, joined in a head to tail pattern membranes whose structure, properties and (Mattea, 2009; Domonkos, 2013). Structurally, SOURCES OF CAROTENOIDS AND THEIR USES stability can be modified, leading to possible carotenoids take the form of a polyene chain AS ANIMAL FEED ADDITIVES – A REVIEW beneficial effects on human health (Zaheer, that functions as a chromophore, due to 9-11 2017). conjugated double bonds and possibly Diana PASARIN, Camelia ROVINARU Out of high production and marketability terminating in rings, what determines their reasons, carotenoids are present in the animal characteristic color in the yellow to red range National Institute for Research and Development in Chemistry and Petrochemistry kingdom, playing functions such as coloring (Vershinin, 1999). The presence of different 202 Spl. Independentei, Bucharest, Romania (pets/ornamental birds and fish, mimicking), number of conjugated double bounds leades to flavoring (scents and pollination in nature), various stereoisomers abbreviated as E- and Z- Corresponding author email: [email protected] reproduction (bird feathers and finding mates; isomers, depending on whether the double development of embryos), resistance to bonds are in the trans (E) or cis (Z) Abstract bacterial and fungal diseases, immune configuration (Vincente et al., 2017). responses (lutein connected to anti- Carotenoids are synthesized by all Carotenoids are natural pigments, widely distributed in nature, synthesized by plants, algae, fungi, and phototrophic bacteria. Carotenoids have coloring power and antioxidant properties, being used as colorants for foods, cosmetics and inflammatory natural substance in poultry), as photosynthetic organisms and some non- feeds. -
Synthèse Organique D'apo-Lycopénoïdes, Étude Des
Synthèse organique d’apo-lycopénoïdes, étude des propriétés antioxydantes et de complexation avec l’albumine de sérum humain Eric Reynaud To cite this version: Eric Reynaud. Synthèse organique d’apo-lycopénoïdes, étude des propriétés antioxydantes et de com- plexation avec l’albumine de sérum humain. Sciences agricoles. Université d’Avignon, 2009. Français. NNT : 2009AVIG0231. tel-00870922 HAL Id: tel-00870922 https://tel.archives-ouvertes.fr/tel-00870922 Submitted on 8 Oct 2013 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. ACADEMIE D’AIX-MARSEILLE UNIVERSITE D’AVIGNON ET DES PAYS DE VAUCLUSE THESE présentée pour obtenir le grade de Docteur en Sciences de l’Université d’Avignon et des Pays de Vaucluse SPECIALITE : Chimie SYNTHESE ORGANIQUE D'APO-LYCOPENOÏDES ETUDE DES PROPRIETES ANTIOXYDANTES ET DE COMPLEXATION AVEC L'ALBUMINE DE SERUM HUMAIN par Eric REYNAUD soutenue le 23 novembre 2009 devant un jury composé de Hanspeter PFANDER Professeur, Université de Berne (Suisse) Rapporteur Catherine BELLE Chargée de recherche, CNRS Grenoble Rapporteur Paul-Henri DUCROT Directeur de recherche, INRA Versailles Examinateur Patrick BOREL Directeur de recherche, INRA Marseille Examinateur Olivier DANGLES Professeur, Université Avignon Directeur de thèse Catherine CARIS-VEYRAT Chargée de recherche, INRA Avignon Directeur de thèse Ecole doctorale 306 UMR 408, SQPOV A Je remercie l’ensemble du jury pour avoir accepté de juger ce travail : -Pr. -
Biological Value in Milk-Protein Concentrates with Malt Ingredients
─── Food Technology ─── Biological value in milk-protein concentrates with malt ingredients Olena Grek, Olena Onopriichuk, Alla Tymchuk National University of Food Technologies, Kyiv, Ukraine Abstract Keywords: Introduction. It is actual to study of biological value of milk-protein concentrates with malt ingredients. Biological Milk value characterizes the quality of the protein composition Protein with the ability to evaluate it according to physiological Malt norms. Amino acid Materials and methods. Milk protein concentrates without and with malt ingredients used for research. The biological value and amino acid composition of the samples was determined by ion exchange chromatography on LC Article history: 3000 automatic analyzer. Protein digestibility in vitro was Received 04.02.2019 determined by hydrolysis of samples using a solution of 6N Received in revised form hydrochloric acid at a temperature of (120 ± 2) ºС for 24 02.06.2019 hours. Accepted 30.09.2019 Results and discussion. The total amino acid content in milk protein concentrates with malt ingredients increased compared to control due to the addition of germinated Corresponding author: cereals (wheat, barley, oats, corn). The amino acid score for the studied samples has been Olena Onopriichuk calculated. When preparing the mixture: milk-protein E-mail: concentrate + malt ingredients, the content of limiting olena.onopriychuk@ amino acids increases – methionine + cystine and threonine. gmail.com Biological value of the experimental samples is increased. So, with wheat malt this indicator is 65.82%, barley – 65.57%, oat – 64.11%, corn – 63.95%, while for control purposes the value is fixed at 62.84%. The rationality coefficient of amino acid composition is 0.74±0.12, which is 3% higher than in milk protein concentrate obtained by traditional technology. -
Tangential Flow Filtration of Haptoglobin
Received: 10 January 2020 Revised: 7 April 2020 Accepted: 21 April 2020 DOI: 10.1002/btpr.3010 RESEARCH ARTICLE Tangential flow filtration of haptoglobin Ivan S. Pires | Andre F. Palmer William G. Lowrie Department of Chemical and Biomolecular Engineering, The Ohio State Abstract University, Columbus, Ohio Haptoglobin (Hp) is a plasma glycoprotein that scavenges cell-free hemoglobin (Hb). Correspondence Hp has various potential therapeutic applications, but it has been mainly studied for *Andre F. Palmer, William G. Lowrie treatment of acute hemolytic conditions that can arise from situations such as mas- Department of Chemical and Biomolecular Engineering, The Ohio State University, sive blood transfusion, infusion of stored red blood cells, severe burns, trauma, sepsis, 151 West Woodruff Ave, Columbus, OH radiation injury, and others. Therefore, Hp may also be beneficial during chronic 43210. Email: [email protected] hemolytic disease states such as hereditary spherocytosis, nocturnal hemoglobinuria, sickle-cell anemia, and malaria. Various methods have been developed to purify Hp Funding information National Cancer Institute, Grant/Award from plasma or plasma fractions. However, none of these methods have exploited Number: P30 CA016058; National Heart, the large molecular weight (MW) range distribution of Hp polymers to easily isolate Lung, and Blood Institute, Grant/Award Numbers: R01HL126945, R01HL138116, Hp from other plasma proteins. The present study used tangential flow filtration R56HL123015; National Institute of (TFF) to isolate polymeric Hp from plasma proteins using human Fraction IV (FIV) as Biomedical Imaging and Bioengineering, Grant/ Award Number: R01EB021926; NIH Office of the starting material. After removal of insoluble material from a suspension of FIV the Director, Grant/Award Number: S10 paste, the protein mixture was clarified on a 0.2 μm hollow fiber (HF) TFF filter. -
Life Technologies (India) Pvt. Ltd. 306, Aggarwal City Mall, Opposite M2K Pitampura, Delhi – 110034 (INDIA)
Product Specification Sheet Chicken conalbumin (ovotransferrin) proteins Antibodies Cat # CECA15-S Rabbit Anti-Chicken conalbumin protein antiserum SIZE: 100 ul Cat # CECA15-C Chicken conalbumin protein control for Western blot SIZE: 100 ul Cat # CECA16-N Chicken conalbumin proteins SIZE: 10 mg liquid at 10 mg/ml in PBS 0.05% azide or in powder form. Allergy to chicken egg or proteins is one of the more frequent Reconstitute powder in PBS at 1-10 mg/ml. It can be used causes of food hypersensitivity in infants and young children. Both positive control for antibody #CECA15-S or for coating IgG and IgA class antibodies may be detected. Ovalbumin ELISA plates. intolerance has been implicated in a number of conditions affecting children. In particular, children with cystic fibrosis show elevated anti-ovalbumin antibodies. Ovalbumin antibodies have For Western blot +ve control (Cat # CECA15-C) is supplied also been noted in some forms of kidney disease. A relationship in SDS-PAGE sample buffer (reduced). Load 10 ul/lane of between food allergy and infantile autism has also been observed. #CECA15-C for good visibility with antibody Cat #CECA15- Children with insulin-dependent diabetes mellitus show an S. Store at –20oC in suitable size aliquots. SDS may enhanced immune response to both β-lactoglobulin and crystallize in cold conditions. It should redissolve by ovalbumin, a phenomenon that may be related to the development warming before taking it from the stock. It should be of the disease. Conditions related to ovalbumin intolerance usually heated once prior to loading on gels. If the product has resolve once egg and egg based foods have been withdrawn from been stored for several weeks, then it may be preferable to the patient's diet. -
Evaluation of Feeds for Protein
EVALUATION OF FEEDS FOR PROTEIN Dept of Animal Nutrition, CoVSc & AH, Jabalpur • Usefullness of feed as a source of protein depends on two factors – Total concentration of protein – Distribution of amino acids • Common methods Crude Protein True Protein “Stutzer’s reagent” Digestible Crude Protein In Non Ruminants 1. Weight gain Methods • Protein efficiency ratio • Net protein retention • Gross protein Value 2. Nitrogen Balance Experiments • Biological value • Net Protein utilization • Protein replacement value 3. Body nitrogen retention method 4. Chemical Evaluation of protein from AA composition • Chemical score • Essential amino acid index WEIGHT GAIN METHODS i) Protein efficiency ratio (PER): Weight gain per unit weight of protein consumed Gain in wt. PER = Protein intake PER of wheat flour – 1.2 & skimmed milk powder- 2.8 Limitation: Tedious Cannot assess digestibility of protein Weight gain may be due to bone or fat formation ii) Net protein retention (NPR): It is a modification of PER Weight gain of TPG - weight loss of NPG NPR= Protein intake TPG- group fed on test protein NPG- group fed on non protein diet iii) Gross protein value (GPV): Chicks fed 8% protein for 2 weeks After that divide into 3 groups 1st 80g CP/kg 2nd 80g CP/kg + 30g CP/kg of a test protein 3rd 80g CP/kg + 30g CP/kg of a casein g increased weight gain / g test protein GPV= g increased weight gain / g casein NITROGEN BALANCE EXPERIMENTS 1. Biological Value (BV): “Karl Thomas” It is proportion of the nitrogen absorbed which is retained by the animal. N intake – (FN+UN) % BV= X 100 N intake – FN This is apparent BV NI – (FN-MFN)-(UN-EUN) % BV= X 100 NI – (FN-MFN) This is True BV 2. -
Conalbumin More Resistant to Proteolysis and Ther- the Use Of
IRON AND PROTEIN KINETICS STUDIED BY MEANS OF DOUBLY LABELED HUMAN CRYSTALLINE TRANSFERRIN * BY JAY H. KATZ (From the Radioisotope and Medical Services of the Boston Veterans Administration Hospital, and the Dept. of Medicine, Boston University School of Medicine, Boston, Mass.) (Submitted for publication June 16, 1961; accepted August 10, 1961) Although proteins isotopically labeled with io- demonstrated that not only is the iron complex of dine have been used in tracer studies for some conalbumin more resistant to proteolysis and ther- years, interest has been mainly focused on their mal denaturation than the metal-free protein, but distribution and degradation in the body. While it that it is possible to maintain the iron-binding ca- is often possible to produce iodoproteins whose pacity of the former after extensive iodination. physical and chemical properties are not grossly Since both iron and transferrin levels are af- altered, the possible effects of iodination on the fected in a variety of disease states, a technique functional properties of such substances in a in which both can be followed simultaneously in physiologic setting have been less thoroughly in- vivo should prove valuable. Elmlinger and co- vestigated. That it is possible to trace label pro- workers (18) have reported in abstract form on teins without significantly reducing their biologi- the use of doubly labeled "iron-binding globulin" cal activities has been demonstrated in the case of in human subjects, but few details were given as insulin (2) and certain anterior pituitary hor- to the methods of preparation and the distribution mones (3, 4). of the two labels. -
Methionine Livestock
National Organic Standards Board Technical Advisory Panel Review for the USDA National Organic Program May 21, 2001 Methionine Livestock 1 Executive Summary 2 3 The NOSB received a petition in 1995 to add all synthetic amino acids to the National List. After deliberation of a 4 review prepared by the TAP in 1996 and 1999, the NOSB requested a case-by-case review of synthetic amino acids used 5 in livestock production, and referred three forms of methionine to the TAP. 6 7 All of the TAP reviewers found these three forms to be synthetic. Two TAP reviewers advised that synthetic methionine 8 remain prohibited. The one reviewer who advises the NOSB to recommend adding synthetic methionine to the National 9 List agrees that it is not compatible with organic principles and suggests limitations on its use until non-synthetic sources 10 are more widely available. 11 12 The majority of the reviewers advise the NOSB to not add them to the National List for the following reasons: 13 1) Adequate organic and natural sources of protein are available [§6517(c)(1)(A)(ii)]; 14 2) Methionine supplementation is primarily to increase growth and production, not to maintain bird health, and 15 this is counter to principles embodied in the OFPA requirements for organic feed [§6509(c)(1)]; 16 3) Pure amino acids in general and synthetic forms of methionine in particular are not compatible with a 17 sustainable, whole-systems approach to animal nutrition and nutrient cycling [§6518(m)(7)]. 18 19 Methionine is an essential amino acid needed for healthy and productive poultry. -
Sports Nutrition: a Review of Selected Nutritional Supplements for Bodybuilders and Strength Athletes
Sports Nutrition: A Review of Selected Nutritional Supplements For Bodybuilders and Strength Athletes Gregory S. Kelly, N.D. Abstract Because there is widespread belief among athletes that special nutritional practices will enhance their achievements in competition, the use of supplements has become common. Accompanying the growth in supplementation by athletes has been a corresponding increase in exaggerated claims or misleading information. This article reviews several supplements currently popular among bodybuilders and other strength athletes in order to clarify which products can be expected to produce results. Included in the discussion are creatine monohydrate, beta-hydroxy beta-methylbutyrate, whey protein, phosphatidylserine, and selected amino acids and minerals. (Alt Med Rev 1997; 2(3):184-201) Introduction The increased focus on fitness and subsequent research in the exercise field has ex- panded the role of nutrition as it relates to sports performance. Because there is widespread belief among athletes that special nutritional practices will enhance their achievements in com- petition, the use of supplements has become common. Although some of the supplements have proven benefits, historically a great deal of the information on products is either misleading or exaggerated. This is perhaps best witnessed in the products marketed to bodybuilders and other athletes concerned with size, strength, and body composition. This article reviews some of the supplements currently promoted in this market in an effort to determine which contribute to maximizing results. Included in the review are creatine monohydrate, beta-hydroxy beta- methylbutyrate (HMB), whey protein, phosphatidylserine, and selected amino acids and minerals. Creatine Monohydrate Creatine monohydrate has become one of the most popular supplements in the history of bodybuilding. -
Sites of Formation of the Serum Proteins Transferrin and Hemopexin
Sites of Formation of the Serum Proteins Transferrin and Hemopexin G. J. Thorbecke, … , K. Cox, U. Muller-Eberhard J Clin Invest. 1973;52(3):725-731. https://doi.org/10.1172/JCI107234. Research Article Sites of synthesis of hemopexin and transferrin were determined by culturing various tissues of rabbits and monkeys in the presence of labeled amino acids. Labeling of the serum proteins was examined by means of autoradiographs of immunoelectrophoretic patterns as well as by precipitation in the test tubes employing immunospecific antisera. Good correlation was seen between the results obtained by the two different methods. The liver was found to be the only site of many tissues studied that synthesized hemopexin. Transferrin production was observed in the liver, submaxillary gland, lactating mammary gland, testis, and ovary. Find the latest version: https://jci.me/107234/pdf Sites of Formation of the Serum Proteins Transferrin and Hemopexin G. J. THORBECKE, H. H. LiEM, S. KNIGHT, K. Cox, and U. MULLER-EBERHARD From the Department of Pathology, New York University School of Medicine, New York 10016, and the Department of Biochemistry, Scripps Clinic and Research Foundation, and Division of Pediatric Hematology, University of California at San Diego, La Jolla, California 92037 A B S T R A C T Sites of synthesis of hemopexin and in iron deficiency and the decrease in inflammatory re- transferrin were determined by culturing various tis- actions (8). sues of rabbits and monkeys in the presence of labeled Preliminary findings (9, 10) suggested that hemo- amino acids. Labeling of the serum proteins was ex- pexin is formed by the liver.