By J. E. Kinsella, D. J. Rector, L. G. Phillips (auth.), R. Y. Yada, R. L. Jackman, J. L. Smith (eds.)
ISBN-10: 1461361478
ISBN-13: 9781461361473
Food proteins represent a various and intricate number of organic macro molecules. even if contributing to the dietary caliber of the meals we con sume, proteins additionally act as indispensable elements through advantage in their different practical houses. The expression of those sensible homes throughout the instruction, processing and garage of meals is essentially dictated by means of alterations to the constitution or structure-related homes of the proteins concerned. for this reason, germane to the optimum use of latest and destiny foodstuff protein assets is a radical realizing of the character of the relationships among constitution and serve as. it's the aim of this publication to assist in larger defining those relationships. specified sections are obvious: first of all, these chapters which handle struc ture-function relationships utilizing quite a few meals platforms as examples to illustrate the intricacies of this courting, and secondly, these chapters which debate ideas used to both research structural parameters or reduction in setting up quantitative relationships among protein constitution and serve as. The editors wish to thank all individuals for his or her tips, co-operation and, specifically, their endurance in placing this quantity jointly, and the subsequent companies/organizations for his or her monetary help with out which it can now not were the good fortune it was once: Ault meals constrained, most sensible meals Canada restricted, average Sciences and Engineering learn Council of Canada, Ontario Ministry of Agriculture and nutrition, Quest foreign Canada Inc., and college of Guelph. R.Y.Y. R.LJ.
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Extra resources for Protein Structure-function Relationships in Foods
Sample text
Kinsella and W. Soucie), American Oil Chemistry Society, Champaign, Illinois. Lee, land Tirnasheff, S. (1981) The stabilization of proteins by sucrose. 1. Bioi. Chern. 246:7193. Li-Chan, E. and Nakai, S. (1989) Effects of molecular changes (SH groups and hydrophobicity) of food proteins on their functionality, in Food Proteins: Structure and Functional Relationships, (eds lE. Kinsella and W. Soucie), American Oil Chemistry Society, Champaign, Illinois, pp. 232-51. PHYSICOCHEMICAL PROPERTIES OF PROTEINS 21 MacRitchie, F.
Bioi. 184:535-42. Y. (1990) Electron microscopy of thennal aggregation of myosin. J. Biochern. 108:896-98. , Samejima, K. and Yasui, T. (1988) Heat-induced gelation of myosin filaments. Agric. Bioi. Chern. 52:1801-11. Ziegler, R. A. (1990) Gelation of proteins. Adv. Food Nutr. Res. 34:203-98. E. x. CHEN, S. L. g. milk proteins and egg proteins have been shown to yield large polypeptide fragments upon limited proteolysis. Probing for domain structure and preparation of protein domains by limited proteolysis is especially advantageous with immobilized proteinase bioreactors, since autolysis is prevented and the degree of hydrolysis is easily and precisely controlled.
To probe for general changes in protein structure it is desirable to use a proteinase with broad substrate specificity or a mixture of proteinases to ensure that a structural change in a particular region will not be missed due to the lack of a susceptible sequence. , 1982b; Swaisgood and Catignani, 1987; Swaisgood, 1989). 2 M for lysozyme. , 1982a). 46 PROTEIN STRUCTURE FUNCTION A criticism frequently directed at the use of immobilized enzymes is that they continually leak: from the support. However, this problem is not observed if the enzyme is immobilized via a stable covalent bond and if the support is thoroughly washed to remove all noncovalently adsorbed enzyme.
Protein Structure-function Relationships in Foods by J. E. Kinsella, D. J. Rector, L. G. Phillips (auth.), R. Y. Yada, R. L. Jackman, J. L. Smith (eds.)
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