Surface Activity of Proteins. Chemical and Physicochemical Modifications

Автор(ы):Magdassi S.
06.10.2007
Год изд.:1996
Описание: The book gathers several approaches to modifying the surface activity of proteins, and therefore it contains both theoretical and practical descriptions. After an introductory chapter describing the basic phenomena related to the behavior of proteins at various interfaces, the following modification methods are reviewed: attachment of hydrophobic groups, increasing the anionic charges, deamidation and phosphorylation, formation of protein-polysaccharide conjugates, and proteolysis and linking of various functional groups by enzymatic reactions. These chapters are followed by a discussion of noncovalent modifications, such as binding of surfactants to proteins and denaturation of globular proteins. Some of these modifications are presented in the last chapter, which focuses on applications of proteins in food products.
Оглавление:
Surface Activity of Proteins. Chemical and Physicochemical Modifications — обложка книги.
1. Introduction: Surface Activity and Functional Properties of Proteins [1]
  Shlomo Magdassi and Alexander Kamyshny
2. Enhanced Hydrophobicity: Formation and Properties of Surface-Active Proteins [39]
  Shlomo Magdassi and Ofer Toledano
3. Increased Anionic Charge: Conformational and Functional Properties [61]
  K. D. Schwenke
4. Deamidation and Phosphorylation for Food Protein Modification [91]
  Frederick F. Shih
5. Preparation and Functional Properties of Protein-Polysaccharide Conjugates [115]
  Akio Kato
6. Enzymatic Modification as a Tool for Alteration of Safety and Quality of Food Proteins [131]
  Gyongyi Hajos
7. Denaturation of Globular Proteins in Relation to Their Functional Properties [181]
  Jacques Lefebvre and Perla Relkin
8. Protein-Surfactant Interactions [237]
  Malcolm N. Jones
9. Factors Affecting Applications of Native and Modified Proteins in Food Products [285]
  M. E. Mangino and W. James Harper
Index [323]
Формат: djvu
Размер:3622150 байт
Язык:ENG
Рейтинг: 176 Рейтинг
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