Biochemistry of Food Proteins - download pdf or read online

By Marilynn I. Schnepf (auth.), B. J. F. Hudson (eds.)

ISBN-10: 1468498959

ISBN-13: 9781468498950

ISBN-10: 1468498975

ISBN-13: 9781468498974

Developments within the knowing of foodstuff protein constitution, behaviour and functions proceed apace. a lot of those have, long ago decade, been said and evaluated within the sequence 'Developments in meals seasoned­ teins' , comprising seven volumes, with a complete of fifty five chapters. The time has now come to re-assess a few of the issues reviewed in that sequence and so as to add yes others. in spite of the fact that, rather than assembling, a few­ what at random, foodstuff protein subject matters from rather disparate fields in indi­ vidual volumes, we've made up our minds to collect homogeneous teams of themes, every one representing a particular zone of the topic. less than the final subject of 'Progress in foodstuff Proteins' the 1st of those teams covers 'Biochemistry' . Readers will notice that, although six of the themes reviewed during this quantity are new, 5 of them have already featured in 'Developments in foodstuff Proteins'. those final are in energetic learn fields within which new improve­ ments were of precise importance. during this feel, as a result, they're welcome updates.

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In Water, A comprehensive Treatise, ed. F. Franks. Plenum Press, NY, 1975, pp. 305-518. 31. Melander, W. , Effect of neutral salts on the formation and dissociation of protein aggregates. 1. , 2(2) (1977) 141-161. 32. , Kato, A. , Emulsifying and foaming properties of heat-denatured soybean 115 globulins in relation to their surface hydrophobicity. Agric. BioI. , 49(4) (1985) 915-919. 33. Schnepf, M. , Partial characterization of an iron soy protein complex. Nutr. Repts. , 31 (1985) 371-380. 34.

Water may be held in a gel by hydrogen bonding to hydrophilic groups, dipolar interactions with ionic groups, or structured around hydrophobic groups. Protein-water interactions tend to reduce protein-protein interactions. 44 Since gels can be formed with a concentration as low as 1%, the distance between macromolecules is very large. A tremendous amount of free space is available for water. The properties of water in gels are almost the same as that of pure bulk water. Water does not leak out of the gels, due to either some unusually weak, long range forces, or due to capillary suction in the pores formed between macromolecules.

J. , 32 (1972) 860-864. 74. Trout, G. & Schmidt, G. The effect on cooking temperature on the functional properties of beef proteins: the role of ionic strength, pH, and pyrophosphate. , 20 (1987) 129-147. 75. Labuza, T. , The nonenzymatic browning reactions as affected by water in foods. In Water Activity: Influences on Food Quality, ed. L. Rockland & G. Steward. Academic Press, NY, 1981, pp. 605-650. 76. Eichner, K. , Formation and decomposition of browning intermediates and visible sugar-amine browning reactions.

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Biochemistry of Food Proteins by Marilynn I. Schnepf (auth.), B. J. F. Hudson (eds.)


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