Biochemistry of Food Proteins by B. J. F. Hudson

By B. J. F. Hudson

Advancements within the knowing of meals protein constitution, behaviour and purposes proceed apace. a lot of those have, some time past decade, been pronounced and evaluated within the sequence 'Developments in nutrition seasoned­ teins' , comprising seven volumes, with a complete of fifty five chapters. The time has now come to re-assess a few of the subject matters reviewed in that sequence and so as to add definite others. in spite of the fact that, rather than assembling, a few­ what at random, nutrients protein subject matters from rather disparate fields in indi­ vidual volumes, we now have made up our minds to compile homogeneous teams of issues, each one representing a particular area of the topic. lower than the overall subject of 'Progress in meals 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 nutrients Proteins'. those final are in energetic examine fields within which new strengthen­ ments were of specified value. during this feel, accordingly, they're welcome updates.

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R. Duckworth. Academic Press, NY, 1975, pp. 73-92. 30. , Nucleic acids, peptides and proteins. 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.

In studies using blood plasma proteins, Hermannsson & Lucisan057 reported that water binding and texture are not always correlated and should be treated separately. Changes in gel structure may affect texture and water binding quite differently. As gels are heated above the gelation temperature, protein-protein interactions increase. Shrinkage will occur if protein-protein interactions are uniform throughout the gel. If the protein has not been distributed evenly in the gel, the stronger protein-protein interactions will cause a partial disruption of the gel network.

Chou, D. , Protein-water interactions and functional properties. 1. Am. Oil Chem. , S6 (1979) 53A-62A. 4. Bull, H. , Protein hydration. II. Specific heat of egg albumin. Arch. Biochem. , 128 (1968) 497-502. 5. , The physical properties of water associated with biomolecules. In Water Relations of Foods, ed. 93-109. 6. , Water in aqueous solutions: recent advances. In Properties of Water in Foods, ed. D. Simatos & J. Multon. Martinus Nijhoff Publishers, Dordrecht, The Netherlands, 1985, pp. 1-23.

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