Cheese 1, General aspects by Patrick F Fox; et al PDF

By Patrick F Fox; et al

ISBN-10: 0122636511

ISBN-13: 9780122636516

ISBN-10: 012263652X

ISBN-13: 9780122636523

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The first phase starts with the cleavage of K-casein at the F105~M106 bond which results in the release of a hydrophilic glycopeptide (residues 106-169) that passes into the whey, and para-K-casein that remains in the micelles, para-K-Casein is positively charged at neutral pH and causes a decrease of electric repulsive forces between casein micelles (Green, 1973). , 1989). , 1968; Larson and Whitaker, 1970). Porcine pepsin A and C, and R. miehei proteinase cleave the same bond as chymosin (F105~M106), but C.

And Ward, M. (1991). Aspergillus niger var. W. , eds, Plenum Press, New York. pp. 273-292. J. (1942). The second phase of rennet coagulation. Nature i49, 149-194. J. (1945). The purification and crystallization of rennin. Biochem. J. 39,179-187. J. (1952). Some observations on the determination of the activity of rennet. Analyst 77, 57-60. , Young, P. A. (1989). Comparison of Cheddar cheese made with a recombinant calf chymosin and with standard calf rennet. J. Dairy Res. 56, 657-664. P. P. (1990).

K-Casein is a calcium-insensitive protein which forms a protective layer around the calciumsensitive caseins (ORS1-, Ors2- , ~ - and y-), resulting in stable casein micelles. In the presence of chymosin, milk clotting occurs in two separate steps. The first phase starts with the cleavage of K-casein at the F105~M106 bond which results in the release of a hydrophilic glycopeptide (residues 106-169) that passes into the whey, and para-K-casein that remains in the micelles, para-K-Casein is positively charged at neutral pH and causes a decrease of electric repulsive forces between casein micelles (Green, 1973).

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Cheese 1, General aspects by Patrick F Fox; et al


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