Cheese: Chemistry, Physics & Microbiology by Patrick F. Fox, Paul L. H. McSweeney, Timothy M. Cogan,

By Patrick F. Fox, Paul L. H. McSweeney, Timothy M. Cogan, Timothy P. Guinee

The marketplace for cheese as a nutrients aspect has elevated quickly lately and now represents upto nearly 50% of cheese construction in a few international locations. This 3rd version of the hugely profitable two-volume paintings at the medical elements of Cheese: Chemistry, Physics, and Microbiology comes in volumes entitled General elements and Major Cheese teams. This identify comprises up to date stories of the literature at the chemical, biochemical, microbiological and physico-chemical features of cheese in most cases. quantity one will specialize in normal points at the ideas of cheese technological know-how, whereas quantity makes a speciality of significant cheese teams that is dedicated to the features of the primary households of cheese. Cheese: Chemistry, Physics, and Microbiology Two-Volume Set is accessible for buy as a collection, and besides, so are the volumes separately. *Extensive referencing supplies extra exploration on comparable cheese subject matters *Produced in a brand new 2-color layout *Illustrated with quite a few figures and tables

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1986); (5) Chen etaL (1991); (6) Horiuchi etaL (1988); (7) Harris et aL (1982) and Moir et aL (1982); (8) Pungercar et aL (1991); (9) Lin et aL (1989); (10) Hayano et aL (1988); (11)Ishihara etaL (1989); (12) Birch and Loh (1990); (13) Ammerer etaL (1986); (14) MacKay etaL (1988); (15) Togni etal. (1991); (16) Runeberg-Roos et aL (1991) (adapted from Orprayoon, 1994). Tertiary structure The three-dimensional structure of several aspartic proteinases has been solved by X-ray crystallography (Fig.

282. In addition, ion-pairs are found between R59... D57, R157... E308, R157. 9 9 1326 (COO-), R307... Dll and R315... , 1991). , 1991). , 1992). The active site of aspartic proteinases is highly conserved and consists of residues, Asp--Thr--Gly, from each domain of the enzyme. , 1991). , 1990). Chymosin has the closest structural agreement with porcine pepsin. Of the fungal proteinases, the rhizopus protease molecule has higher structural homology with chymosin than with penicillopepsin or cryphonectria protease.

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). Cloning, sequence and expression of rat cathepsin D. Nucleic Acids Res. 18, 6445-6446. T. and Pedersen, V. (1985). , Walter de Gruyter, Berlin. pp. 151-161. , Atrash, B. and Szelke, M. (1987). On the rational design of renin inhibitors: X-ray studies of aspartic proteinases complexed with transition-state analogues.

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