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Additional info for Cheese 1, General aspects, Edition: 3rd ed
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). 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.
210 and 2 4 9 . . 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.
These changes may be due to the increased negative charge at the 'flap' region that may have altered the network hydrogen bonding and influenced the substrate recognition of the enzyme. , 1976a,b). , 1985). , 1985). As pepstatin is relatively ineffective towards calf chymosin, analogue inhibitors have been developed. A series of inhibitors have been designed by Powell et al. 1 than pepstatin. , 1990). M e c h a n i s m of Milk Clotting In milk, the primary soluble proteins are the whey proteins, ot-lactalbumin and [3-1actoglobulin.