By Patrick F Fox; et al
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Additional info for Cheese 1, General aspects
GFSIFGDIFLKSQYV~FDSDGPQLGFAPQA 2APR IAGFGYG-NW .... GFAIIGDTFLKNNYVVFNQGVPEVQIAPVAE 4APE FGGIQSSAGIG .... INIFGDVALKAAFWFNGATTPTLGFASK YPA ISAITPMDFPEPVGPLAIVGAFLRKYYSIYDLGNNAVGLAKAI Figure 4 The sequence alignment of calf chymosin (4CMS, Newman et aL, 1991) with other aspartic proteinases based on threedimensional structures. References: 4PEP: porcine pepsin (Sielecki et aL, 1990); 2APP: penicillopepsin (James and Sielecki, 1983); 2APR: rhizopuspepsin (Suguna etaL, 1987); 4APE: endothiapepsin (Pearl and Blundell, 1984); YPA: S.
The formation of a clot is Ca 2+ dependent. The primary and the secondary phases of milk clotting overlap as the aggregation of micelles begins before the enzymatic process is complete (Brown and Collinge, 1986; Bringe and Kinsella, 1986b). , 1985a,b; Bringe and Kinsella, 1986a,b). , 1985a), while at low pH (3-4), the hydrolytic activity is high and a decrease in curd yield occurs. 6. The rate of milk clotting increases with temperature as long as the enzyme is stable (Berridge, 1942). 6 permits flocculation at a lower percentage of K-casein hydrolysis (Dalgleish, 1982).
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. Biochemistry 26, 5585-5589. , Veerapandian, B. R (1990). 1 A resolution of endothiapepsin. J. Mol. Biol. 210, 919-941. P. and Foltmann, B. (1986).
Cheese 1, General aspects by Patrick F Fox; et al