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Additional info for Cheese 1, General aspects
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). , 1986). The differences in milk constituents (both proteins and other chemicals) as well as the pre-treatment process can affect the rate of the primary enzymatic stage.
62 A resolution and suggest that human progastricsin has a conformational structure and mechanism of activation analogous to those for pepsinogen. Site-directed mutagenesis at the two sites for autoproteolysis of prochymosin suggests that these processing sites can function independent of one another (McCaman and Cummings, 1986, 1988). 5, normal activation processing and proteolytic processing occurred (McCaman and Cummings, 1986). 5 while the processing site at pH 2 was not affected (McCaman and Cummings, 1988).
1996, 1998a). , 1980). 2 Berridge (1945); Fish (1957) Foltmann (1959a) Fish (1957) Lindqvist and Storgads (1960) Okigbo et aL (1985a) Raymond et aL (1972) van Hooydonk et al. (1984) Visser et aL (1976, 1987) Fish (1957) Hofmann and Shaw (1964) William et aL (1972) Arima et al. (1970) Arima et al. 1 Takahashi (1995) Pepsin Penicillopepsin Endothiapepsin Rhizomucorpepsin S. cerevisiae References proteinase A A. niger proteinase A Rennets: General and Molecular Aspects similar to the native enzyme.