✦ LIBER ✦

Investigations on biochemical properties of milk-clotting enzymes

✍ Scribed by Braun, I. ;Kunath, H.

Publisher: John Wiley and Sons
Year: 1988
Tongue: English
Weight: 308 KB
Volume: 32
Category: Article
ISSN: 0027-769X
DOI: 10.1002/food.19880320419

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✦ Synopsis

The properties of proteolytic enzymes produces from calf maws and from an Ascomycete were studied. Both milk-clotting proteases have their optimum activity at pH 5.2 and 45 "C. The microbiological rennin has a second maximum activity at pH 3.5 and 55 "C. Temperatures above 55 "C cause a rapid decrease of activity.

The behaviour of enzyme activity is similar with varying substrate and enzyme concentrations. However, increasing amounts of enzyme in ratio to the substrate lead to reaction rates of the calf rennin differing clearly from that of the microbiological rennet complex.

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