Purification & properties of goat milk protease
Varshney, G.C.; Mathur, M.P.
Indian Journal of Biochemistry and Biophysics 16(6): 375-378
1979
ISSN/ISBN: 0301-1208 PMID: 398329 Document Number: 141896
Protease activities in fresh milk from goats, cows and buffaloes were assayed and compared using casein as a substrate. Protease activity was highest in goats' milk when the substrate was buffalo casein. Activity was greatest on kappa -casein, followed by alpha s-casein, and least on beta -casein from buffaloes' or goats' milk. The goats' milk protease was partially purified (208-fold) and the purity confirmed by electrophoresis. The protease was resolved into 5 major fractions and one minor band by sodium dodecylsulphate/polyacrylamide electrophoresis. The partially purified enzyme had a pH optimum of 8.0 and an optimum temp. of 37 deg C.