Proteolytic activity of two commercial proteinases from Aspergillus oryzae and Bacillus subtilis on ovine and bovine caseins
1991 ◽
Vol 58
(4)
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pp. 461-467
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Keyword(s):
SummaryElectrophoretic analysis of the action of two commercial enzymes, Neutrase 0·5 and MKC Fungal Protease, on whole casein and αs-, β- and κ-caseins from cows' and ewes' milk showed that Neutrase 0·5 chiefly degraded β-casein, giving rise to peptides soluble at pH 4·6 detectable by PAGE. In contrast, although MKC Fungal Protease caused intense hydrolysis of bovine β-casein, in ovine casein it resulted in more active degradation of αs- than β-casein. The latter enzyme did not produce peptides soluble at pH 4·6 detectable by PAGE. Both enzymes degraded κ-casein, yielding a breakdown product that exhibited an electrophoretic mobility similar to that of the breakdown product produced by the action of commercial rennet.
1987 ◽
Vol 9
(4)
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pp. 217-220
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1914 ◽
Vol 88
(602)
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pp. 258-262
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2007 ◽
Vol 227
(1)
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pp. 159-165
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2000 ◽
Vol 90
(4)
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pp. 422-425
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1977 ◽
Vol 41
(7)
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pp. 1309-1310
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1959 ◽
Vol 37
(1)
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pp. 1361-1366
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