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Proteolytic activity of two commercial proteinases from Aspergillus oryzae and Bacillus subtilis on ovine and bovine caseins

Published online by Cambridge University Press:  01 June 2009

Rosina López-Fandiño ,
Mercedes Ramos ,
Estrella Fernández-García  and
Agustin Olano
Rosina López-Fandiño
Affiliation:
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva 3, 28006 Madrid, España
Mercedes Ramos
Affiliation:
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva 3, 28006 Madrid, España
Estrella Fernández-García
Affiliation:
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva 3, 28006 Madrid, España
Agustin Olano
Affiliation:
Instituto de Fermentaciones Industriales (CSIC), Juan de la Cierva 3, 28006 Madrid, España
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Summary

Electrophoretic 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.

Type
Original Articles
Information
Journal of Dairy Research , Volume 58 , Issue 4 , November 1991 , pp. 461 - 467
Copyright
Copyright © Proprietors of Journal of Dairy Research 1991

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