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Partial characterization of cheese-ripening proteinases produced by the yeast Kluyveromyces lactis

Published online by Cambridge University Press:  01 June 2009

Paul A. Grieve ,
Barry J. Kitchen ,
John R. Dulley  and
John Bartley
Paul A. Grieve
Affiliation:
Otto Madsen Dairy Research Laboratory, Department of Primary Industries, Hamilton, Queensland 4007, Australia
Barry J. Kitchen
Affiliation:
Otto Madsen Dairy Research Laboratory, Department of Primary Industries, Hamilton, Queensland 4007, Australia
John R. Dulley
Affiliation:
Otto Madsen Dairy Research Laboratory, Department of Primary Industries, Hamilton, Queensland 4007, Australia
John Bartley
Affiliation:
Department of Chemistry, Queensland Institute of Technology, Brisbane, Queensland 4001, Australia
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Summary

An extract of Kluyveromyces lactis 416 and a β-galactosidase preparation (Maxilact 40000) contaminated with proteinase, showed similar pH profiles of caseinolytic activity. Similar modes of casein hydrolysis (κ-, > αs-, ≥ β-) were observed at pH 5·0 (the pH of Cheddar cheese), without detection of bitterness. The contaminated Maxilact preparation contained similar proteinase types to those detected in an autolysate of K. lactis. Both the autolysate and the Maxilact preparation contained acid endopeptidase (proteinase A), serine endopeptidase (proteinase B) and serine exopeptidase (carboxypeptidase Y) activities. Some aminopeptidase activity was also detected in both preparations. There were some differences in apparent molecular weight and charge properties between proteinase A and B and carboxypeptidase Y from the 2 proteinase sources.

Type
Original Articles
Information
Journal of Dairy Research , Volume 50 , Issue 4 , November 1983 , pp. 469 - 480
Copyright
Copyright © Proprietors of Journal of Dairy Research 1983

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