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Purification and characterization of a cell wall proteinase from Streptococcus lactis NCDO 763

Published online by Cambridge University Press:  01 June 2009

Véronique Monnet ,
Dominique Le Bars  and
Jean-Claude Gripon
Véronique Monnet
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France
Dominique Le Bars
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France
Jean-Claude Gripon
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France
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Summary

A proteinase was purified from a cell wall extract of a culture of Streptococcus lactis NCDO 763 grown in skim milk. Being active at a low pH (at pH 4·8 on haemoglobin and pH 6·–6·5 on casein) and completely inhibited by diisopropylfluorophosphate, it was considered to be a serine proteinase partly inhibited by EDTA; the mol. wt was ∼ 80000.

Type
Original Articles
Information
Journal of Dairy Research , Volume 54 , Issue 2 , May 1987 , pp. 247 - 255
Copyright
Copyright © Proprietors of Journal of Dairy Research 1987

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References

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