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Effect of aspartyl proteinases of Penicillium caseicolum and Penicillium roqueforti on caseins

Published online by Cambridge University Press:  01 June 2009

Patrick Trieu-Cuot ,
Marie-Jose Archieri-Haze  and
Jean-Claude Gripon
Patrick Trieu-Cuot
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique, CNRZ, 78350 Jouy-en-Josas, France
Marie-Jose Archieri-Haze
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique, CNRZ, 78350 Jouy-en-Josas, France
Jean-Claude Gripon
Affiliation:
Laboratoire de Biochimie et Technologie Laitières, Institut National de la Recherche Agronomique, CNRZ, 78350 Jouy-en-Josas, France
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Summary

The aspartyl proteinases of Penicillium caseicolum and P. roqueforti acted identically on β-casein; both enzymes split at least 3 bonds: Lys29–Ile30, Lys97–Val98 and Lys99–Glu100. From αsl-casein, these proteinases released 6 main degradation products which arose from the splitting of 4 bonds; P. roqueforti aspartyl proteinase was found to cleave 1 bond at a higher rate than P. caseicolum aspartyl proteinase. A hypothetical sequential hydrolysis mechanism of αsl-casein by these 2 enzymes is proposed from a study of the degradation by isoelectric focusing and by 2-dimensional electrophoresis.

Type
Original Articles
Information
Journal of Dairy Research , Volume 49 , Issue 3 , August 1982 , pp. 487 - 500
Copyright
Copyright © Proprietors of Journal of Dairy Research 1982

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References

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