Effect of aspartyl proteinases ofPenicillium caseicolumandPenicillium roquefortion caseins
- 1 August 1982
- journal article
- research article
- Published by Cambridge University Press (CUP) in Journal of Dairy Research
- Vol. 49 (3) , 487-500
- https://doi.org/10.1017/s0022029900022627
Abstract
SUMMARY: The aspartyl proteinases ofPenicillium caseicolumandP. roquefortiacted identically on β-casein; both enzymes split at least 3 bonds: Lys29–Ile30, Lys97–Val98and Lys99–Glu100. From αsl-casein, these proteinases released 6 main degradation products which arose from the splitting of 4 bonds;P. roquefortiaspartyl proteinase was found to cleave 1 bond at a higher rate thanP. caseicolumaspartyl 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.This publication has 9 references indexed in Scilit:
- Electrofocusing and two-dimensional electrophoresis of bovine caseinsJournal of Dairy Research, 1981
- Role of Penicillium roqueforti proteinases during blue cheese ripeningJournal of Dairy Research, 1981
- EXOGENOUS PROTEINASES IN DAIRY TECHNOLOGYPublished by Elsevier ,1981
- Les caractères du système protéolytique de Penicillium caseicolum. III. Caractérisation d'une protéase acideLe Lait, 1979
- A rennin-sensitive bond in αs1Β-caseinJournal of Dairy Research, 1974
- Le système protéolytique de Penicillium roqueforti: II - Purification et propriétés de la protéase acideBiochimie, 1974
- Structure primaire de la caséine αsl‐bovineEuropean Journal of Biochemistry, 1971
- The Binding of Detergents to ProteinsJournal of Biological Chemistry, 1971
- PREPARATORY FRACTIONATION OF BOVINE AND SHEEP CASEINS BY CHROMATOGRAPHY ON DEAE CELLULOSE IN A UREA AND 2-MERCAPTOETHANOL MEDIUM1968