Abstract
Proteinase, endopeptidase, dipeptidase, dipeptidyl aminopeptidase, aminopeptidase, carboxypeptidase and esterase activities of cell-free extracts of ten strains of Pediococcus pentosaceus isolated from traditional Greek cheeses were examined. Proteolytic activity measured spectrophotometrically was based on hydrolysis of whole casein and casein fractions (α- and β-), while the α- and β-casein digests were examined by polyacrylamide gel electrophoresis. Crude cell-free extracts of all strains preferentially hydrolysed b-casein. The strains had high proteinase, aminopeptidase and dipeptidyl aminopeptidase activities while exhibiting quite low esterase activity using 4-nitrophenyl butyrate as substrate.
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