The autoproteolysis of Lactococcus lactis lactocepin III affects its specificity towards beta-casein.

Abstract:

:The effect of autoproteolysis of Lactococcus lactis lactocepin III on its specificity towards beta-casein was investigated. beta-Casein degradation was performed by using either an autolysin-defective derivative of L. lactis MG1363 carrying the proteinase genes of L. lactis SK11, which was unable to transport oligopeptides, or autoproteolyzed enzyme purified from L. lactis SK11. Comparison of the peptide pools by high-performance liquid chromatography analysis revealed significant differences. To analyze these differences in more detail, the peptides released by the cell-anchored proteinase were identified by on-line coupling of liquid chromatography to mass spectrometry. More than 100 oligopeptides were released from beta-casein by the cell-anchored proteinase. Analysis of the cleavage sites indicated that the specificity of peptide bond cleavage by the cell-anchored proteinase differed significantly from that of the autoproteolyzed enzyme.

journal_name

Appl Environ Microbiol

authors

Flambard B,Juillard V

doi

10.1128/aem.66.12.5134-5140.2000

keywords:

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

5134-40

issue

12

eissn

0099-2240

issn

1098-5336

journal_volume

66

pub_type

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