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 Microbioljournal_title
Applied and environmental microbiologyauthors
Flambard B,Juillard Vdoi
10.1128/aem.66.12.5134-5140.2000keywords:
subject
Has Abstractpub_date
2000-12-01 00:00:00pages
5134-40issue
12eissn
0099-2240issn
1098-5336journal_volume
66pub_type
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