Action of a cell wall proteinase from Lactococcus lactis subsp. cremoris SK11 on bovine alpha s1-casein

The cell wall-associated proteinase from Lactococcus lactis subsp. cremoris SK11 was partially purified and incubated with alpha(s1)-casein for various times up to 48 h. Sixteen trifluoroacetic acid-soluble oligopeptide hydrolysis products were identified by determination of the amino acid sequence....

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Bibliographic Details
Published in:Applied microbiology and biotechnology 1991-05, Vol.35 (2), p.222-227
Main Authors: Reid, J.R, Moore, C.H, Midwinter, G.G, Pritchard, G.G
Format: Article
Language:English
Subjects:
alphaS1-casein
Amino Acid Sequence
amino acid sequences
Animals
Binding Sites
Biological and medical sciences
Biotechnology
Caseins - metabolism
Cattle
Cell Wall - enzymology
cell wall components
Cysteine Endopeptidases - metabolism
enzyme activity
Enzyme engineering
Fundamental and applied biological sciences. Psychology
Hydrolysis
Lactococcus lactis - enzymology
Lactococcus lactis subsp. cremoris
Methods. Procedures. Technologies
Miscellaneous
Molecular Sequence Data
peptides
proteinases
proteolysis
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Summary:The cell wall-associated proteinase from Lactococcus lactis subsp. cremoris SK11 was partially purified and incubated with alpha(s1)-casein for various times up to 48 h. Sixteen trifluoroacetic acid-soluble oligopeptide hydrolysis products were identified by determination of the amino acid sequence. Eleven of these oligopeptides originated from the 78-residue sequence comprising the C-terminal region of alpha(s1)-casein and were present among the products after the first 60 min of digestion. Three oligopeptides from the N-terminal region and two others from the central region of the alpha(s1)-casein sequence were also present among the early digestion products although in smaller amounts than most of the oligopeptides from the C-terminal region. No clear consensus sequence of amino acid residues surrounding the cleavage sites could be identified.
ISSN:0175-7598
1432-0614
DOI:10.1007/BF00184690