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. 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.
Reid
J R
JR
Department of Chemistry and Biochemistry, Massey University, Palmerston North, New Zealand.
Moore
C H
CH
Midwinter
G G
GG
Pritchard
G G
GG
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002364:Caseins / Q000378:metabolism*; D002417:Cattle; D002473:Cell Wall / Q000201:enzymology; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D006868:Hydrolysis; D013294:Lactococcus lactis / Q000201:enzymology*; D008969:Molecular Sequence Data
D002364:Caseins; D003546:Cysteine Endopeptidases; C042477:streptopain