Action of a cell wall proteinase fromLactococcus lactissubsp.cremorisSK11 on bovine αs1-casein

✍ Scribed by Julian R. Reid; Christopher H. Moore; Graeme G. Midwinter; Graham G. Pritchard

• Book ID: 104654888
• Publisher: Springer
• Year: 1991
• Tongue: English
• Weight: 665 KB
• Volume: 35
• Category: Article
• ISSN: 1432-0614
• DOI: 10.1007/bf00184690

✦ Synopsis

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.