Effect of Peptides from the Sequence 58-72 of .beta.-Casein on the Activity of Endopeptidase, Aminopeptidase, and X-Prolyl-Dipeptidyl Aminopeptidase from Lactococcus lactis ssp. lactis MG1363

The Ki values for the inhibition of the 70 kDa intracellular, o-phenanthroline-sensitive endopeptidase from Lactococcus lactis ssp. lactis MG1363 by bovine beta-casein (CN) f58-72, beta-CN f58-70, beta-CN f60-68, beta-CN f60-70, and beta-CN f60-66 were 0.018, 0.01, 0.045, 0.150 and 0.28 mM, respecti...

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Published inJournal of agricultural and food chemistry Vol. 43; no. 3; pp. 849 - 853
Main Authors Stepaniak, Leszek, Fox, Patrick F, Sorhaug, Terje, Grabska, Jadwiga
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 01.03.1995
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Summary:The Ki values for the inhibition of the 70 kDa intracellular, o-phenanthroline-sensitive endopeptidase from Lactococcus lactis ssp. lactis MG1363 by bovine beta-casein (CN) f58-72, beta-CN f58-70, beta-CN f60-68, beta-CN f60-70, and beta-CN f60-66 were 0.018, 0.01, 0.045, 0.150 and 0.28 mM, respectively. The 95 kDa aminopeptidase, which is also sensitive to o-phenanthroline, from the cytoplasm of the same microorganism was inhibited by the above peptides but the corresponding Ki values were 3-10 times higher. The X-prolyl-dipeptidyl aminopeptidase from the same source, which is insensitive to o-phenanthroline, was not inhibited by any of the above peptides and in fact hydrolyzed beta-CN f60-66 and beta-CN f60-70. beta-Casein f58-72 did not inhibit thermolysin and was degraded by it. The results demonstrate that cheese ripening may be influenced by inhibitory peptides originating from beta-casein
Bibliography:1997052627
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ISSN:0021-8561
1520-5118
DOI:10.1021/jf00051a055