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 in | Journal of agricultural and food chemistry Vol. 43; no. 3; pp. 849 - 853 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Chemical Society
01.03.1995
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Subjects | |
Online Access | Get full text |
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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 |
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Bibliography: | 1997052627 Q04 Q02 istex:A591470B7E2EB6CC34F49FB437E001E0F4703E15 ark:/67375/TPS-8XFQZ10R-M ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0021-8561 1520-5118 |
DOI: | 10.1021/jf00051a055 |