IMMUNOREACTIVITY AND SENSITIVITY OF PEPTIDES FROM ß-CASEIN, WHICH INHIBIT LACTOCOCCAL PEPTIDASES, TO HYDROLYSIS BY THERMOLYSIN AND PROTEINASE FROM PSEUDOMONAS FLUORESCENS
 
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Pol. J. Food Nutr. Sci. 1997;47(4):41–48
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ABSTRACT
Thermolysin and metalloproteinase from Pseudomonas fluorescens P1, both standardized to approximately the same activity on methionine enkephalin, degraded readily bovine ß-casein (ß-CN) fragments 58-70, 58-72, and 1 93-209. These peptides inhibit 70 kDa intracellular endopeptidase and 95 kDa intracellular aminopeptidase from Lactococcus spp. Thedegradation patterns of peptides released from each of the 3 fragments were different for thermolysin and Pseudomonas proteinase. The two enzymes cleaved different peptide bonds of ß-CN f193-209. Cheddar, Norvegia and Roquefort type cheeses contained peptides reactive with antibodies raised against ß-CN f58-70.
ISSN:1230-0322