L. Stepaniak, M. Gobbetti
Polish Journal of Food and Nutrition Sciences
Thermolysin and metalloproteinase from Pseudomonas fluorescens P1, both standardized to approximately the same activity on methionine enkephalin, degraded readily bovine β-casein (β-CN) fragments 58-70, 58-72, and 193-209. These peptides inhibit 70 kDa intracellular endopeptidase and 95 kDa intracellular aminopeptidase from Lactococcus spp. The degradation 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 β-CN f193-209. Cheddar, Norvegia and Roquefort type cheeses contained peptides reactive with antibodies raised against β-CN f58-70.