Wyniki wyszukiwania

Sortuj według:

Ogranicz wyniki do:

Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik

Immunoreactivity and sensitivity of peptides from beta-casein, which inhibit lactococcal peptidases, to hydrolysis by thermolysin and proteinase from Pseudomonas fluorescens

100%

Stepaniak L., Gobbetti M.

Polish Journal of Food and Nutrition Sciences

1997

tom 06

nr 4

41-48

Thermolysin and metalloproteinase from Pseudomonas fluorescens PI, both standardized to approximately the same activity on methionine enkephalin, degraded readily bovine ß-casein (ß-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 ß-CN f193-209. Cheddar, Norvegia and Roquefort type cheeses contained peptides reactive with antibodies raised against ß-CN f58-70.

Ograniczanie wyników

1 Polish Journal of Food and Nutrition Sciences

1 Gobbetti M.

1 Stepaniak L.

1 1997

Wyniki wyszukiwania

Immunoreactivity and sensitivity of peptides from beta-casein, which inhibit lactococcal peptidases, to hydrolysis by thermolysin and proteinase from Pseudomonas fluorescens