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Hydrolysis of β-casein (193-209) fragment by whole cells and fractions of Lactobacillus casei and Lactococcus lactis

AuthorsParra, L.; Fernández de Palencia, P. ; Casal, V.; Requena, Teresa ; Peláez, Carmen
KeywordsB-CN (f193-209) peptide
Cheese ripening.
Lactobacillus casei
Lactococcus lactis
Issue Date1999
CitationJournal of Food Science 64: 899- 902 (1999)
AbstractWhole cells and fractions of Lactococcus lactis subsp. lactis IFPL 359 and Lactobacillus casei subsp. casei IFPL731 were studied. Hydrolysis products were separated by reversed-phase, high-performance liquid chromatography (RPHPLC). Under conditions, pH 5.2 and 3% NaCl, L. casei IFPL 731 was more active in hydrolysis of the β-casein (f193-209) peptide than was L. lactis IFPL 359. This hydrolyzing activity was attributed for L. casei IFPL 731 by the cell-wall proteinase. Hydrolysis of the peptide by the intracellular extract of L. casei IFPL731 was mainly located in the fraction that contained endopeptidase and Pep N aminopeptidase activities. Results may help provide approaches and treatments to control bitterness in cheese products.
Identifiersdoi: 10.1111/j.1365-2621.1999.tb15936.x
issn: 0022-1147
Appears in Collections:(IF) Artículos
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