Hydrolysis of β-casein (193-209) Fragment by Whole Cells and Fractions of Lactobacillus casei and Lactococcus lactis |
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| Authors: | L Parra P Fernández de Palencia V Casal T Requena C Peláez |
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| Affiliation: | Authors Parra, Fernández de Palencia, Casal, Requena and Peláez are affiliated with Departamento de Ciencia y Tecnología de Productos Lácteos, Instituto del Frío (CSIC), Ciudad Universitaria, E-28040, Madrid Spain. |
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| Abstract: | Whole 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 b-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. |
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| Keywords: | b-CN (f 193-209) peptide bitterness Lactobacillus casei Lactococcus lactis cheese ripening |
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