Journal
JOURNAL OF FOOD SCIENCE
Volume 65, Issue 7, Pages 1145-1150Publisher
WILEY
DOI: 10.1111/j.1365-2621.2000.tb10255.x
Keywords
general and proline-specific aminopeptidases casein hydrolysates; enzymatic debittering; sensory analysis
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The role of leucine aminopeptidase (LAP) from pig kidney cytosol and X-prolyldipeptidyl aminopeptidase (Pep X) from Lactococcus lactis subsp. cremoris AM2 in the hydrolysis and debittering of a tryptic digest of beta -casein was studied. Hydrolysis was monitored by quantifying the release of primary amino groups and bitterness by use of a trained sensory panel, Sequential incubation of the bitter tryptic hydrolysate with LAP, Pep X and LAP resulted in higher levels of hydrolysis and significantly (P < 0.001) lower levels of bitterness than incubation with; LAP alone. The results demonstrate the central role proline-specific aminopeptidases can play in the hydrolysis and debittering of food protein hydrolysates.
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