Debittering of a tryptic digest of bovine beta-casein using porcine kidney general aminopeptidase and X-prolydipeptidyl aminopeptidase from Lactococcus lactis subsp. cremoris AM2
2000
Barry, C.M. | O'Cuinn, G. | Harrington, D. | O'Callaghan, D.M. | Fitzgerald, R.J.
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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