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Titolo:
Debittering and hydrolysis of a tryptic hydrolysate of beta-casein with purified general and proline specific aminopeptidases from Lactococcus lactisssp cremoris AM2
Autore:
Bouchier, PJ; OCuinn, G; Harrington, D; FitzGerald, RJ;
Indirizzi:
Univ Limerick, Dept Life Sci, Limerick, Ireland Univ Limerick Limerick Ireland merick, Dept Life Sci, Limerick, Ireland TEAGASC, Dairy Prod Res Ctr, Fermoy, Cork, Ireland TEAGASC Fermoy Cork Ireland C, Dairy Prod Res Ctr, Fermoy, Cork, Ireland TEAGASC, Data Syst Dept, Fermoy, Cork, Ireland TEAGASC Fermoy Cork Ireland AGASC, Data Syst Dept, Fermoy, Cork, Ireland Galway Mayo Inst Technol, Dept Life Sci, Galway, Ireland Galway Mayo Inst Technol Galway Ireland Dept Life Sci, Galway, Ireland
Titolo Testata:
JOURNAL OF FOOD SCIENCE
fascicolo: 6, volume: 66, anno: 2001,
pagine: 816 - 820
SICI:
0022-1147(200108)66:6<816:DAHOAT>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACETYL-L-CYSTEINE; BITTER PEPTIDES; SUBSP CREMORIS; DIPEPTIDYL-AMINOPEPTIDASE; ORTHO-PHTHALALDEHYDE; MILK-PROTEINS; PURIFICATION; ASSAY; MECHANISM;
Keywords:
debittering; hydrolysates; aminopeptidase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: FitzGerald, RJ Univ Limerick, Dept Life Sci, Limerick, Ireland Univ Limerick Limerick Ireland fe Sci, Limerick, Ireland
Citazione:
P.J. Bouchier et al., "Debittering and hydrolysis of a tryptic hydrolysate of beta-casein with purified general and proline specific aminopeptidases from Lactococcus lactisssp cremoris AM2", J FOOD SCI, 66(6), 2001, pp. 816-820

Abstract

In this study, purified P-casein was hydrolysed with trypsin to produce a bitter substrate. The role of 3 aminopeptidases, a general aminopeptidase lysyl-para-nitroanilide hydrolase (KpNA-H), X-prolyl dipeptidyl aminopeptidase (Pep X) and aminopeptidase P (Pep P) each purified from Lactococcus lactis ssp. cremoris AM2, in the hydrolysis and debittering of the tryptic hydrolysate of beta -casein, was then studied. The hydrolysates were analyzed for percentage degree of hydrolysis (DH%) and bitterness score. Results indicate that the hydrolysis and debittering potential of the general aminopeptidase (KpNA-H) is limited in the absence of proline specific aminopeptidases. Statistically significant (p<0.001) reductions in bitterness were obtained following incubation of the tryptic digest of <beta>-casein with specific combinations of the above aminopeptidases.

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Documento generato il 14/07/20 alle ore 06:19:02