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Titolo:
Emulsification of chemical and enzymatic hydrolysates of beta-lactoglobulin: characterization of the peptides adsorbed at the interface
Autore:
Rahali, V; Chobert, JM; Haertle, T; Gueguen, J;
Indirizzi:
Inst Natl Rech Agron, Unite Biochim & Technol Prot, F-44316 Nantes 3, France Inst Natl Rech Agron Nantes France 3 hnol Prot, F-44316 Nantes 3, France Ecole Super Agr, Angers, France Ecole Super Agr Angers FranceEcole Super Agr, Angers, France Inst Natl Rech Agron, Lab Etud & Interact Mol Alimentaires, F-44316 Nantes, France Inst Natl Rech Agron Nantes France F-44316 aires, F-44316 Nantes, France
Titolo Testata:
NAHRUNG-FOOD
fascicolo: 2, volume: 44, anno: 2000,
pagine: 89 - 95
SICI:
0027-769X(200004)44:2<89:EOCAEH>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
EMULSIFYING PROPERTIES; LIQUID INTERFACES; MILK-PROTEINS; FUNCTIONAL-PROPERTIES; TRYPTIC PEPTIDES; FOOD PROTEINS; WHEY PROTEINS; CASEIN; PROTEOLYSIS; SOLUBILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Gueguen, J Inst Natl Rech Agron, Unite Biochim & Technol Prot, BP 71627, F-44316 Nantes 3, France Inst Natl Rech Agron BP 71627 Nantes France 3 Nantes 3, France
Citazione:
V. Rahali et al., "Emulsification of chemical and enzymatic hydrolysates of beta-lactoglobulin: characterization of the peptides adsorbed at the interface", NAHRUNG, 44(2), 2000, pp. 89-95

Abstract

Bovine beta-Lactoglobulin (BLG) was cleaved by BNPS-skatole (2-(2'-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine), trypsin, or pepsin in 40% ethanol before emulsification with hexadecane in order to characterize the peptides active at the interfaces. The total digests and the different phases obtained after emulsification were analyzed by RP-HPLC to separate the peptides according to their gradual order on a hydrophilicity-to-hydrophobicity scale. In each case, hydrophobic peptides were recovered in the creamed phase and characterized by mass spectrometry and sequencing. After tryptic hydrolysis, short peptides were identified at the interfacial layer as fragments S-21-L-32, V-41-L-57, V-41-K-60, and W-61-K-70 linked to L-149-I-162 by aC-66-C-160 bond. It indicates that the hydrophilic/hydrophobic distribution of the amino acids in the sequence of the fragments is more relevant to adsorption than the length of the peptide. BNPS-skatole and peptic hydrolysis produced larger hydrophobic peptides which were also recovered in the creamed phase of the emulsion and characterized.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/07/20 alle ore 20:52:44