The extent of ovalbumin in vitro digestion and the nature of generated peptides are modulated by the morphology of protein aggregates

Food Chemistry

Volumn 157, Issue , 2014, Pages 429-438

  Nyemb, Kéra ^a,b   Guérin Dubiard, Catherine ^a,b   Dupont, Didier ^a,b   Jardin, Julien ^a,b   Rutherfurd, Shane M ^c   Nau, Françoise ^a,b  

^a UMR1253   (France)

^b AGROCAMPUS OUEST   (France)

^c MASSEY UNIVERSITY   (New Zealand)

Author keywords

Aggregation; Food processing; Globular protein; In vitro digestion; Peptide

Indexed keywords

AGGLOMERATION; FOOD PROCESSING; MORPHOLOGY; PEPTIDES;

GLOBULAR PROTEINS; HEAT INDUCED AGGREGATION; IN-VITRO DIGESTIONS; LINEAR AGGREGATES; PEPTIDE IDENTIFICATION; PROTEIN AGGREGATES; QUALITATIVE DIFFERENCES; SPHERICAL AGGREGATES;

AGGREGATES;

OVALBUMIN; PEPTIDE; PROTEIN; PROTEIN AGGREGATE;

ARTICLE; DIGESTION; FOOD PROCESSING; HYDROLYSIS; IN VITRO DIGESTION; IN VITRO STUDY; LIQUID CHROMATOGRAPHY; MORPHOLOGY; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SECRETION; SURFACE PROPERTY; TANDEM MASS SPECTROMETRY; CHEMISTRY; MASS SPECTROMETRY; PHYSIOLOGY; PROCEDURES;

IN VITRO TECHNIQUES; MASS SPECTROMETRY; OVALBUMIN; PEPTIDES; PROTEIN AGGREGATES; PROTEINS; TANDEM MASS SPECTROMETRY;

EID: 84896108126     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2014.02.048     Document Type: Article

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