Influence of denaturation and aggregation of β-lactoglobulin on its tryptic hydrolysis and the release of functional peptides

Food Chemistry

Volumn 187, Issue , 2015, Pages 545-554

  Leeb, Elena ^a   Götz, Alexander ^a   Letzel, Thomas ^a   Cheison, Seronei Chelulei ^a,b   Kulozik, Ulrich ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b Mars GmbH   (Germany)

Author keywords

Bioactive peptides; Denaturation of lactoglobulin; Non native monomers; Protein hydrolysis; Trypsin

Indexed keywords

DENATURATION; HYDROLYSIS; MONOMERS; PEPTIDES; PROTEINS;

BIOACTIVE PEPTIDES; LACTOGLOBULIN; NON-NATIVE; PROTEIN HYDROLYSIS; TRYPSIN;

ENZYMATIC HYDROLYSIS;

BETA LACTOGLOBULIN; MONOMER; PEPTIDE; LACTOGLOBULIN; WHEY PROTEIN;

ARTICLE; CONCENTRATION (PARAMETERS); ELECTROSPRAY MASS SPECTROMETRY; HEAT TREATMENT; HYDROLYSIS; LIQUID CHROMATOGRAPHY; PH; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN SECRETION; TIME OF FLIGHT MASS SPECTROMETRY; CHEMISTRY; HEAT; MASS SPECTROMETRY;

HOT TEMPERATURE; HYDROLYSIS; LACTOGLOBULINS; MASS SPECTROMETRY; PEPTIDES; PROTEIN DENATURATION; WHEY PROTEINS;

EID: 84929458631     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2015.04.034     Document Type: Article

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