Peptide composition and dipeptidyl peptidase IV inhibitory properties of β-lactoglobulin hydrolysates having similar extents of hydrolysis while generated using different enzyme-to-substrate ratios

Food Research International

Volumn 99, Issue , 2017, Pages 84-90

  Le Maux, Solène ^a   Nongonierma, Alice B ^a   FitzGerald, Richard J ^a  

^a UNIVERSITY OF LIMERICK   (Ireland)

Author keywords

Degree of hydrolysis; DPP IV inhibition; Elastase; Enzyme to substrate ratio; Peptide identification; Lactoglobulin

Indexed keywords

ENZYME KINETICS; ENZYMES; HYDROLYSIS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MOLECULAR MASS; PEPTIDES;

DEGREE OF HYDROLYSIS; DIPEPTIDYL PEPTIDASE IV; ELASTASE; LACTOGLOBULIN; LIQUID CHROMATOGRAPHY TANDEM MASS SPECTROMETRY (LC MS/MS); MOLECULAR MASS DISTRIBUTIONS; PEPTIDE IDENTIFICATION; PHYSICOCHEMICAL PROPERTY;

ENZYME INHIBITION;

DIPEPTIDYL PEPTIDASE IV INHIBITOR; LACTOGLOBULIN; PANCREATIC ELASTASE; PEPTIDE FRAGMENT; PROTEIN HYDROLYSATE;

COMPARATIVE STUDY; HUMAN; HYDROLYSIS; KINETICS; LIQUID CHROMATOGRAPHY; METABOLISM; MOLECULAR WEIGHT; TANDEM MASS SPECTROMETRY;

CHROMATOGRAPHY, LIQUID; DIPEPTIDYL-PEPTIDASE IV INHIBITORS; HUMANS; HYDROLYSIS; KINETICS; LACTOGLOBULINS; MOLECULAR WEIGHT; PANCREATIC ELASTASE; PEPTIDE FRAGMENTS; PROTEIN HYDROLYSATES; TANDEM MASS SPECTROMETRY;

EID: 85019562771     PISSN: 09639969     EISSN: 18737145     Source Type: Journal    
DOI: 10.1016/j.foodres.2017.05.012     Document Type: Article

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