Fish skin gelatin hydrolysates produced by visceral peptidase and bovine trypsin: Bioactivity and stability

Food Chemistry

Volumn 215, Issue , 2017, Pages 383-390

  Ketnawa, Sunantha ^a   Benjakul, Soottawat ^b   Martínez Alvarez, Oscar ^c   Rawdkuen, Saroat ^a  

^a MAE FAH LUANG UNIVERSITY   (Thailand)

^b PRINCE OF SONGKLA UNIVERSITY   (Thailand)

^c INSTITUTE OF FOOD SCIENCE   (Spain)

Author keywords

Angiotensin I converting enzyme inhibitory; Antioxidative; Gelatin hydrolysates; Giant catfish; Peptidase; Stability

Indexed keywords

BIOACTIVITY; CONVERGENCE OF NUMERICAL METHODS; HYDROLYSIS; MAMMALS;

ANGIOTENSIN I-CONVERTING ENZYME; ANTIOXIDATIVE; GELATIN HYDROLYSATES; GIANT CATFISH; PEPTIDASE;

STABILITY;

DIPEPTIDYL CARBOXYPEPTIDASE; GELATIN; PEPTIDASE; PROTEIN HYDROLYSATE; TRYPSIN; ANTIOXIDANT; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; PEPTIDE HYDROLASE; SCAVENGER;

ABTS RADICAL SCAVENGING ASSAY; ANTIOXIDANT ACTIVITY; ARTICLE; BIOLOGICAL ACTIVITY; CATFISH; DPPH RADICAL SCAVENGING ASSAY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME STABILITY; ENZYME SUBSTRATE; HYDROLYSIS; IN VITRO STUDY; NONHUMAN; PROTEIN CONTENT; SKIN; THERMOSTABILITY; VISCERA; ANIMAL; BOVINE; DRUG STABILITY; ENZYMOLOGY; METABOLISM;

ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANIMALS; ANTIOXIDANTS; CATFISHES; CATTLE; DRUG STABILITY; FREE RADICAL SCAVENGERS; GELATIN; HYDROLYSIS; PEPTIDE HYDROLASES; PROTEIN HYDROLYSATES; TRYPSIN; VISCERA;

EID: 84982840420     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2016.07.145     Document Type: Article

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