title: Fish skin gelatin hydrolysates produced by visceral peptidase and bovine trypsin: Bioactivity and stability.
abstract: The peptidase from the viscera of farmed giant catfish was used for producing gelatin hydrolysates (HG) and compared with those produced from commercial bovine trypsin (HB). The degree of hydrolysis (DH) observed suggests that proteolytic cleavage rapidly occurred within the first 120min of incubation, and there was higher DH in HG than in HB. HG demonstrated the highest ACE-inhibitory activity, DPPH, ABTS radical scavenging activity, and FRAP. HB showed the highest FRAP activity. The DPPH radical scavenging activity of HG was quite stable over the pH range of 1-11, but it increased slightly when the heating duration time reached 240min at 100°C. The ACE-inhibitory activity of HG showed the highest stability at a pH of 7, and it remained very stable at 100°C for over 15-240min. The visceral peptidase from farmed giant catfish could be an alternative protease for generating protein hydrolysates with desirable bioactivities. The resulting hydrolysates showed good stability, making them potential functional ingredients for food formulations.
authors.affiliation: Program of Food Technology, School of Agro-Industry, Mae Fah Luang University, Chiang Rai 57100, Thailand.
authors.forename: Sunantha
authors.initials: S
authors.lastname: Ketnawa
authors.affiliation: Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla 90112, Thailand.
authors.forename: Soottawat
authors.initials: S
authors.lastname: Benjakul
authors.affiliation: Department of Products, Institute of Food Science, Technology and Nutrition (ICTAN-CSIC), Jose Antonio Novais, 10, Madrid 28040, Spain.
authors.forename: Oscar
authors.initials: O
authors.lastname: Martínez-Alvarez
authors.affiliation: Program of Food Technology, School of Agro-Industry, Mae Fah Luang University, Chiang Rai 57100, Thailand. Electronic address: saroat@mfu.ac.th.
authors.forename: Saroat
authors.initials: S
authors.lastname: Rawdkuen
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors; D000818:Animals; D000975:Antioxidants / Q000494:pharmacology; D002397:Catfishes; D002417:Cattle; D004355:Drug Stability; D016166:Free Radical Scavengers; D005780:Gelatin / Q000378:metabolism* / Q000494:pharmacology; D006868:Hydrolysis; D010447:Peptide Hydrolases / Q000378:metabolism*; D011492:Protein Hydrolysates / Q000378:metabolism* / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism*; D014781:Viscera / Q000201:enzymology*
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D000975:Antioxidants; D016166:Free Radical Scavengers; D011492:Protein Hydrolysates; D005780:Gelatin; D010447:Peptide Hydrolases; D014357:Trypsin
keywords: Angiotensin I-converting enzyme inhibitory; Antioxidative; Gelatin hydrolysates; Giant catfish; Peptidase; Stability