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

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 120 min 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 240 min 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 15–240 min. 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.

Bibliographic Details

Main Authors:	Ketnawa, Sunantha, Benjakul, Soottawat, Martínez Álvarez, Óscar, Rawdkuen, Saroat
Other Authors:	Mae Fah Luang University
Format:	artículo biblioteca
Published:	Elsevier 2017
Subjects:	Gelatin hydrolysates, Antioxidative, Peptidase, Stability, Giant catfish, Angiotensin I-converting enzyme inhibitory,
Online Access:	http://hdl.handle.net/10261/171331 http://dx.doi.org/10.13039/501100004396 http://dx.doi.org/10.13039/501100004154
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