Zamani A, Khajavi M. Antioxidative activity of peptide from protein isolate hydrolysate from common kilka (Clupeonella cultriventris caspia) muscle using pyloric caeca enzyme extraction. JFST 2017; 5 (4) :43-56
URL:
http://jfst.modares.ac.ir/article-6-3682-en.html
1- Head of Fisheries Department of Malayer University
Abstract: (9590 Views)
Lipid oxidation is one of the major processes in deterioration of food quality and nutritional value. In this study, antioxidative activity of peptide was determined from hydrolysate of protein isolate from common kilka (Clupeonella cultriventris caspia) muscle using trypsin enzyme of pyloric caeca extraction. The optimum pH and temperature of trypsin enzyme for BAPNA (Nα –benzoyl -DL- argentine – ρ – nitroanilide -HCL) hydrolysis were measured 8.0 and 60 °C, respectively. The finding showed that antioxidative activities determined by DPPH, ABTS radical scavenging activities and ferric reducing antioxidant power (FRAP) increased significantly with variation of degree of hydrolysates from 20 to 40% (p<0.05). The results suggest that trypsin enzyme from pyloric caeca extraction could be a useful tool for peptide production from protein isolate with antioxidant activity and used as an alternative for commercial enzymes such as microbial enzymes in production of protein hydrolysates.
Article Type:
Research Article |
Subject:
Sea food processing Received: 2016/01/23 | Published: 2017/02/19