Enzymatic hydrolysis of grass carp myofibrillar protein and antioxidant properties of hydrolysates

Jiaoyan Ren, Haiyan Wang, Mouming Zhao, Chun Cui and Xiao Hu
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Jiaoyan Ren: College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, P. R. China
Haiyan Wang: Technical Center of Shanghai Tobacco (Group) Corp., Shanghai, P. R. China
Mouming Zhao: College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, P. R. China
Chun Cui: College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, P. R. China
Xiao Hu: College of Light Industry and Food Sciences, South China University of Technology, Guangzhou, P. R. China

Czech Journal of Food Sciences, 2010, vol. 28, issue 6, 475-484

Abstract: Myofibrillar protein was extracted from grass carp, a freshwater fish, and hydrolysed using five commercial proteases (papain, pancreatin 6.0, bromelain, Neutrase 1.5MG, and Alcalase 2.4 L). The antioxidant activities of the hydrolysates were determined. Pancreatin 6.0 proved to be the most efficient protease for hydrolysing myofibrillar protein with a very high protein recovery (90.20%), its hydrolysates exhibiting the highest hydroxyl radical (*OH) scavenging activity (IC50 = 349.89 ± 11.50 μg/ml) out of all five hydrolysates. Molecular weight distribution analysis revealed that pancreatin 6.0 hydrolysate rendered a higher proportion of the 6-10 kDa fraction and a lower proportion of the 3-6 kDa fraction as compared with other hydrolysates. The maximum *OH scavenging activity for pancreatin 6.0 hydrolysate (IC50 = 229.90 µg/ml) was obtained at the enzyme to substrate ratio of 0.52%, the incubation time of 7.03 h, and the incubation temperature of 50.56°C, as optimised by response surface methodology. In vitro antioxidant experiments proved that pancreatin 6.0 hydrolysates had obvious inhibitory effects on lipid peroxidation and low-density lipoproteins oxidation under optimised conditions.

Keywords: grass carp; myofibrillar protein; proteolysis; oxidation; inhibition; response surface methodology (search for similar items in EconPapers)
Date: 2010
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Persistent link: https://EconPapers.repec.org/RePEc:caa:jnlcjf:v:28:y:2010:i:6:id:343-2009-cjfs

DOI: 10.17221/343/2009-CJFS

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