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http://dx.doi.org/10.3746/pnf.2015.20.3.176

Abalone Protein Hydrolysates: Preparation, Angiotensin I Converting Enzyme Inhibition and Cellular Antioxidant Activity  

Park, Soo Yeon (School of Food Technology and Nutrition, Chonnam National University)
Je, Jae-Young (Department of Marine-Bio Convergence Science, Pukyong National University)
Hwang, Joung-Youl (Korea Abalone Laboratory)
Ahn, Chang-Bum (School of Food Technology and Nutrition, Chonnam National University)
Publication Information
Preventive Nutrition and Food Science / v.20, no.3, 2015 , pp. 176-182 More about this Journal
Abstract
Abalone protein was hydrolyzed by enzymatic hydrolysis and the optimal enzyme/substrate (E/S) ratios were determined. Abalone protein hydrolysates (APH) produced by Protamex at E/S ratio of 1:100 showed angiotensin I converting enzyme inhibitory activity with $IC_{50}$ of 0.46 mg/mL, and APH obtained by Flavourzyme at E/S ratio of 1:100 possessed the oxygen radical absorbance capacity value of $457.6{\mu}M$ trolox equivalent/mg sample. Flavourzyme abalone protein hydrolysates (FAPH) also exhibited $H_2O_2$ scavenging activity with $IC_{50}$ of 0.48 mg/mL and $Fe^{2+}$+ chelating activity with $IC_{50}$ of 2.26 mg/mL as well as high reducing power. FAPH significantly (P<0.05) protected $H_2O_2$-induced hepatic cell damage in cultured hepatocytes, and the cell viability was restored to 90.27% in the presence of FAPH. FAPH exhibited 46.20% intracellular ROS scavenging activity and 57.89% lipid peroxidation inhibition activity in cultured hepatocytes. Overall, APH may be useful as an ingredient for functional foods.
Keywords
abalone; angiotensin I converting enzyme; antioxidant; enzymatic hydrolysis;
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