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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)
  • Received : 2015.06.26
  • Accepted : 2015.07.21
  • Published : 2015.09.30

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

Acknowledgement

Supported by : Chonnam National University

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