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Mineral Ion Chelating Activity of Enzymatic Protein Hydrolysates from Decapterus maruadsi Muscle

YANG Yiran1,2, HU Xiao1, YANG Xianqing1,*, LI Laihao1, CHEN Shengjun1, WU Yanyan1, LIN Wanling1, HUANG Hui1, MA Haixia1   

  1. 1. Key Laboratory of Aquatic Producut Processing, Ministry of Agriculture, National R&D Center for Aquatic Product Processing, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciencces, Guangzhou 510300, China; 2. College of Food Science and Engineering, Dalian Ocean University, Dalian 116023
  • Online:2017-02-15 Published:2017-02-28

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Abstract: In this research, we studied the chelating activity of Decapterus maruadsi muscle hydrolyzed by three different proteases, trypsin, papain and alcalase, towards Ca2+, Fe2+ and Zn2+. The results showed that the hydrolysates produced by trypsin (DH = 23.14%) had the highest chelating activity towards Fe2+ and Zn2+ with chelating rates of 96.63% and 94.28%, respectively. The hydrolysates by papain (DH = 22.0%) had the highest Ca2+ chelating activity with a chelating rate of 96.78%. It was also shown that both enzymatic hydrolysates had good antioxidant activity. The half maximal inhibitory concentration (IC50) values of the trypsin and papain hydrolysates for 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging activity were 3.74 and 3.64 mg/mL, respectively. In addition, the amino acid sequence analysis showed that the hydrolysates with higher contents of Glu, Asp and Lys had higher mineral ion chelating activity.

Key words: Decapterus maruadsi, hydrolysate, chelating activity, mineral ions, antioxidant

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