FOOD SCIENCE ›› 2019, Vol. 40 ›› Issue (24): 53-59.doi: 10.7506/spkx1002-6630-20190521-240

• Food Chemistry • Previous Articles     Next Articles

Identification and Metal Chelation Activity of a Copper-Binding Peptide from Rice Globulin Hydrolysate

XING Changrui, CHU Chenlu, ZHANG Xiaoyun, WANG Jinyan, JU Xingrong, YUAN Jian   

  1. (College of Food Science and Engineering, Collaborative Innovation Center for Modern Grain Circulation and Safety, Key Laboratory of Grains and Oils Quality Control and Processing, Nanjing University of Finance and Economics, Nanjing 210023, China)
  • Online:2019-12-25 Published:2019-12-24

Abstract: Four rice proteins were obtained by sequential extraction, and their metal element contents were determined. Rice globulin was selected from these proteins for hydrolysis by pepsin, and the hydrolysate was purified by ultrafiltration. The fraction containing polypeptides was collected and detected by mass spectrometry (MS). A total of 23 polypeptides with molecular mass ranging from 725 to 1 409 Da were obtained through software analysis. Based on the data reported in the literature, the polypeptides QGWSSSSE and YYGGEGSSSEQGY may have potential metal chelation activity. The Cu2+ chelation activity of the two synthetic polypeptides was compared with that of EDTA, citric acid and metallothionein. It was found that YYGGEGSSSEQGY had a better Cu2+ chelation activity than QGWSSSSE. The IC20 of YYGGEGSSSEQGY was 5.40 mmol/L, which was comparable to that of citric acid in a low concentration range, but was worse than EDTA and metallothionein. Furthermore, these two polypeptides could more strongly bind Fe2+ than other metal ions. Amino acid composition analysis showed that continuous serine SS, SSS, and SSSS may be associated with the copper-binding activity.

Key words: rice globulin, copper-binding peptide, metal chelation activity

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