Abstract：In order to analyze the binding characteristics of rice globulin and metal elements, four types of rice proteins were obtained by sequential extraction method, and metal elements in them were determined. The rice globulin is selected to be hydrolyzed by pepsin, and the hydrolysates are purified by ultrafiltration. A mixed polypeptide solution with molecular weight less than 3000 was collected. The obtained hydrolysates was detected by mass spectrometry and 23 polypeptides were obtained based on software analysis, with molecular weight ranged from 725 to 1409. Based on reported literatures, polypeptides, QGWSSSSE and YYGGEGSSSEQGY, may have potential metal chelation activity. Their chelation activity with Cu2+ was compared using two synthetic polypeptides and compared with that of EDTA, citric acid and metallothionein. It was found that YYGGEGSSSEQGY has better Cu2+ chelation activity than QGWSSSSE. The IC20 of YYGGEGSSSEQGY was 5.40 mM, which was comparable to citric acid in low concentration range, and worse than EDTA and metallothionein. Further analysis, the chelation experiments between these two peptides and other metal ions showed that they could strongly bind to Fe2+. By amino acid analysis, continuous serine SS, SSS, and SSSS may be associated with copper binding activity.