Keywords
Rice Globulin, Copper Ion-Binding Peptide, Chelating Activity
Abstract
In order to analyze the binding characteristics of rice globulin and metal elements, four kinds of rice proteins were obtained through fractionated extraction method, and their metal element contents were determined. Rice globulin was selected and enzymatically hydrolyzed by pepsin, and the enzymatic hydrolyzate was purified by ultrafiltration. The obtained hydrolyzate was subjected to mass spectrometry detection, and 23 polypeptide sequences were obtained through software analysis, with molecular masses ranging from 725 to 1 409 Da. Combined with reported related studies, the peptide sequences QGWSSSSE and YYGGEGSSSEQGY were analyzed to have potential metal chelating activity. By artificially synthesizing these two polypeptide sequences, and selecting ethylenediaminetetraacetic acid (EDTA), citric acid and metallothionein as reference substances, we compared their chelating activities with Cu2+. The results showed that YYGGEGSSEQGY is better than QGWSSSSE in chelating Cu2+. The IC20 of chelating Cu2+ is 5.40 mmol/L, and is equivalent to citric acid in the low concentration range and worse than EDTA and metallothionein. Further analysis showed that the chelating activity between these two polypeptides and other metal ions was found to be stronger binding to Fe2+. Through amino acid analysis, the consecutive serines SS, SSS and SSSS may be related to the chelating activity of copper
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Original research done by Chu Chenlu, Zhang Xiaoyun, Wang Jinyan, Yuan Jian, Xing Changrui, Ju Xingrong
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