Affinity purification and characterisation of zinc chelating peptides from rapeseed protein hydrolysates: Possible contribution of characteristic amino acid residues
文献类型: 外文期刊
第一作者: Xie, Ningning
作者: Xie, Ningning;Huang, Jingjing;Cheng, Jianghua;Wang, Zhuochen;Yin, Junfeng;Yan, Xiaoming;Li, Bo;Li, Bo
作者机构:
关键词: Zinc;Rapeseed protein hydrolysates;Chelating peptides;Immobilized metal affinity chromatography;Alcalase
期刊名称:FOOD CHEMISTRY ( 影响因子:7.514; 五年影响因子:7.516 )
ISSN:
年卷期:
页码:
收录情况: SCI
摘要: Zinc is an essential trace element for human growth and development. In this work, zinc-chelating peptides from rapeseed protein hydrolysates produced with alcalase were investigated by affinity chromatography with immobilized zinc and Sephadex G-25 gel filtration. Four small peptides, namely, Ala-Arg, Asn-Ser-Met (NSM), Gly-Lys-Arg, and Glu-Pro-Ser-His, were obtained and identified by reversed-phase high-performance liquid chromatography and electrospray ionization mass spectrometry. The zinc-chelating ability of the four peptides was further validated by inductively coupled plasma atomic emission spectrometry (ICP-AES). NSM was found to exhibit the highest zinc-chelating rate, which was better than that of reduced glutathione. We speculated that the Asn residue at the amino-terminus might facilitate this zinc-chelating ability. Therefore, utilizing small peptides from rapeseed protein as novel carriers for zinc supplement was feasible. (C) 2014 Elsevier Ltd. All rights reserved.
分类号: TS2`TS201.2
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