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
作者： Xie, Ningning 1 ; Huang, Jingjing 1 ; Li, Bo 2 ; Cheng, Jianghua 1 ; Wang, Zhuochen 1 ; Yin, Junfeng 1 ; Yan, Xiaoming 1 ;
作者机构： 1.Anhui Acad Agr Sci, Inst Agrofood Sci & Technol, Hefei 230031, Peoples R China
2.China Agr Univ, Coll Food Sci & Nutr Engn, Beijing 100083, Peoples R China
3.Minist Educ, Key Lab Funct Dairy, Beijing 100083, Peoples R China
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 ）
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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.
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