Affinity purification and characterisation of zinc chelating peptides from rapeseed protein hydrolysates: Possible contribution of characteristic amino acid residues

作者：Xie Ningning^*; Huang Jingjing; Li Bo; Cheng Jianghua; Wang Zhuochen; Yin Junfeng; Yan Xiaoming

来源：Food Chemistry, 2015, 173: 210-217.

DOI：10.1016/j.foodchem.2014.10.030

• Zinc
• Rapeseed protein hydrolysates
• Chelating peptides
• Immobilized metal affinity chromatography
• Alcalase

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.

• 出版日期2015-4-15
• 单位安徽省农业科学院; 中国农业大学