1. Affinity purification and characterisation of zinc chelating peptides from rapeseed protein hydrolysates: possible contribution of characteristic amino acid residues
- Author
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Wang Zhuochen, Huang Jingjing, Yan Xiaoming, Xie Ningning, Yin Junfeng, Cheng Jianghua, and Bo Li
- Subjects
Protein Hydrolysates ,Electrospray ionization ,Size-exclusion chromatography ,Molecular Sequence Data ,chemistry.chemical_element ,Zinc ,Analytical Chemistry ,Residue (chemistry) ,Affinity chromatography ,Humans ,Chelation ,Amino Acid Sequence ,Amino Acids ,Chelating Agents ,Drug Carriers ,Chromatography ,Brassica rapa ,General Medicine ,chemistry ,Biochemistry ,Sephadex ,Inductively coupled plasma atomic emission spectroscopy ,Chromatography, Gel ,Peptides ,Food Science - Abstract
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.
- Published
- 2014