食品科学2018，Vol.39Issue(6)：63-68,6.DOI:10.7506/spkx1002-6630-201806011
酪蛋白铁螯合肽的分离纯化及结构解析
Isolation, Purification and Structural Analysis of Iron-Binding Peptides from Casein Hydrolysate
摘要
Abstract
Iron-binding peptides from tryptic casein hydrolysate were separated by immobilized metal affinity chromatography or anion exchange chromatography followed by purification by Sephacryl S-100 HR gel chromatography.The purified peptide was structurally elucidated by UV-Vis spectroscopy,Fourier transform infrared (FT-IR) spectroscopy and liquid chromatography-tandem mass spectrometry (LC-MS/MS).The results showed that a fraction with high iron chelating capacity of 39.56 μg/mg purified by affinity chromatography followed by gel filtration chromatography was obtained,which was better than that purified by anion exchange chromatography.The formation of peptide-iron chelate was confirmed by UV-Vis and FT-IR spectra,and some changes at the carboxyl site occurred after chelating.Besides,three peptide fragments were identified by MS,whose amino acid sequences were HIQKEDVPSER,ITVDDKHYQK and TRLHPVQER,respectively.Asp,Glu and Gln were found to be abundant in these peptide fragments with each of them containing carbonyl group,suggesting that the carbonyl site of the peptide is among the main iron-binding sites.关键词
酪蛋白/铁/螯合肽/纯化/结构Key words
casein/iron/chelating peptide/purification/structure分类
轻工纺织引用本文复制引用
纪晓雯,王志耕,阚文翰,梅林,薛秀恒..酪蛋白铁螯合肽的分离纯化及结构解析[J].食品科学,2018,39(6):63-68,6.基金项目
安徽省科技计划项目(12Z0102055) （12Z0102055）
