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 chromatogra...
【基金】
安徽省科技计划项目(12Z0102055)
【更新日期】
2018-04-09
【分类号】
TS201.2
【正文快照】
引文格式:纪晓雯,王志耕,阚文翰,等.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.DOI:10.7506/spkx1002-6630-201806011.http://www.spkx.net.cnJI Xiaowen,WANG Zhigeng,KAN Wenhan,et al.Isolation,purification and structural analysis of iron-bind