Isolation, Purification and Structural Analysis of Iron-Binding Peptides from Casein Hydrolysate

doi:10.7506/spkx1002-6630-201806011

Abstract

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.

Key words: casein, iron, chelating peptide, purification, structure

CLC Number:

TS252

JI Xiaowen, WANG Zhigeng, KAN Wenhan, MEI Lin, XUE Xiuheng. Isolation, Purification and Structural Analysis of Iron-Binding Peptides from Casein Hydrolysate[J]. FOOD SCIENCE, 2018, 39(6): 63-68.

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Isolation, Purification and Structural Analysis of Iron-Binding Peptides from Casein Hydrolysate

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