Purification and characterisation of a zinc-binding peptide from oyster protein hydrolysate

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• 作者：Da Chen¹ ; Zunying Liu¹ ; Wenqian Huang ; Yuanhui Zhao ; Shiyuan Dong ; Mingyong Zeng ; ^{mingyz@ouc.edu.cn}
• 关键词：Zinc-binding peptide ; Oyster protein ; Hydrolysates ; Immobilised metal affinity chromatography
• 刊名：Journal of Functional Foods
• 出版年：2013
• 出版时间：April, 2013
• 年：2013
• 卷：5
• 期：2
• 页码：689-697
• 全文大小：1022 K

文摘

A novel zinc-binding peptide produced from oyster protein hydrolysis using pepsin was purified and characterised. The hydrolysate was fractionated by immobilised metal ion affinity chromatography (IMAC-Zn²⁺). The zinc-binding peptide identified by reverse-phase high-pressure liquid chromatography (RP-HPLC) and sequenced by liquid chromatography (LC/LTQ) mass spectrometry (sequence from N to C terminal) had a molecular weight of 1882.0 Da. The zinc-binding capacity of the peptide (HLRQEEKEEVTVGSLK) was 6.56 |? mg^?1 and it was preserved at 85.98 % of its original level upon in vitro simulated digestion. The UV-vis and FTIR spectra demonstrate that the amino nitrogen atoms and the oxygen atoms belonging to the carboxylate groups are the primary binding sites for Zn²⁺. The results provide a feasible approach to isolate zinc-binding peptides and contribute to clarification of binding mechanism between zinc and peptides.