Preparation, purification and identification of iron-chelating peptides derived from tilapia (Oreochromis niloticus) skin collagen and characterization of the peptide-iron complexes

文献类型： 外文期刊

第一作者： Lin, Shanting

作者： Lin, Shanting;Hu, Xiao;Li, Laihao;Yang, Xianqing;Chen, Shengjun;Wu, Yanyan;Yang, Shaoling;Li, Laihao;Yang, Xianqing;Lin, Shanting

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关键词： Tilapia skin collagen hydrolysate; Iron-chelating peptides; Peptide-iron complexes; Structure; Bio-accessibility

期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：4.952； 五年影响因子：5.383 ）

ISSN： 0023-6438

年卷期： 2021 年 149 卷

页码：

收录情况： SCI

摘要： Tilapia skin collagen was hydrolyzed by five proteases (trypsin, pepsin, neutral protease, alkaline protease and protamex). The results showed that the tilapia skin collagen hydrolysate (TSCH) obtained by 2 h hydrolysis with trypsin exhibited the highest iron chelating rate. The TSCH was then separated by immobilized metal affinity chromatography (IMAC-Fe2+) and obtained the tilapia skin collagen iron-chelating peptides (TSCICP). The iron chelating sites of TSCICP were corresponding to carboxylic groups of Asp/Glu and guanidine nitrogen of Arg/Lys. After chelated with iron ions, TSCICP was folded and aggregated to form spherical particles with increased particle size. The TSCICP-iron complexes could maintain high iron solubility at various pH and in simulated gastrointestinal digestion. The iron bio-accessibility of TSCICP-iron complexes was high than that of ferrous glycinate and ferrous sulfate. Finally, TSCICP was purified by RP-HPLC and identified by LC-MS/MS. Four ironchelating peptides were identified as GPAGPAGEK (782.39 Da), DGPSGPKGDR (984.46 Da), GLPGPSGEEGKR (1198.59 Da) and DGPSGPKGDRGETGL (1441.68 Da). These results indicating that the iron-chelating peptides derived from tilapia skin collagen could be used as potential dietary iron supplement.

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