Isolation and characterization of zinc-binding peptides from mung bean protein hydrolysates
作者： Tianxin Fu , Shu Zhang , Yanan Sheng , Yuchao Feng , Yingjun Jiang
DOI: 10.1007/S00217-019-03397-8
关键词: Amide 、 Chelation 、 Peptide sequence 、 Ingredient 、 Ultrafiltration 、 Nitrogen 、 Chromatography 、 Absorption (chemistry) 、 Chemistry 、 Peptide
摘要: The aim of this study was to isolate, purify, and characterize a novel peptide with zinc-binding ability from mung bean protein hydrolysates obtained by alcalase. purification process performed using ultrafiltration, TSK-GEL size-exclusion chromatography, reversed-phase high-performance liquid chromatography (RP-HPLC). molecular weight the isolated determined chromatography–electrospray ionization mass spectrometry (LC–ESI/MS) found be 1192.56 Da amino acid sequence SSEDQPFNLR. identified showed capacity 80.82 mg/g, which is 55.09% higher than that original hydrolyzate. Moreover, UV–vis FTIR spectra indicated sites on were nitrogen atoms amide, terminal group, oxygen carboxyl group. zinc-releasing experiments peptide–zinc chelate highly soluble under both acidic alkaline conditions. Furthermore, significantly promoted transportation absorption zinc ions in Caco-2 cell model. These findings indicate potential for production utilization as ingredient functional foods.
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