食品与发酵工业2017，Vol.43Issue(7)：93-97,5.DOI:10.13995/j.cnki.11-1802/ts.013274
酪蛋白磷酸肽锌螯合肽的分离及结构性质表征
Separation and structure characterizations of zinc-binding peptide from Casein Phosphopeptides
阚文翰 1纪晓雯 1王玉婷 1梅林 1王志耕1
作者信息
- 1. 安徽农业大学茶与食品科技学院,安徽合肥,230036
- 折叠
摘要
Abstract
Casein Phosphopeptides (Casein Phosphopeptides,referred to as CPPs) is a class of polypeptides which has divalent metal chelating activity.The theory and practical significance of CPPs is its specific nutrient chelated.CPPs was obtained by enzymatic hydrolysis,and separated Q strong anion exchange chromatography and reverse phase preparative chromatography (RP-HPLC);it had highly active zinc chelate peptide(CPP-Zn).Its structural was analyzed by proportion of amino acids、UV-VIS spectra、infrared spectroscopy、13C NMR spectra、1H NMR spectra and 31p NMR spectra.Result:CPP purified from continuous chromatographic separation had strong zinc chelating ability of 88.68ug / mg.Structure analysis showed CPP structure and proportion of amino acids before and after chelation significantly changed.The phosphate groups are involved in the chelation,-COOH、-NH2 and-OH in P-OH were the primary binding site.关键词
酪蛋白磷酸肽/分离/锌/螯合/结构Key words
Casein Phosphopeptides/isolated/zinc/chelate/structure引用本文复制引用
阚文翰,纪晓雯,王玉婷,梅林,王志耕..酪蛋白磷酸肽锌螯合肽的分离及结构性质表征[J].食品与发酵工业,2017,43(7):93-97,5.
