高螯合锌活性的酪蛋白磷酸肽分离及结构性质表征
详细信息 查看官网全文
- 英文论文题名：Isolation and characterization of casein phosphopeptides with high chelating activity
- 论文作者：阚文翰 ; 梅林 ; 薛秀恒 ; 纪晓雯 ; 王志耕
- 英文论文作者：Kan Wenhan ; Mei Lin ; Xue Xiuheng ; Ji Xiaowen ; Wang Zhigeng ; Tea and Food Science academy ; Anhui Agriculture University ; Anhui agriculture product Engineering Laboratory
- 年：2016
- 作者机构：安徽农业大学茶与食品科技学院;安徽省农产品加工工程实验室;
- 论文关键词：酪蛋白磷酸肽 ; 分离 ; 锌螯合肽 ; 结构
- 英文论文关键词：casein phosphopeptides ; isolated ; zinc chelating peptide ; structure
- 会议召开时间：2016-11-09
- 会议录名称：中国食品科学技术学会第十三届年会论文摘要集
- 英文会议录名称：Abstracts of the 13th Annual Meeting of CIFST
- 语种：中文
- 分类号：TS201.2
- 学会代码：ZGSP
- 会议名称：中国食品科学技术学会第十三届年会
- 会议地点：中国北京
- 主办单位：中国食品科学技术学会
- 学会名称：中国食品科学技术学会
- 页数：2
- 文件大小：107k
- 原文格式：O
- 会议级别：全国
摘要
酪蛋白磷酸肽是一类具有二价金属元素螯合活性的多肽集,酶解酪蛋白获得酪蛋白磷酸肽(CaseinPhosphopeptides,简称CPP),通过连续色谱手段分离出高螯合锌活性的肽,再通过结构表征研究其螯合锌离子的特性。采用碱性蛋白酶酶水解酪蛋白制备酪蛋白磷酸肽,通过Q强阴离子交换色谱、透析和C_(18)反相制备色谱连续分离酪蛋白磷酸肽,得到特异性锌螯合肽。运用核磁共振氢谱、磷谱以及红外光谱表征分析肽螯合锌离子的特性。结果表明,设计的连续色谱方案,可从酪蛋白酶解液中获得高螯合锌能力的酪蛋白磷酸肽,命名为CP-18,其锌螯合活性达88.68ug/mg。表征分析发现螯合前后CPP结构变化明显,酪蛋白磷酸肽链中的磷酸丝氨酸残基可能是螯合锌离子的主要基团,其主要结合位点是-COOH中的羰基及-NH_2。试验研究结果为高活性酪蛋白磷酸肽锌制备提供理论依据。
CaseinPhosphopeptides is a class of polypeptides set which haveactivity to chelate with divalent metal element,the casein phosphopeptides obtained by enzymatic hydrolysis(CaseinPhosphopeptides,referred to as CPP),by means of a continuous chromatographic separation and find out strongest zinc chelate peptide,again through structural characterization to study the properties of zinc chelate.Firstlyusing the degradation catalysed with alkaline proteasein casein to obtainCPP then using Q strong anion exchange chromatography,dialysis and C18 reverse phase preparative chromatography to gain the specific peptide chelating zinc,and under~1H NMR and ~(31)P NMR spectroscopy and infrared spectroscopy to characterizezinc chelating properties.In result,CPP purified from continuous chromatographic separation have strong zinc chelating ability,named CP-18,its zinc chelate activity up to 88.68 ug /mg,structure identification was found CPP chelation structure before and after significantly changed,phosphoserine residues in peptide chain are likely to be a major group of chelating zinc ions,carbonyl group in-COOH and-NH_2 were the primary binding site.This conclusion can be the production and application of high-activity CPP chelating zinc.
CaseinPhosphopeptides is a class of polypeptides set which haveactivity to chelate with divalent metal element,the casein phosphopeptides obtained by enzymatic hydrolysis(CaseinPhosphopeptides,referred to as CPP),by means of a continuous chromatographic separation and find out strongest zinc chelate peptide,again through structural characterization to study the properties of zinc chelate.Firstlyusing the degradation catalysed with alkaline proteasein casein to obtainCPP then using Q strong anion exchange chromatography,dialysis and C18 reverse phase preparative chromatography to gain the specific peptide chelating zinc,and under~1H NMR and ~(31)P NMR spectroscopy and infrared spectroscopy to characterizezinc chelating properties.In result,CPP purified from continuous chromatographic separation have strong zinc chelating ability,named CP-18,its zinc chelate activity up to 88.68 ug /mg,structure identification was found CPP chelation structure before and after significantly changed,phosphoserine residues in peptide chain are likely to be a major group of chelating zinc ions,carbonyl group in-COOH and-NH_2 were the primary binding site.This conclusion can be the production and application of high-activity CPP chelating zinc.
引文