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虾头自溶产物中ACE抑制肽的分离鉴定     被引量:7

Isolation and identification of ACE inhibitory peptides from the autolysis product of shrimp head(Litopenaeus vannamei)

文献类型:期刊文献

中文题名:虾头自溶产物中ACE抑制肽的分离鉴定

英文题名:Isolation and identification of ACE inhibitory peptides from the autolysis product of shrimp head(Litopenaeus vannamei)

作者:朱国萍[1];章超桦[2,3];曹文红[2,3];吉宏武[2,3]

机构:[1]广东海洋大学分析测试中心;[2]广东海洋大学广东省水产加工与安全重点实验室;[3]广东海洋大学食品科技学院

年份:2013

卷号:37

期号:4

起止页码:631

中文期刊名:水产学报

外文期刊名:Journal of Fisheries of China

收录:CSTPCD、、北大核心2011、Scopus、北大核心、CSCD、CSCD2013_2014

基金:国家科技支撑计划项目(2007BAD29B09);教育部科学技术重点项目(210155);国家虾产业技术体系专项(CARS-47)

语种:中文

中文关键词:虾头自溶产物;ACE抑制肽;色谱层析;RP-HPLC;电喷雾质谱;氨基酸序列

外文关键词:shrimp head autolysate;ACE inhibitory peptide;chromatography;RP-HPLC;electrospray ionization mass spectrometry;amino acid sequence

中文摘要:虾头在一定的条件下发生自溶作用,其所含蛋白质以肽和氨基酸等形式释放出来,有些肽产物具有ACE抑制活性。实验采用8 000、5 000和3 000 u的超滤膜分级分离虾头自溶产物,活性检测结果表明,ACE抑制肽主要分布在3 000 u超滤组分中;3 000 u超滤组分进一步经Sephadex G-25葡聚糖凝胶层析、SP Sephadex C-25离子交换层析及Sephadex G-15葡聚糖凝胶层析纯化,ACE抑制活性提高将近8倍(IC50=0.19 mg/mL);Sephadex G-15葡聚糖凝胶层析收集的高活性成分再经两次RP-HPLC纯化,分离纯化得到两条ACE抑制肽,质谱分析推测其氨基酸序列为Tyr-Pro和Leu-Pro/Ile-Pro,分子量分别为279和229 u。

外文摘要:Shrimp head is susceptible to autolysis under certain conditions,the protein in it is degraded into soluble protein,peptides and amino acids,and some peptides are active peptides which can inhibit the ACE enzyme activity.At present,many ACE inhibitory peptides derived from food protein have been developed.In the present study,two ACE inhibitory peptides(Tyr-Pro and Leu-Pro/Ile-Pro)were highly purified from the shrimp head(Litopenaeus vannamei)autolysate by extra fine membrane and a series of column chromatographies.In the first autolysis solution of shrimp head was consecutively extracted through extra fine membrane with molecular weight cut-offs(MWCO)at 8,5,3 ku,respectively.The active results shown that filtrate through MWCO at 3 000 u had the highest ACE inhibitory activity.The crude filtrate through MWCO at 3 ku was purified by Sephadex G-25 gel chromatography,SP Sephadex C-25 anion-exchange chromatography as well as Sephadex G-15 gel chromatography,respectively.After that,the ACE inhibitory activity of purified filtrate almost increased by 8 times(IC50=0.19 mg/mL)that of crude filtrate.The high active collected fraction from Sephadex G-15 gel chromatography was carried out by RP-HPLC(High-Performance Liquid Chromatography)twice for the further purification and two kinds of dipeptide were obtained,and the identification of dipeptide by mass spectra showed that they were Tyr-Pro and Leu-Pro/Ile-Pro,and the molecular weight was 279 u and 229 u,respectively.

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