中国毛虾蛋白水解物中血管紧张素转移酶抑制肽的研究  

Studies of Angiotensin I-converting Enzyme Inhibitory Peptides from Acetes Chinensis Protein Hydrolysate

作　　者：薛勇[1] 薛长湖[1] 许萍[1] 张香治[1] 赵雪[1] 李兆杰[1] 

机构地区：[1]中国海洋大学食品学院,青岛266003

出　　处：《中国食品学报》2006年第5期28-33,共6页Journal of Chinese Institute Of Food Science and Technology

基　　金：国家"863"高技术研究发展项目(No.2004AA6250100);国家"十五"攻关重大专项资助项目(No.2001BA501A26)

摘　　要：目的:采用蛋白酶酶解中国毛虾蛋白,制备具有抑制血管紧张素转移酶(ACE)活性的肽。方法:用黄海黄杆菌低温碱性蛋白酶水解中国毛虾,得到具有ACE抑制活性的酶解物;将中国毛虾蛋白酶解物粗品通过截留分子质量2000Da和1000Da的透析袋透析,再将抑制ACE的活性部分F1继续用SephadexG-15和SP-SephadexC-50分离纯化,取活性最好的峰,最后用反相高压液相C18制备柱纯化得到单一组分FAI。结果:通过氨基酸组成分析及快原子轰击质谱分析,确认FAI为新型血管紧张素转移酶抑制肽Pro-Arg-Tyr。FAI对ACE抑制活性的IC50值为212μmol/L。结论:Pro-Arg-Tyr为一种新型的血管紧张素转移酶抑制肽,其活性较好,结构特点与其它ACE抑制肽相似。Objective： Protease was used to hydrolyse A cetes chinensis protein to prepare peptide which could inhibit angiotensin I-converting enzyme （ACE） . Methods： Hydrolysates with ACE inhibitory activity were obtained from Acetes Chinesnsis prptein using low-tempreture alkaline protease from oceanic microbe F. yellowsea. First, the crude hydrolysate was dialysed with dialyzer molecular-weight cut-off 2 000 Da and 1 000 Da, then fraction F1 which was found to be active segment with ACE inhibitory activity was separated and purified by Sephadex G-15 and SP-Sephadex C-50. The most potent fraction was concentrated and further purified by reverse-phase high-performance liquid chromatography （HPLC） C18 preparative column to get pure sample FAI. Results： FAI was affirmed by amino acid composition analysis and fast atom bombardment MS to be an new ACE inhibitory peptide Pro-Arg-Tyr, whose IC50 value was 212 μmol/L. Conclusiton： Pro-Arg-Tyr with potent activity was found to be a new ACE inhibitory peptides. Structure characteristic of Pro-Arg-Tyr is similar to those of other ACE inhibitory peptides.

关 键 词：中国毛虾 血管紧张素转移酶 黄海黄杆菌低温碱性蛋白酶 分离纯化 

分 类 号：TQ464[化学工程—制药化工]