猪后腿肉中亮氨酰氨肽酶的纯化与酶学特性研究  

Purification and characterization of leucyl aminopeptidase from pig hind legs

作　　者：赵改名[1] 胡东华[1] 柳艳霞[1] 田玮[1] 赵景丽[1] 高晓平[1] 

机构地区：[1]河南农业大学河南省肉制品加工与质量安全控制重点实验室,河南郑州450002

出　　处：《南京农业大学学报》2013年第5期88-92,共5页Journal of Nanjing Agricultural University

基　　金：国家自然科学基金项目(30972129)

摘　　要：通过匀浆、硫酸铵沉淀、Sephadex G-100凝胶过滤和Phenyl-Sepharose HP疏水层析,从猪后腿肉中分离纯化了一种亮氨酰氨肽酶,并对其部分生化特性进行了研究。结果表明:亮氨酰氨肽酶的得率为12.14%,纯化了77.62倍;亮氨酰氨肽酶的最适温度为40℃左右,最适pH为7.0左右,Mg2+对酶活性有激活作用,Zn2+、Cu2+、Co2+、EDTA和EGTA对酶活性有抑制作用;Ca2+、Fe2+和Mn2+对亮氨酰氨肽酶活性的影响取决于离子浓度,浓度为0.5 mmol·L-1时对酶具有激活作用,而浓度为1.0 mmol·L-1时则表现为抑制作用。A kind of leucyl aminopeptidase was isolated and purified from pig hind legs by using homogenation, ammonium sulfate precipitation, Sephadex G-100 gel filtration and Phenyl-Sepharose HP hydrophobic chromatography, of which some biochemical char- acteristics were investigated. The results showed the purification fold and yield were 77. 62 and 12. 14% , respectively. The aminopeptidase activity was optimal at 40 ℃ and pH 7.0, stimulated by Mg2＋ ions and inhibited by Zn2＋, Cu2＋ , Co2＋ ions and EDTA, EGTA. The effects of Ca2＋, Fe2＋ and Mn2＋ on enzyme activity depended on their different concentrations, which could improve the enzyme activity at the concentration of 0.5 mmol. L^-1 and inhibit at the concentration of 1.0 mmol· L^-1.

关 键 词：猪后腿 亮氨酰氨肽酶 纯化 酶活性 

分 类 号：TS251.1[轻工技术与工程—农产品加工及贮藏工程]