摘要
采用超滤-离子交换色谱分步洗脱法,对牛初乳中的乳过氧化物酶进行了分离和纯化。经SDS-PAGE测定,分离出的乳过氧化物酶显示为单一区带,相对分子质量为75035D。该酶酶活回收率为76.17%,其最适pH为5.0～5.5,最适温度为55℃。在70℃、75℃时LP酶活的热失活曲线呈现一般植物过氧化物酶失活的双相特征。
A stepwise procedure for isolation and purification of lactoperoxidase by ultrafiltration and ion exchange chromatography was investigated. It was shown as a single band in SDS-PAGE. The molecular weight of lactopemxidase was 75035D. The recovery of lactoperoxidase activity was 76. t7%. The optimum pH for tactoperoxidase was 5.0-5.5, and the optimum temperature for lactoperoxidase was 55℃. At 70℃ and 75℃, two independent first-order inactivation reactions were found just as the peroxidases from plants.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2006年第2期100-104,共5页
Food Science
关键词
乳过氧化物酶
分离
纯化
酶活
lactoperoxidase
isolation
purification
enzyme activity
