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Position: Home > Articles > Isolation and Purification of Lactoperoxidase and Its Enzymatic Properties FOOD SCIENCE 2006,27 (2) 100-104

乳过氧化物酶的分离纯化和酶学性质研究

作  者:
卢蓉蓉;许时婴;王璋
单  位:
江南大学食品学院
关键词:
乳过氧化物酶;分离;纯化;酶活
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。
译  名:
Isolation and Purification of Lactoperoxidase and Its Enzymatic Properties
作  者:
LU Rong-rong1,2,XU Shi-ying1,2,WANG Zhang1,2 (1.School of Food Science and Technology, Southern Yangtze University, Wuxi 214036, China; 2.Key Laboratory of Food Science and Safety, Ministry of Education, Southern Yangtze University, Wuxi 214036, China)
关键词:
lactoperoxidase;isolation;purification;enzyme activity
摘  要:
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 lactoperoxidase was 75035D. The recovery of lactoperoxidase activity was 76.17%. The optimum pH for lactoperoxidase 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.

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