摘要
分别采用柱色谱技术对K.fragilisLFS-8611β-D-半乳糖苷酶进行了纯化,十二烷基硫酸钠聚丙烯酰胺凝胶电泳(SDS-PAGE)鉴定了该酶的纯度。粗酶先后经过(NH4)2SO4分级沉淀、CM-SepharoseCL-6B、DEAE-SepharoseCL-6B、SephacrylS-200柱色谱四步分离纯化,酶的最终回收率为16%,纯化倍数为45.8。纯化的酶在SDS-PAGE上为一条染色谱带,相对分子质量约为60000。
The β-D-galactosidase from K. fragilis LFS-8611 was purified by chromatography methods, and the purity ofenzyme was identified by sodium dodecyl sulphate polyacrylamide gel electrophoresis(SDS-PAGE). The enzyme was purified about 45.8 fold with a yield of 16% total activity by successive ammonium sulfate-fractionation, CM-Sepharose CL-6B, DEAE-Sepharose CL-6B, and Sephacryl S-200 column chromatography. When the purified enzyme samples were subjected to SDS-PAGE, one single band was observed, which suggested that the enzyme samples were almost pure. The molecular weightestimated for K. fragilis LFS-8611 β-D-galactosidase by PAGE was 60000.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2005年第7期46-49,共4页
Food Science
