工业微生物2019，Vol.49Issue(1)：33-38,6.DOI:10.3969/j.issn.1001-6678.2019.01.006
类芽孢杆菌环果寡糖糖基转移酶的分离纯化和酶学性质
Purification and characterization of cycloinulooligosaccharide fructanotransferase from Paenibacillus sp. Lfos16
摘要
Abstract
The cycloinulo-oligosaccharide fructanotransferase (CFTase) was purified from the cultured medium of Paenibacillus sp. Lfos16 to electrophoretic homogeneity by ammonium sulfate sedimentation, column chromatographies on phenyl-sepharose and DEAE-sepharose. The molecular mass of the enzyme was estimated to be 120 kDa by SDS-PAGE and Native-PAGE, indicating a double-subunit structure. The characterization of CFTase was explored. Maximal activity was observed at 40 ℃ ～ 45 ℃ and pH 7.0. The enzyme was active from pH 5.0 to pH 9.0, at temperatures between 30 and 45 ℃. The catalytic mechanism of CFTase was analyzed and it showed that the CFTase could splite the terminal 6 fructoses from inulin and cyclized them into CFs.关键词
菊糖/环果寡糖糖基转移酶/分离纯化/性质研究Key words
inulin/cycloinulooligosaccharide fructanotransferase/purification/characterization引用本文复制引用
马俊,刘思敏,唐文竹..类芽孢杆菌环果寡糖糖基转移酶的分离纯化和酶学性质[J].工业微生物,2019,49(1):33-38,6.基金项目
辽宁省高等学校基本科研项目(No.2017J030) （No.2017J030）
