A novel sucrose phosphorylase from the metagenomes of sucrose-rich environment: isolation and characterization

A novel sucrose phosphorylase from the metagenomes of sucrose-rich environment: isolation and characterization
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来自富含蔗糖环境的宏基因组的新型蔗糖磷酸化酶:分离和表征

DOI:
10.1007/s11274-012-1098-y
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发表时间:
2012-06
影响因子:
4.1
通讯作者:
Huang, Ribo
Huang, Ribo
中科院分区:
工程技术3区
文献类型:
--
作者:
Du, Liqin;Yang, Hui;Huo, Yunlong;Wei, Hang;Xu, Yuanjin;Wei, Yutuo;Huang, Ribo

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蔗糖磷酸化酶是一种主要参与通用淀粉和蔗糖途径的重要酶,由于其转糖基化活性,研究人员现在引起了研究人员的注意。一种新型的蔗糖磷酸化酶,Uncpase已被分离,其T
Sucrose phosphorylase, an important enzyme mainly involved in the generic starch and sucrose pathways, has now caught the attention of researchers due to its transglycosylation activity. A novel sucrose phosphorylase, unspase, has been isolated, and its transglycosylation properties were characterized. Compared with Bisp, the sucrose phosphorylase fromBifidobacterium adolescentis, unspase had two deleted regions in itsC-terminal. These deleted regions were probably equivalent to the important five-stranded anti-parallel β-sheet domain in sucrose phosphorylase. Unspase has a kmof 21.12 mM, a Vmaxof 69.24 μmol min−1mg−1and a kcatof 31.19 s−1with sucrose as substrate. In 3-(N-morpholino) propanesulfonic acid (MOPS) buffer, unspase transferred the glycosyl moiety tol-arabinose,d-fructose andl-sorbose. Much to our surprise, unspase can catalyze the transglycosylation in which a glycosyl moiety was transferred tol-arabinose in the presence of phosphate, which is an interesting exception to the generally accepted fact that transglycosylation can only occur under the condition of phosphate absence. The final yield of the transglycosylation product (37.9 %) in phosphate buffer was even higher than that (5.8 %) in MOPS buffer. This is a novel phenomenon that a sucrose phosphorylase can catalyze a transglycosylation reaction in the presence of phosphate.
DOI: 10.1271/bbb.60.322
发表时间: 1996-02
期刊: Bioscience, biotechnology, and biochemistry
影响因子: --
作者:
Haruhiko Kawasaki;Narutoshi Nakamura;Masaaki Ohmori;Takuo Sakai
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