CLC number: Q814
On-line Access: 2024-08-27
Received: 2023-10-17
Revision Accepted: 2024-05-08
Crosschecked: 2010-10-11
Cited: 2
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Qing-bao Ding, Ling Ou, Dong-zhi Wei, Xiao-kun Wei, Yan-mei Xu, Chun-yan Zhang. Enzymatic synthesis of nucleosides by nucleoside phosphorylase co-expressed in Escherichia coli[J]. Journal of Zhejiang University Science B, 2010, 11(11): 880-888.
@article{title="Enzymatic synthesis of nucleosides by nucleoside phosphorylase co-expressed in Escherichia coli",
author="Qing-bao Ding, Ling Ou, Dong-zhi Wei, Xiao-kun Wei, Yan-mei Xu, Chun-yan Zhang",
journal="Journal of Zhejiang University Science B",
volume="11",
number="11",
pages="880-888",
year="2010",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B1000193"
}
%0 Journal Article
%T Enzymatic synthesis of nucleosides by nucleoside phosphorylase co-expressed in Escherichia coli
%A Qing-bao Ding
%A Ling Ou
%A Dong-zhi Wei
%A Xiao-kun Wei
%A Yan-mei Xu
%A Chun-yan Zhang
%J Journal of Zhejiang University SCIENCE B
%V 11
%N 11
%P 880-888
%@ 1673-1581
%D 2010
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1000193
TY - JOUR
T1 - Enzymatic synthesis of nucleosides by nucleoside phosphorylase co-expressed in Escherichia coli
A1 - Qing-bao Ding
A1 - Ling Ou
A1 - Dong-zhi Wei
A1 - Xiao-kun Wei
A1 - Yan-mei Xu
A1 - Chun-yan Zhang
J0 - Journal of Zhejiang University Science B
VL - 11
IS - 11
SP - 880
EP - 888
%@ 1673-1581
Y1 - 2010
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1000193
Abstract: nucleoside phosphorylase is an important enzyme involved in the biosynthesis of nucleosides. In this study, purine nucleoside phosphorylase and pyrimidine nucleoside phosphorylase were co-expressed in Escherichia coli and the intact cells were used as a catalyst for the biosynthesis of nucleosides. For protein induction, lactose was used in place of isopropyl β-D-1-thiogalactopyranoside (IPTG). When the concentration of lactose was above 0.5 mmol/L, the ability to induce protein expression was similar to that of IPTG. We determined that the reaction conditions of four bacterial strains co-expressing these genes (TUD, TAD, DUD, and DAD) were similar for the biosyntheses of 2,6-diaminopurine nucleoside and 2,6-diaminopurine deoxynucleoside. When the substrate concentration was 30 mmol/L and 0.5% of the recombinant bacterial cell volume was used as the catalyst (pH 7.5), a greater than 90% conversion yield was reached after a 2-h incubation at 50 °C. In addition, several other nucleosides and nucleoside derivatives were efficiently synthesized using bacterial strains co-expressing these recombinant enzymes.
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