Induction of Recombinant Uridine Phosphorylase and Its Application in Biosynthesis of Pyrimidine Nucleosides

丁庆豹; 欧伶; 魏东芝; 魏晓琨; 许彦梅; 张春艳

doi:10.1016/S1004-9541(09)60187-7

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Induction of Recombinant Uridine Phosphorylase and Its Application in Biosynthesis of Pyrimidine Nucleosides

Updated：2026-01-06

- Induction of Recombinant Uridine Phosphorylase and Its Application in Biosynthesis of Pyrimidine Nucleosides
- Chinese Journal of Chemical Engineering Vol. 19, Issue 1, Pages: 122-127(2011)
- Affiliations：
  
  1. State Key Lab of Bioreactor Engineering, East China University of Science and Technology,Shanghai,China,200237
  2. Shanghai Pucheng Bioscience and Biotechnology Co., Ltd.,Shanghai,China,200235
- Author bio：
- Funds：
- DOI：10.1016/S1004-9541(09)60187-7
  CLC：
- Published：2011
- Accepted：
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DING Qingbao, OU Ling, WEI Dongzhi, WEI Xiaokun, XU Yanmei, ZHANG Chunyan. Induction of Recombinant Uridine Phosphorylase and Its Application in Biosynthesis of Pyrimidine Nucleosides[J]. , 2011, 19(1): 122-127.
DOI：

DING Qingbao, OU Ling, WEI Dongzhi, WEI Xiaokun, XU Yanmei, ZHANG Chunyan. Induction of Recombinant Uridine Phosphorylase and Its Application in Biosynthesis of Pyrimidine Nucleosides[J]. , 2011, 19(1): 122-127. DOI： 10.1016/S1004-9541(09)60187-7.

摘要

Abstract

Recombinant

Escherichia coli

pUDP

which overexpressed uridine phosphorylase(UPase)

was constructed.0.5 mmol·L

-1

lactose had a similar induction effect as the commonly used inducer IPTG during 2.5-5.5 h of cell growth.The lactose-induced UPase was stable at 50℃.Wet cells of pUDP was used as catalyst to biosynthesize 5-fluorouridine from

0 mmol·L

-1

uridine and 5-fluorouracil in phosphate buffer(pH 7.0)catalyzed at 50℃ for 1.5 h and the yield of 5-fluorouridine was higher than 68%.Under the optimum reaction conditions for production of 5-fluorouridine

5-methyluridine and azauridine were synthesized from uridine by pUDP

the yield was 61.7% and 47.2% respectively.Deoxynucleosides were also synthesized by pUDP

but the yield was only about 20%.

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