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Enzymatic synthesis of 2′-deoxyadenosine and 6-methylpurine-2′-deoxyriboside by Escherichia coli DH5α overexpressing nucleoside phosphorylases from Escherichia coli BL21

Paper ID Volume ID Publish Year Pages File Format Full-Text
21501 43225 2010 4 PDF Available
Title
Enzymatic synthesis of 2′-deoxyadenosine and 6-methylpurine-2′-deoxyriboside by Escherichia coli DH5α overexpressing nucleoside phosphorylases from Escherichia coli BL21
Abstract

Genes encoding purine nucleoside phosphorylase (deo D), uridine phosphorylase (udp) and thimidine phosphorylase (deo A) from Escherichia coli BL21 were cloned and overexpressed in E. coli DH5α. The recombinant strains were employed to synthesize 2′-deoxyadenosine (dAR) and 6-methylpurine-2′-deoxyriboside (MePdR). Experimental parameters such as strains, temperature, pH, reagent concentration and cell mass were optimized. Under the optimal situation, 96% adenine was converted to dAR and 95% 6-methylpurine (MeP) was converted to MePdR in an hour, using 0.2‰ (dry wt./v) cell paste as biocatalyst.

Keywords
2′-Deoxyadenosine; Enzymatic synthesis; Escherichia coli; 6-Methylpurine-2′-deoxyriboside; Nucleoside phosphorylases
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Enzymatic synthesis of 2′-deoxyadenosine and 6-methylpurine-2′-deoxyriboside by Escherichia coli DH5α overexpressing nucleoside phosphorylases from Escherichia coli BL21
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 110, Issue 2, August 2010, Pages 165–168
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us