Characterization of a recombinant cold-adapted purine nucleoside phosphorylase and its application in ribavirin bioconversion
World Journal of Microbiology and Biotechnology, ISSN: 0959-3993, Vol: 27, Issue: 5, Page: 1175-1181
2011
- 4Citations
- 5Captures
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Article Description
Ribavirin is a broad-spectrum antiviral drug and can be produced by enzymatic synthesis by purine nucleoside phosphorylase (PNP). In this study, we describe the application of such a cold-adapted XmPNP in ribavirin bioconversion which showed approximately 15°C lower optimum temperature and 1. 80-fold higher catalytic efficiency (k/K) at 37°C within substrate inosine than homolog in E. coli. By contrast, E. coli (XmPNP) took only 12 h to reach maximum substrate conversion rate (70%) under its optimum temperature (50°C) by using recombinant strain cell as enzyme source, but E. coli (EcPNP) did at 24 h. These results suggest cold-adapted PNP is one attractive candidate for ribavirin bioconversion and other nucleoside medications to improve the catalytic efficiency. © 2010 Springer Science+Business Media B.V.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=79955065406&origin=inward; http://dx.doi.org/10.1007/s11274-010-0564-7; http://link.springer.com/10.1007/s11274-010-0564-7; http://link.springer.com/content/pdf/10.1007/s11274-010-0564-7; http://link.springer.com/content/pdf/10.1007/s11274-010-0564-7.pdf; http://link.springer.com/article/10.1007/s11274-010-0564-7/fulltext.html; http://www.springerlink.com/index/10.1007/s11274-010-0564-7; http://www.springerlink.com/index/pdf/10.1007/s11274-010-0564-7; https://dx.doi.org/10.1007/s11274-010-0564-7; https://link.springer.com/article/10.1007/s11274-010-0564-7
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