Enzyme activity and thermostability of a non-specific nuclease from Yersinia enterocolitica subsp. palearctica by site-directed mutagenesis
Reprint PDF

Keywords

factors affecting enzyme activity
mutation
mutagenesis
nucleases without sequence specificity
nuclease

How to Cite

1.
Zhang Y, Li Z-H, Zheng W, Tang Z-X, Zhang Z-L, Shi L-E. Enzyme activity and thermostability of a non-specific nuclease from Yersinia enterocolitica subsp. palearctica by site-directed mutagenesis. Electron. J. Biotechnol. [Internet]. 2016 Nov. 15 [cited 2024 Dec. 4];24. Available from: https://www.ejbiotechnology.info/index.php/ejbiotechnology/article/view/2016.02.010

Abstract

Background: To identify the critical amino acid residues that contribute to the high enzyme activity and good thermostability of Yersinia enterocolitica subsp. palearctica (Y. NSN), 15 mutants of Y. NSN were obtained by site-directed mutagenesis in this study. And their enzyme activity and thermostability were assayed. Effect of several factors on the enzyme activity and thermostability of Y. NSN, was also investigated.

Results: The results showed that the I203F and D264E mutants retained approximately 75% and 70% enzyme activity, respectively, compared to the wild-type enzyme. In addition to the I203F and D264E mutants, the mutant E202A had an obvious influence on the thermostability of Y. NSN. According to the analysis of enzyme activity and thermostability of Y. NSN, we found that Glu202, Ile203 and Asp264 might be the key residues for its high enzyme activity and good thermostability.

Conclusions: Among all factors affecting enzyme activity and thermostability of Y. NSN, they failed to explain the experimental results well. One reason might be that the enzyme activity and thermostability of Y. NSN were affected not only by a single factor but also by the entire environment.

Reprint PDF

Upon acceptance of an article by the journal, authors will be asked to transfer the copyright to Electronic Journal of Biotechnology, which is committed to maintain the electronic access to the journal and to administer a policy of fair control and ensure the widest possible dissemination of the information. The author can use the article for academic purposes, stating clearly the following: "Published in Electronic Journal of Biotechnology at DOI:10.2225/volXX-issueX-fulltext-XX".

The Copyright Transfer Agreement must be submitted as a signed scanned copy to biotec@ucv.cl. All authors must send a copy of this document.