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Zhang,Yu; Li,Zhen-Hua; Zheng,Wei; Tang,Zhen-Xing; Zhang,Zhi-Liang; Shi,Lu-E. |
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... |
Tipo: Journal article |
Palavras-chave: Factors affecting enzyme activity; Nuclease; Mutation; Mutagenesis; Nucleases without sequence specificity. |
Ano: 2016 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000600005 |
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