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Effects of the polyhistidine tag on kinetics and other properties of trehalose synthase from Deionococcus geothermalis
Abstract
Two recombinant trehalose synthases from Deinococcus geothermalis (DSMZ 11300) were compared. A significant influence of the artificial polyhistidine tag was observed in protein constitution. The recombinant trehalose synthase from D. geothermalis with His6 -tag has a higher K m value of 254 mM, in comparison with the wild-type trehalose synthase (K m 170 mM), and displayed a lower activity of maltose conversion when compared to the wild type. Moreover, differences in properties like temperature, pH, thermal- and pH-stability were observed. Presence of the histidine tag caused a decrease of thermal resistance in case of trehalose synthase with His6 -tag. These data confirmed a suggestion that the introduction of the histidine domain produces in some seldom cases undesirable changes in the protein.
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- Category:
- Articles
- Type:
- artykuł w czasopiśmie wyróżnionym w JCR
- Published in:
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Acta Biochimica Polonica
no. 60,
pages 163 - 166,
ISSN: 0001-527X - Language:
- English
- Publication year:
- 2013
- Bibliographic description:
- Panek A., Pietrow-Tobiszewska O., Filipkowski P., Synowiecki J.: Effects of the polyhistidine tag on kinetics and other properties of trehalose synthase from Deionococcus geothermalis// Acta Biochimica Polonica. -Vol. 60, iss. 2 (2013), s.163-166
- DOI:
- Digital Object Identifier (open in new tab) 10.18388/abp.2013_1966
- Verified by:
- Gdańsk University of Technology
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