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2013 | 60 | 2 |

Tytuł artykułu

Effects of the polyhistidine tag on kinetics and other properties of trehalose synthase from Deinococcus geothermalis

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
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 Km value of 254 mM, in comparison with the wild-type trehalose synthase (Km 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.

Wydawca

-

Rocznik

Tom

60

Numer

2

Opis fizyczny

p.163-166,fig.,ref.

Twórcy

autor
  • Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdansk, Poland
autor
  • Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdansk, Poland
  • Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdansk, Poland
  • Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdansk, Poland

Bibliografia

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Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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