title: Effects of the polyhistidine tag on kinetics and other properties of trehalose synthase from Deinococcus 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 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.
authors.affiliation: Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdańsk, Poland.
authors.forename: Anna
authors.initials: A
authors.lastname: Panek
authors.forename: Olga
authors.initials: O
authors.lastname: Pietrow
authors.forename: Paweł
authors.initials: P
authors.lastname: Filipkowski
authors.forename: Józef
authors.initials: J
authors.lastname: Synowiecki
mesh_terms: D034301:Deinococcus / Q000201:enzymology*; D005964:Glucosyltransferases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D006639:Histidine; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009842:Oligopeptides; D013696:Temperature
chemical_list: C471213:His-His-His-His-His-His; D009842:Oligopeptides; D006639:Histidine; D005964:Glucosyltransferases; C099692:trehalose synthase