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2013 | 60 | 2 | 163-166
Article title

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

Content
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Languages of publication
EN
Abstracts
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.
Publisher

Year
Volume
60
Issue
2
Pages
163-166
Physical description
Dates
published
2013
received
2012-11-23
revised
2013-04-25
accepted
2013-05-14
(unknown)
2013-06-06
Contributors
author
  • Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdańsk, Poland
author
  • Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdańsk, Poland
  • Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdańsk, Poland
  • Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdańsk, Poland
References
  • Benaroudj N, Lee DH, Goldberg AL (2001) Trehalose accumulation during cellular stress protects cells and cellular proteins from damage by oxygen radicals. J Biol Chem 276: 24261-24267.
  • Berendsen DH (2002) Trehalose: a review of properties, history of use and human tolerance, and resultes of multiple safety studies. Food Chem Toxicol 40: 871-898.
  • Crowe JH, Crowe IM (2000) Preservation of mammalian cells, Learning on nature tricks. Nat Biotechnol 18: 145-147.
  • Ferreira AC, Nobre MF, Rainey FA, Silva MT, Wait R (1997) Deinococcus geothermalis sp. Nov. and Deinococcus murrayi sp. Nov. two extremely radiation-resistant and slightly thermophilic species from hot springs. Int J Syst Bacteriol 47: 939-947.
  • Filipkowski P, Duraj-Thatte A, Kur JW (2006) Novel thermostable single-stranded DNA-binding protein (SBB) from Deinococcus geothermalis. Arch Microbiol 186: 129-137.
  • Filipkowski P, Panek A, Felczykowska A, Pietrow O, Synowiecki J (2012) Expression of Deinococcus geothermalis trehalose synthase gene in Escherichia coli and its enzymatic properties. Afr J Biotechnol 11: 13131-13139.
  • Filipkowski P, Pietrow O, Panek A, Synowiecki J (2012) Properties of recombinant trehalose synthase from Deinococcus radiodurans expressed in Escherichia coli. Acta Biochim Pol 59: 425-431.
  • Halliwell CM, Morgan G, Ou CP, Cass AE (2001) Introduction of a (poly)histidine tag in L-lactate dehydrogenase products a mixture of active and inactive molecules. Anal Biochem 295: 257-261.
  • Higashiyama T (2002) Novel functions and applications of trehalose. Pure Appl Chem 74: 1263-1269.
  • Hochuli E, Dobeli H, Schacher A (1987) New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J Chromatogr 411: 177-184.
  • Jain KN, Roy I (2008) Effect of trehalose on protein structure. Protein Sci 18: 24-36.
  • Khan F, Legler PM, Mease RM, Duncan EH, Bergmann-Leitner ES, Angov E (2012) Histidine affinity tags affect MSP142 structural stability and immunoobominance in mice. Biotechnol J 7: 133-147.
  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
  • Lins RD, Pereira CS, Hünenberger PH (2004) Trehalose-Protein Interaction in Aqueous Solution. Proteins 55: 177-186.
  • Ma Y, Xue L, Sun DW (2006) Characteristic of trehalose synthase from permeabilized Pseudomonas putida cells and its application in converting maltose to trehalose. J Food Eng 77: 342-347.
  • Nishimoto T, Nakano M, Nakada T, Chaen H, Fukuda S, Sugimoto T, (1996a) Purification and properties of a novel enzyme, trehalose synthase from Pimelobacter sp. R48. Biosci Biotechnol Biochem 60: 640-644.
  • Nishimoto T, Nakada T, Chaen H, Fukuda S, Sugimoto T, KurimotoM (1996b) Action of thermostable trehalose synthase from Thermus aquaticus on sucrose. Biosci Biotechnol Biochem 60: 835-839.
  • Pan YT, Carroll JD, Asano N, Pastuszak I, Edavana VK, Elbein AD (2008) Trehalose synthase converts glycogen to trehalose. FEBS J 275: 3408-3420.
  • Pietzsch M, Wiese A, Ragnitz K, Wilms B, Altenbuchner J, Mattes R, Syldatk C (2000) Purification of recombinant hydantoinase and L-Ncarbamoylase from Arthobacter aurescans expressed in Escherichia coli: comparison of wild-type and genetically modified proteins. J Chromatogr B 737: 179-186.
  • Richards AD, Krakowska S, Dexter LB, Schmid H, Wolterbeek APM, Waalkens-Roser B (1991) Trehalose, a new approach to premium dried foods. Trends Food Sci Technol 2: 166-169.
  • Terpe K (2003) Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems Appl Microbiol Biotechnol 60: 523-533.
  • Wu J, Filutowicz M (1999) Hexahistidine (His6)-tag dependent protein dimerization: A cautionary tale. Acta Biochim Polonica 46: 591-599.
  • Xiuli W, Hongbiao D, Ming Y, Yu Q (2009) Gene cloning, expression, and characterization of a novel trehalose synthase from Arthrobacter aurescens. Appl Microbiol Biotechnol 83: 477-482.
  • Zdziebło A, Synowiecki J (2006) Production of trehalose by intramolecular transglucosylation of maltose catalyzed by a new enzyme from Thermus thermophilus. Food Chem 96: 8-13.
  • Zhu Y, Zhang J, Wei D, Wang Y, Chen X, Xing L, Li M (2008) Isolation and identification of a thermophilic strain producing trehalose synthase from geothermal water in China. Biosci Biotechnol Biochem 72: 2019-2024.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv60p163kz
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