Production and characterization of a recombinant thermophilic trehalose synthase from Thermus antranikianii.

Szczegóły
Abstrakt

Tytuł:: Production and characterization of a recombinant thermophilic trehalose synthase from Thermus antranikianii.
Autorzy:: Lin YF; Department of Biotechnology and Food Technology, Southern Taiwan University of Science and Technology, Tainan 710, Taiwan.
Su PC; Department of Biotechnology and Food Technology, Southern Taiwan University of Science and Technology, Tainan 710, Taiwan.
Chen PT; Department of Biotechnology and Food Technology, Southern Taiwan University of Science and Technology, Tainan 710, Taiwan. Electronic address: .
Źródło:: Journal of bioscience and bioengineering [J Biosci Bioeng] 2020 Apr; Vol. 129 (4), pp. 418-422. Date of Electronic Publication: 2019 Nov 09.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Publication: 2003-: Osaka, Japan : Society for Biotechnology, Japan
Original Publication: Osaka, Japan : Amsterdam, The Netherlands : Society for Bioscience and Bioengineering, Japan ; Distributed outside Japan by Elsevier Science, 1999-
MeSH Terms:: Recombinant Proteins*/analysis
Recombinant Proteins*/genetics
Recombinant Proteins*/metabolism
Glucosyltransferases/*genetics
Glucosyltransferases/*metabolism
Thermus/*genetics
Catalysis ; Cloning, Molecular ; Enzyme Stability/genetics ; Escherichia coli/genetics ; Glucosyltransferases/analysis ; Hot Temperature ; Hydrogen-Ion Concentration ; Maltose ; Thermus/enzymology ; Trehalose/metabolism
Contributed Indexing:: Keywords: Enzyme characterization; Maltose; Thermophilic enzyme; Trehalose; Trehalose synthase
Substance Nomenclature:: 0 (Recombinant Proteins)
69-79-4 (Maltose)
B8WCK70T7I (Trehalose)
EC 2.4.1.- (Glucosyltransferases)
EC 2.4.1.- (trehalose synthase)
SCR Organism:: Thermus antranikianii
Entry Date(s):: Date Created: 20191113 Date Completed: 20200608 Latest Revision: 20200608
Update Code:: 20240105
DOI:: 10.1016/j.jbiosc.2019.10.009
PMID:: 31711928
: Czasopismo naukowe

Full Text Finder

Trehalose synthase converts maltose into trehalose in a single conversion step via intramolecular transformation and is thus useful for industrial production. In this study, we synthesized a thermophilic trehalose synthase from Thermus antranikianii (TaTS), which was recombinantly expressed in Escherichia coli BL21(DE3). The recombinant TaTS showed the highest activity at pH 7.0 and 60°C, with the maximum trehalose yield (76.8%) obtained at pH 7.0 and 30°C. TaTS activity was stable over a wide pH and temperature range of 6-10 and 4-70°C, respectively, over 6 h of incubation. The enzyme activity was strongly inhibited by Co 2+ , Cu 2+ , Zn 2+ , sodium dodecyl sulfate, and Tris. TaTS showed a 1.48-fold higher catalytic efficiency (k cat /K m ) for maltose than for trehalose. Overall, these results demonstrate the good application potential of the recombinant enzyme TaTS in the efficient conversion of trehalose from maltose, with superior environmental tolerance to other trehalose synthases reported.
(Copyright © 2019 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.)

Informacja