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Thermostable CITase from Thermoanaerobacter thermocopriae shows negative cooperativity

Authors
  • Yang, So-Jin1
  • Choi, Su-Jeong1
  • Park, Bo-Ram2
  • Kim, Young-Min1
  • 1 Chonnam National University, Department of Food Science and Technology, Gwangju, 61186, Republic of Korea , Gwangju (South Korea)
  • 2 National Institute of Agricultural Sciences, Department of Agrofood Resources, Wanju, 55365, Republic of Korea , Wanju (South Korea)
Type
Published Article
Journal
Biotechnology Letters
Publisher
Springer-Verlag
Publication Date
Mar 29, 2019
Volume
41
Issue
4-5
Pages
625–632
Identifiers
DOI: 10.1007/s10529-019-02666-6
Source
Springer Nature
Keywords
License
Yellow

Abstract

ObjectiveThe biochemical properties of a putative thermostable cycloisomaltooligosaccharide (CI) glucanotransferase gene from Thermoanaerobacter thermocopriae were determined using a recombinant protein (TtCITase) expressed in Escherichia coli and purified to a single protein.ResultsThe 171-kDa protein displayed maximum activity at pH 6.0, and enzyme activity was stable at pH 5.0–11.0. The optimal temperature was 60 °C in 1 h incubation, and thermal stability of the protein was 63% at 60 °C for 24 h. TtCITase produced CI-7 to CI-17, as well as CI-18, CI-19, and CI-20, which are relatively large CIs. Additionally, an unusual kinetic feature of TtCITase was its negative cooperative behavior in the dextran T2000 cleavage reaction.ConclusionsBased on our results, TtCITase can be applied to produce relatively large CIs at high temperature.

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