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  • Title: Thermostable CITase from Thermoanaerobacter thermocopriae shows negative cooperativity.
    Author: Yang SJ, Choi SJ, Park BR, Kim YM.
    Journal: Biotechnol Lett; 2019 May; 41(4-5):625-632. PubMed ID: 30927134.
    Abstract:
    OBJECTIVE: The 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. RESULTS: The 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. CONCLUSIONS: Based on our results, TtCITase can be applied to produce relatively large CIs at high temperature.
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