Reference - Detail
|Author||Yang SJ, Choi SJ, Park BR, Kim YM.|
|Title||Thermostable CITase from Thermoanaerobacter thermocopriae shows negative cooperativity.|
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.
|MeSH||Dextrans / metabolism* Enzyme Stability Escherichia coli / genetics Escherichia coli / metabolism Glucosyltransferases / chemistry Glucosyltransferases / genetics Glucosyltransferases / isolation & purification Glucosyltransferases / metabolism* Hydrogen-Ion Concentration Kinetics Molecular Weight Recombinant Proteins / chemistry Recombinant Proteins / genetics Recombinant Proteins / isolation & purification Recombinant Proteins / metabolism* Temperature Thermoanaerobacter / enzymology*|
|DNA material||Genomic DNA of Thermoanaerobacter thermocopriaeJCM 7501 T (JGD12533)|