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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Characterization of a thermostable endo-beta-1,4-D-galactanase from the hyperthermophile Thermotoga maritima
Hong Yang1, Hitomi Ichinose, Makoto Yoshida
1National Food Research Institute, Ibaraki, Japan.
Abstract:
A putative endo-beta-1,4-D-galactanase gene of Thermotoga maritima was cloned and overexpressed in Escherichia coli. The recombinant enzyme hydrolyzed pectic galactans and produced D-galactose, beta-1,4-D-galactobiose, beta-1,4-D-galactotriose, and beta-1,4-D-galactotetraose. The enzyme displayed optimum activity at 90 degrees C and pH 7.0. It was slowly inactivated above pH 8.0 and below pH 5.0 and stable at temperatures up to 80 degrees C.
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