Characterization of a thermostable endo-beta-1,4-D-galactanase from the hyperthermophile Thermotoga maritima
2006
Yang, H.(National Food Research Inst., Tsukuba, Ibaraki (Japan)) | Ichinose, H. | Yoshida, M. | Nakajima, M. | Kobayashi, H. | Kaneko, S.
A putative endo-beta-1,4-D-galactanase gene of Thrmotoga 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 deg 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 deg C.
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