Biosci Biotechnol Biochem. 2006 Feb;70(2):538-41.

Characterization of a thermostable endo-beta-1,4-D-galactanase from the hyperthermophile Thermotoga maritima.

Yang H, Ichinose H, Yoshida M, Nakajima M, Kobayashi H, Kaneko S.

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National 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.

PMID:: 16495677; [PubMed - indexed for MEDLINE]

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Characterization of a thermostable endo-beta-1,4-D-galactanase from the hyperthe...
Characterization of a thermostable endo-beta-1,4-D-galactanase from the hyperthermophile Thermotoga maritima.
Biosci Biotechnol Biochem. 2006 Feb ;70(2):538-41.

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