Characterization of a thermostable endo-beta-1,4-D-galactanase from the hyperthermophile Thermotoga maritima.
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.
National Food Research Institute, Ibaraki, Japan.
Hong
H
Yang
Hitomi
H
Ichinose
Makoto
M
Yoshida
Mitsutoshi
M
Nakajima
Hideyuki
H
Kobayashi
Satoshi
S
Kaneko
D004795:Enzyme Stability; D005685:Galactans / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D011198:Solanum tuberosum / Q000378:metabolism; D013696:Temperature; D020124:Thermotoga maritima / Q000201:enzymology*
D005685:Galactans; D006026:Glycoside Hydrolases; C094192:arabinogalactan endo-1,4-beta-galactosidase