Characterization of a Thermostable Endo-β-1,4-D-galactanase from the Hyperthermophile Thermotoga maritima
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A putative endo-β-1,4-<small>D</small>-galactanase gene of <I>Thermotoga maritima</I> was cloned and overexpressed in <I>Escherichia coli</I>. The recombinant enzyme hydrolyzed pectic galactans and produced <small>D</small>-galactose, β-1,4-<small>D</small>-galactobiose, β-1,4-<small>D</small>-galactotriose, and β-1,4-<small>D</small>-galactotetraose. The enzyme displayed optimum activity at 90 °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 °C.
- Agricultural and Biological Chemistry
Agricultural and Biological Chemistry 70(2), 538-541, 2006-02-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry