Related Experiment Video
Updated: May 4, 2026

Author Spotlight: Integrating Biochemical Functions of β-Glucanases and Peroxidase Enzymes in Wheat-RWA Interaction
Published on: July 26, 2024
First thermostable endo-β-1,4-glucanase from newly isolated Xanthomonas sp. EC102
Mi-Hee Woo1, Young-Hyo Chang, Hoi-Seon Lee
1Infection Control Material Research Center, Korea Research Institute of Bioscience and Biotechnology, Jeongeup, 580-185, Korea.
Abstract:
A novel gene encoding thermostable endoglucanase was identified in Xanthomonas sp. EC102 from soil. The gene had 1,458 base pairs of open reading frame, which encode a 52-kDa protein of 486 amino acid residues. Sequence of the amino acid residues was similar with the endoglucanase from Xanthomonas campestris pv. campestris ATCC33913 (GenBank Accession No. NP_638867.1) (94 % identity). The endoglucanase was overexpressed in Escherichia coli BL21 and purified. Temperature for the highest enzymatic activity was 70 °C and pH optima was pH 5.5. The specific activity of the endoglucanase toward carboxymethylcellulose (CMC) was approximately 2 μmol min⁻¹ mg⁻¹, V max for CMC was 1.44 μmol mg⁻¹ min⁻¹, and K m values was 25.6 mg mL⁻¹. The EC102 endoglucanase was stable at temperatures up to 60 °C, and it was activated by 0.1 mM of Mn²⁺ and Co²⁺. This is the first report about thermostable endoglucanase from Xanthomonas sp.

