title: First thermostable endo-β-1,4-glucanase from newly isolated Xanthomonas sp. EC102.
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.
authors.affiliation: Infection Control Material Research Center, Korea Research Institute of Bioscience and Biotechnology, Jeongeup, 580-185, Korea.
authors.forename: Mi-Hee
authors.initials: MH
authors.lastname: Woo
authors.forename: Young-Hyo
authors.initials: YH
authors.lastname: Chang
authors.forename: Hoi-Seon
authors.initials: HS
authors.lastname: Lee
authors.forename: Pyo June
authors.initials: PJ
authors.lastname: Pak
authors.forename: Joong-Su
authors.initials: JS
authors.lastname: Kim
authors.forename: Namhyun
authors.initials: N
authors.lastname: Chung
mesh_terms: D002480:Cellulase / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D004795:Enzyme Stability; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013696:Temperature; D014974:Xanthomonas / Q000201:enzymology*
chemical_list: D002480:Cellulase