First thermostable endo-beta-1,4-glucanase from newly isolated Xanthomonas sp. EC102 = Xanthomonas sp. EC102로 부터 신규 내열성 Endo-beta-1,4-glucanase 분리
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- First thermostable endo-beta-1,4-glucanase from newly isolated Xanthomonas sp. EC102 = Xanthomonas sp. EC102로 부터 신규 내열성 Endo-beta-1,4-glucanase 분리
- Mi-Hee Woo; Young Hyo Chang; H S Lee; P J Pak; Joong Su Kim; N Chung
- Bibliographic Citation
- Protein Journal, vol. 33, no. 1, pp. 110-117
- Publication Year
- 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, Vmax for CMC was 1.44 μmol mg-1 min-1, and Km 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.
- CharacterizationEndoglucanaseThermostabilityXanthomonas sp.
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- Ochang Branch Institute > Division of National Bio-Infrastructure > Bio-Infrastructure Policy Support Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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