First Thermostable Endo-β-1,4-Glucanase from Newly Isolated Xanthomonas sp. EC102

被引:0
|
作者
Mi-Hee Woo
Young-Hyo Chang
Hoi-Seon Lee
Pyo June Pak
Joong-Su Kim
Namhyun Chung
机构
[1] Korea Research Institute of Bioscience and Biotechnology,Infection Control Material Research Center
[2] Korea Research Institute of Bioscience and Biotechnology,Biological Resource Center
[3] Chonbuk National University,College of Agriculture and Life Science
[4] Korea University,College of Life Sciences and Biotechnology
来源
The Protein Journal | 2014年 / 33卷
关键词
Thermostability; sp.; Endoglucanase; Characterization;
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中图分类号
学科分类号
摘要
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.
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页码:110 / 117
页数:7
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