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

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• 作者：Mi-Hee Woo (1)
  Young-Hyo Chang (2)
  Hoi-Seon Lee (3)
  Pyo June Pak (4)
  Joong-Su Kim (1)
  Namhyun Chung (4)
  
• 关键词：Thermostability ; Xanthomonas sp. ; Endoglucanase ; Characterization
• 刊名：The Protein Journal
• 出版年：2014
• 出版时间：February 2014
• 年：2014
• 卷：33
• 期：1
• 页码：110-117
• 全文大小：619 KB
• 作者单位：Mi-Hee Woo (1)
  Young-Hyo Chang (2)
  Hoi-Seon Lee (3)
  Pyo June Pak (4)
  Joong-Su Kim (1)
  Namhyun Chung (4)
  
  1. Infection Control Material Research Center, Korea Research Institute of Bioscience and Biotechnology, Jeongeup, 580-185, Korea
  2. Biological Resource Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 305-806, Korea
  3. College of Agriculture and Life Science, Chonbuk National University, Jeonju, 561-756, Korea
  4. College of Life Sciences and Biotechnology, Korea University, Seoul, 136-712, Korea
  
• ISSN：1573-4943

文摘

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??mg?, V max for CMC was 1.44?μmol?mg??min?, and K m values was 25.6?mg?mL?. 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.