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

Mi Hee Woo, Young Hyo Chang, Hoi Seon Lee, Pyo June Pak, Joong Su Kim, Namhyun Chung

Research output: Contribution to journalArticle

2 Citations (Scopus)

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, 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.

Original languageEnglish
Pages (from-to)110-117
Number of pages8
JournalProtein Journal
Volume33
Issue number1
DOIs
Publication statusPublished - 2014

Keywords

  • Characterization
  • Endoglucanase
  • Thermostability
  • Xanthomonas sp.

ASJC Scopus subject areas

  • Analytical Chemistry
  • Bioengineering
  • Biochemistry
  • Organic Chemistry

Fingerprint Dive into the research topics of 'First Thermostable Endo-β-1,4-Glucanase from Newly Isolated Xanthomonas sp. EC102'. Together they form a unique fingerprint.

  • Cite this