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 language | English |
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Pages (from-to) | 110-117 |
Number of pages | 8 |
Journal | Protein Journal |
Volume | 33 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2014 Feb |
Keywords
- Characterization
- Endoglucanase
- Thermostability
- Xanthomonas sp.
ASJC Scopus subject areas
- Analytical Chemistry
- Bioengineering
- Biochemistry
- Organic Chemistry