First Thermostable Endo-beta-1,4-Glucanase from Newly Isolated Xanthomonas sp EC102
- Authors
- Woo, Mi-Hee; Chang, Young-Hyo; Lee, Hoi-Seon; Pak, Pyo June; Kim, Joong-Su; Chung, Namhyun
- Issue Date
- 2월-2014
- Publisher
- SPRINGER
- Keywords
- Thermostability; Xanthomonas sp.; Endoglucanase; Characterization
- Citation
- PROTEIN JOURNAL, v.33, no.1, pp.110 - 117
- Indexed
- SCIE
SCOPUS
- Journal Title
- PROTEIN JOURNAL
- Volume
- 33
- Number
- 1
- Start Page
- 110
- End Page
- 117
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/99485
- DOI
- 10.1007/s10930-013-9535-9
- ISSN
- 1572-3887
- 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 A degrees C and pH optima was pH 5.5. The specific activity of the endoglucanase toward carboxymethylcellulose (CMC) was approximately 2 mu mol min(-1) mg(-1), V (max) for CMC was 1.44 mu mol mg(-1) min(-1), and K (m) values was 25.6 mg mL(-1). The EC102 endoglucanase was stable at temperatures up to 60 A degrees 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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