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

被引:3
|
作者
Woo, Mi-Hee [1 ]
Chang, Young-Hyo [2 ]
Lee, Hoi-Seon [3 ]
Pak, Pyo June [4 ]
Kim, Joong-Su [1 ]
Chung, Namhyun [4 ]
机构
[1] Korea Res Inst Biosci & Biotechnol, Infect Control Mat Res Ctr, Jeongeup 580185, South Korea
[2] Korea Res Inst Biosci & Biotechnol, Biol Resource Ctr, Taejon 305806, South Korea
[3] Chonbuk Natl Univ, Coll Agr & Life Sci, Jeonju 561756, South Korea
[4] Korea Univ, Coll Life Sci & Biotechnol, Seoul 136712, South Korea
来源
PROTEIN JOURNAL | 2014年 / 33卷 / 01期
基金
新加坡国家研究基金会;
关键词
Thermostability; Xanthomonas sp; Endoglucanase; Characterization; ISOLATED BACILLUS-SUBTILIS; CELLULASE; EXPRESSION; ENZYMES; GENE; CLONING;
D O I
10.1007/s10930-013-9535-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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 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.
引用
收藏
页码:110 / 117
页数:8
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