An expansin-like protein from Hahella chejuensis binds cellulose and enhances cellulase activity

被引:67
作者
Lee, Hee Jin [2 ]
Lee, Saeyoung [1 ]
Ko, Hyeok-jin [1 ]
Kim, Kyoung Heon [2 ]
Choi, In-Geol [1 ]
机构
[1] Korea Univ, Coll Life Sci & Biotechnol, Seoul 136713, South Korea
[2] Korea Univ, Sch Life Sci & Biotechnol, Seoul 136713, South Korea
关键词
cellulose binding; cellulase synergism; EXLX2; expansin; CRYSTAL-STRUCTURE; BACTERIAL CELLULASE; TRICHODERMA-REESEI; BACILLUS-SUBTILIS; DOMAIN; SUPERFAMILY; HYDROLYSIS; DISRUPTION; EXPRESSION; DEGRADATION;
D O I
10.1007/s10059-010-0033-z
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
Molecular function of the expansin superfamily has been highlighted for cellulosic biomass conversion. In this report, we identified a new bacterial expansin subfamily by analysis of related bacterial sequences and biochemically examined a member of this new subfamily from Hahella chejuensis (HcEXLX2). Among the various complex polysaccharides tested, HcEXLX2 bound most efficiently to cellulose. The relative binding constant (K (r) ) against Avicel was 2.1 L g(-1) at pH 6.0 and 4A degrees C. HcEXLX2 enhanced the activity of cellulase, producing about 4.6 times more hydrolysis product after a 36 h reaction relative to when only cellulase was used. The extension strength test on filter paper indicated that HcEXLX2 has a texture loosening effect on filter paper, which was 53% of that observed for 8 M urea treatment. These activities, compared with a cellulose binding domain from Clostridium thermocellum, implied that the synergistic effect of HcEXLX2 comes from not only binding to cellulose but also disrupting the hydrogen bonds in cellulose. Based on these results, we suggest that the new bacterial expansin subfamily functions by binding to cell wall polysaccharides and increasing the accessibility of cell wall degrading enzymes.
引用
收藏
页码:379 / 385
页数:7
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