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作 者:Phillip J. Brumm Spencer Hermanson Joshua Luedtke David A. Mead
机构地区:[1]C5-6 Technologies, 2120 W. Greenview Drive, Middleton, W153562, USA
出 处:《Journal of Life Sciences》2011年第7期488-496,共9页生命科学(英文版)
摘 要:The discovery of new, highly active, biomass-degrading enzymes is important to the development of a sustainable biofuels industry. Dictyoglomus turgidum, a thermophilic, anaerobic eubacterium that ferments cellulose and produces ethanol and hydrogen, was chosen as a candidate to screen for novel enzymes. A novel thermostable endoglucanase, CelA, was identified and purified during screening of a shotgun library of Dic(yoglomus turgidum and subsequently subcloned and expressed in E. coli. The celA gene coding for a 312 amino acid protein showed low homology to proteins outside the genus Dictoglomi and lacked an apparent signal peptide. CelA had a broad substrate range, possessing both endo and exo activity on soluble and insoluble β-(1,4)-Iinked glucose-containing substrates as well as endo activity on soluble and insoluble β-(1,4)-linked mannose containing substrates. The specific activity of CelA was 226 U/rag using β-glucan, 66 U/mg using glucomannan, and 63 U/mg using CMC as substrates. The high temperature optimum of 70 ℃ to 80 ℃ and wide substrate range of the enzyme might make it an excellent tool for biomass degradation at high temperature.
关 键 词:CELLULASE MANNANASE THERMOPHILIC biomass degradation Dictyoglomus turgidum.
分 类 号:Q785[生物学—分子生物学] TS261.11[轻工技术与工程—发酵工程]
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