Characterization of supercharged cellulase activity and stability in ionic liquids
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- 作者：Lucas B. Johnson ; Sehoo Park ; Lucas P. Gintner ; Christopher D. Snow ; Christopher.Snow@ColoState.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：E1 ; endoglucanase 1 ; pE1 ; superpositive E1 ; nE1 ; supernegative E1 ; pNPC ; p-nitrophenol-β-d-cellobioside ; IL ; ionic liquid ; [Emim] ; 1-ethyl-3-methylimidazolium ; [Bmim] ; 1-butyl-3-methylimidazolium ; [Amim] ; 1-allyl-3-methylimidzaolium ; [Dmim] ; 1 ; 3-dimethylimidazolium ; BF4 ; tetrafluoroborate ; DMP ; dimethylphosphate ; DEP ; diethylphosphate ; DBP ; dibutylphosphate ; NO3 ; nitrate ; OA ; cacetate ; HEPES ; 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid ; MES ; 2-(N-morpholino)ethanesulfonic acid ; CHES ; N-Cy
- 刊名：Journal of Molecular Catalysis B: Enzymatic
- 出版年：2016
- 出版时间：October 2016
- 年：2016
- 卷：132
- 期：Complete
- 页码：84-90
- 全文大小：1415 K
文摘
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A thermostable endoglucase was computationally designed to have significantly altered surface charge.
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Positive supercharging preserved near native activity while negative supercharging decreased both activity and stability.
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Enzymatic activity was assessed in the presence of nine different aqueous ionic liquids.
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20">Common cellulose dissolving solvent 1-ethyl-3-methylimidazolium acetate severely reduced enzyme activity.