Hyperthermophilic endoglucanase for in planta lignocellulose conversion
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چکیده
منابع مشابه
Hyperthermophilic endoglucanase for in planta lignocellulose conversion
UNLABELLED BACKGROUND The enzymatic conversion of lignocellulosic plant biomass into fermentable sugars is a crucial step in the sustainable and environmentally friendly production of biofuels. However, a major drawback of enzymes from mesophilic sources is their suboptimal activity under established pretreatment conditions, e.g. high temperatures, extreme pH values and high salt concentrati...
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The cel12B gene was cloned, optimized through directed evolution using error-prone polymerase chain reaction, and then expressed in the Escherichia coli BL21 (DE3) host strain. Five mutants promoting the enzyme activities were selected. The specific activity of the best-evolved Cel16 (L20R, D37V, I108T) was improved approximately 3-fold compared to the parental enzyme. The residual enzyme activ...
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The microstructure of porous lignocellulose has irregularity, which represents self-similarity within the scope of a certain scale, and the conversion process of lignocellulose to bioethanol is complex. The fractal theory appears to be well suited to be an effective tool for describing and studying such irregularity and complexity. Why not introduce the fractal theory as a potentially efficient...
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Plant biomass, as an abundant renewable carbon source, is a promising alternative to fossil fuels. However, the enzymes most commonly used for depolymerization of lignocellulosic biomass are expensive, and the development of cost-effective alternative conversion technologies would be desirable. One possible option is the heterologous expression of genes encoding lignocellulose-digesting enzymes...
متن کاملCorrection: Site-Directed Mutagenesis of a Hyperthermophilic Endoglucanase Cel12B from Thermotoga maritima Based on Rational Design
Fig 4 is incorrect. Fig 4 incorrectly appears a duplicate of Fig 5. The authors have provided a corrected version of Fig 4 here. Fig 4. Structures of site-directed amino acid residues with other vicinal residues by H-bond. Copyright: © 2015 Zhang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distrib...
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ژورنال
عنوان ژورنال: Biotechnology for Biofuels
سال: 2012
ISSN: 1754-6834
DOI: 10.1186/1754-6834-5-63