NDLI: Engineering ionic liquid-tolerant cellulases for biofuels production.

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Engineering ionic liquid-tolerant cellulases for biofuels production.

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Engineering ionic liquid-tolerant cellulases for biofuels production.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wolski, Paul W. Dana, Craig M. Clark, Douglas S. Blanch, Harvey W.
Description	Country affiliation: United States Author Affiliation: Wolski PW ( Energy Biosciences Institute, University of California, Berkeley, CA 94720, USA Graduate Group of Comparative Biochemistry at University of California, Berkeley, CA, USA Department of Chemical and Biomolecular Engineering, University of California, Berkeley, CA 94720, USA.); Dana CM ( Energy Biosciences Institute, University of California, Berkeley, CA 94720, USA Department of Chemical and Biomolecular Engineering, University of California, Berkeley, CA 94720, USA.); Clark DS ( Energy Biosciences Institute, University of California, Berkeley, CA 94720, USA Department of Chemical and Biomolecular Engineering, University of California, Berkeley, CA 94720, USA clark@berkeley.edu blanch@berkeley.edu.); Blanch HW ( Energy Biosciences Institute, University of California, Berkeley, CA 94720, USA Department of Chemical and Biomolecular Engineering, University of California, Berkeley, CA 94720, USA clark@berkeley.edu blanch@berkeley.edu.)
Abstract	Dissolution of lignocellulosic biomass in certain ionic liquids (ILs) can provide an effective pretreatment prior to enzymatic saccharification of cellulose for biofuels production. Toward the goal of combining pretreatment and enzymatic hydrolysis, we evolved enzyme variants of Talaromyces emersonii Cel7A to be more active and stable than wild-type T. emersonii Cel7A or Trichoderma reesei Cel7A in aqueous-IL solutions (up to 43% (w/w) 1,3-dimethylimdazolium dimethylphosphate and 20% (w/w) 1-ethyl-3-methylimidazolium acetate). In general, greater enzyme stability in buffer at elevated temperature corresponded to greater stability in aqueous-ILs. Post-translational modification of the N-terminal glutamine residue to pyroglutamate via glutaminyl cyclase enhanced the stability of T. emersonii Cel7A and variants. Differential scanning calorimetry revealed an increase in melting temperature of 1.9-3.9°C for the variant 1M10 over the wild-type T. emersonii Cel7A in aqueous buffer and in an IL-aqueous mixture. We observed this increase both with and without glutaminyl cyclase treatment of the enzymes.
File Format	HTM / HTML
ISSN	17410126
e-ISSN	17410134
Journal	Protein Engineering Design and Selection
Issue Number	4
Volume Number	29
Language	English
Publisher	Oxford University Press
Publisher Date	2016-04-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Biochemistry Discipline Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Biochemistry Molecular Biology Bioengineering Biotechnology

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