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Bi-functional cellulases complexes displayed on the cell surface of Corynebacterium glutamicum increase hydrolysis of lignocelluloses at elevated temperature

Paper ID Volume ID Publish Year Pages File Format Full-Text
16994 42629 2014 7 PDF Available
Title
Bi-functional cellulases complexes displayed on the cell surface of Corynebacterium glutamicum increase hydrolysis of lignocelluloses at elevated temperature
Abstract

•Bi-functional cellulases complexes enhance efficient biomass hydrolysis.•Co-displayed endoglucanase and β-glucosidase reduces additional loading solution.•This is the first successful report that macromolecular complex displaying in C. glutamicum.•Msc conjugated enzyme complex enhances thermostability.•Increasing thermostability of enzyme complex will lead to cost effective biomass-hydrolysis.

Introducing cellulases into Corynebacterium glutamicum leads to the direct degradation of lignocellulosic materials for energy sources. In this study, a cellulase complex containing two cellulolytic enzymes, endoglucanase E (CelE) and β-glucosidase A (BglA), was established to completely degrade cellulose to glucose. The cellulases complexes were displayed on the cell surface of C. glutamicum by using the mechanosensitive channel (Msc) to anchor enzymes in the cytoplasmic membrane. As confirmed by comparison enzyme activities in the cell pellet fraction and supernatant and dual color based immunofluorescence microscopy, the cellulolytic enzymes was successfully associated with the cell surface of C. glutamicum. The displayed cellulases complexes had a synergic effect on the direct conversion of biomass to reducing sugars leading to 3.1- to 6.0-fold increase compared to the conversion by the secreted cellulases complexes. In addition, the displayed cellulases complexes increased the residual activities of cCelE and cBglA at 70 °C from 28.3% and 24.3% in the secreted form to 65.1% and 82.8%, respectively. The display of cellulases complexes on the cell surface of C. glutamicum enhances the polysaccharide equivalent and the direct saccharification of low cost biomass via the action of multi-thermostable enzyme complexes.

Keywords
Corynebacterium glutamicum; Anchoring protein; Lignocelluloses degradation; Thermostability; Consolidated bioprocess; Cellulases complex
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Bi-functional cellulases complexes displayed on the cell surface of Corynebacterium glutamicum increase hydrolysis of lignocelluloses at elevated temperature
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 66, November 2014, Pages 67–73
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us