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

Su Jung Kim, Jeong Eun Hyeon, Sang Duck Jeon, Gi wook Choi, Sung Ok Han

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)67-73
Number of pages7
JournalEnzyme and Microbial Technology
Volume66
DOIs
Publication statusPublished - 2014 Nov 1

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Corynebacterium glutamicum
Cellulases
Hydrolysis
Temperature
Enzymes
Cellulase
Biomass
Glucosidases
Saccharification
Enzyme activity
Anchors
Fluorescence Microscopy
Cellulose
Sugars
Polysaccharides
lignocellulose
Microscopic examination
Color
Display devices
Cell Membrane

Cite this

Bi-functional cellulases complexes displayed on the cell surface of corynebacterium glutamicum increase hydrolysis of lignocelluloses at elevated temperature. / Kim, Su Jung; Hyeon, Jeong Eun; Jeon, Sang Duck; Choi, Gi wook; Han, Sung Ok.

In: Enzyme and Microbial Technology, Vol. 66, 01.11.2014, p. 67-73.

Research output: Contribution to journalArticle

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AB - 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.

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