Hydrolyzability of mannan after adsorption on cellulose

Xiao, Wang; Li, Kena; Yang, Ming; Wang, Jingfeng; Zhang, Junhua

doi:10.1007/s10570-016-1098-4

Cited by 14 publications

(9 citation statements)

References 33 publications

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“…However, the amount of mannan re-adsorption on cellulose aer pretreatment was reported to be higher than that of glucomannan and galactomannan at the same concentrations. 322 In a recent study, the Cellic® CTec3 enzyme mixture was reported to be more resistant than Celluclast 1.5L cellulase to the inhibitory compounds produced during steam pretreatment of poplar and lodgepole pine. 323 Furthermore, monomeric sugars were shown to have greater inhibitory effects than phenolics, depending upon their types, and oligomeric sugars.…”

Section: Formation Of Inhibitory Byproductsmentioning

confidence: 99%

Cellulose solvent-based pretreatment for enhanced second-generation biofuel production: a review

Satari

Karimi

Kumar

2019

Sustainable Energy Fuels

195

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Section: Formation Of Inhibitory Byproductsmentioning

confidence: 99%

Cellulose solvent-based pretreatment for enhanced second-generation biofuel production: a review

Satari

Karimi

Kumar

2019

Sustainable Energy Fuels

195

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“…Removal of these substitutions changes cellulose-hemicellulose interactions and may decrease the recalcitrance of the feedstock [265]. On the other hand, removal of substitutions from xylan and glucomannan polymers that are not directly associated with cellulose microfibrils may decrease their solubility in water and lead to the adsorption of linear, unsubstituted hemicellulose fragments onto cellulose fibers [165,195,379]. While these hemicelluloses can be removed by xylanases and mannanases, they will limit cellulose accessibility [379,380].…”

Section: Hemicellulolytic Enzymesmentioning

confidence: 99%

“…On the other hand, removal of substitutions from xylan and glucomannan polymers that are not directly associated with cellulose microfibrils may decrease their solubility in water and lead to the adsorption of linear, unsubstituted hemicellulose fragments onto cellulose fibers [165,195,379]. While these hemicelluloses can be removed by xylanases and mannanases, they will limit cellulose accessibility [379,380]. In addition to acting on hemicelluloses, acetyl esterases may also act on lignin and change its properties [265], but the implications of this effect, and of the effects of deacetylating enzymes in general remain to be studied.…”

Section: Hemicellulolytic Enzymesmentioning

confidence: 99%

Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives

Østby

Hansen

Horn

et al. 2020

Journal of Industrial Microbiology and Biotechnology

136

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Efficient saccharification of lignocellulosic biomass requires concerted development of a pretreatment method, an enzyme cocktail and an enzymatic process, all of which are adapted to the feedstock. Recent years have shown great progress in most aspects of the overall process. In particular, increased insights into the contributions of a wide variety of cellulolytic and hemicellulolytic enzymes have improved the enzymatic processing step and brought down costs. Here, we review major pretreatment technologies and different enzyme process setups and present an in-depth discussion of the various enzyme types that are currently in use. We pay ample attention to the role of the recently discovered lytic polysaccharide monooxygenases (LPMOs), which have led to renewed interest in the role of redox enzyme systems in lignocellulose processing. Better understanding of the interplay between the various enzyme types, as they may occur in a commercial enzyme cocktail, is likely key to further process improvements.

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“…Galactomannan-cellulose complexes were synthesised as described previously [22]. With 2% (w/v) of the galactomannan-cellulose complex used as a substrate, both endo-mannanases displayed lowered specific activities compared to those displayed on locust bean gum.…”

Section: Endo-mannanase Activity On Galactomannan-cellulose Complexesmentioning

confidence: 99%

Combination of CTec2 and GH5 or GH26 Endo-Mannanases for Effective Lignocellulosic Biomass Degradation

Malgas

Pletschke

2020

Catalysts

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Among endo-mannanases, glycoside hydrolase (GH) family 26 enzymes have been shown to be more catalytically active than GH5 enzymes on mannans. However, only GH5 endo-mannanases have been used for the formulation of enzyme cocktails. In this study, Bacillus sp.-derived GH5 and GH26 endo-mannanases were comparatively analysed biochemically for their synergistic action with a commercial cellulase blend, CTec2, during pre-treated lignocellulose degradation. Substrate specificity and thermo-stability studies on mannan substrates showed that GH26 endo-mannanase was more catalytically active and stable than GH5. GH26 also exhibited higher binding affinity for mannan than GH5, while GH5 showed more affinity for lignocellulosic substrates than GH26. Applying the endo-mannanases in combination with CTec2 for lignocellulose degradation led to synergism with a 1.3-fold increase in reducing sugar release compared to when CTec2 was used alone. This study showed that using the activity of endo-mannanases displayed with model substrates is a poor predictor of their activity and synergism on complex lignocelluloses.

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Hydrolyzability of mannan after adsorption on cellulose

Cited by 14 publications

References 33 publications

Cellulose solvent-based pretreatment for enhanced second-generation biofuel production: a review

Cellulose solvent-based pretreatment for enhanced second-generation biofuel production: a review

Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives

Combination of CTec2 and GH5 or GH26 Endo-Mannanases for Effective Lignocellulosic Biomass Degradation

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