Hydrolysis and Fermentation for Cellulosic Ethanol Production

Xiros, Charilaos; Christakopoulos, Paul

doi:10.1002/9781118957844.ch2

Cited by 12 publications

(14 citation statements)

References 109 publications

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“…Today's fossil fuel‐based economy is facing several challenges, such as decreasing reserves and anthropogenic carbon dioxide emission . Along with the problems, renewable biofuels produced from lignocellulosic biomass is gaining increasing attention . Considerable efforts have been devoted to the enzymatic hydrolysis of lignocellulose.…”

Section: Introductionmentioning

confidence: 99%

Enzymaticin situsaccharification of rice straw in aqueous-ionic liquid media using encapsulatedTrichoderma aureoviridecellulase

Liu

et al. 2014

J. Chem. Technol. Biotechnol.

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BACKGROUND: Enzymatic in situ saccharification of lignocellulose in ionic liquids (ILs) has become a hot topic of research, but is hampered by the incompatibility of ILs with cellulase. The aim of this present work was to improve IL tolerance of the cellulase from Trichoderma aureoviride strain HS through an efficient encapsulation method, and thus to develop a compatible IL-cellulase system for biorefining.

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Section: Introductionmentioning

confidence: 99%

Enzymaticin situsaccharification of rice straw in aqueous-ionic liquid media using encapsulatedTrichoderma aureoviridecellulase

Liu

et al. 2014

J. Chem. Technol. Biotechnol.

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“…It is hypothesized that the limiting step in the cellulase-catalysed breakdown of crystalline cellulose is the detachment of the glucan chain from the strong Hbonding network in cellulose into the active site grove [24]. GH1, GH3, GH5, GH9, GH30, GH116 [20] Note: Refs. [19] and [21].…”

Section: Enzymatic Hydrolysis Of Cellulosic Biomassmentioning

confidence: 99%

“…The cohesion module sited on the scaffoldin binds to a dockerin module on each enzymatic subunit [48,49]. This architecture enables synergistic and well-coordinated enzymatic interactions, making cellulosomes about the most adequate biochemical system for the degradation of cellulose [20]. The past decade has seen artificial cellulosomes being constructed for the sole purpose of improving enzymatic functions for the saccharification reaction [50].…”

Section: Cellulosomes: Multienzyme Complexesmentioning

confidence: 99%

“…The GH family 3 (GH3) is one of the most abundant ones in the CAZy database, comprising over 6000 enzymes extensively distributed in plants, fungi and bacteria. The family exhibits various activities such as exo-acting b-Dglucosidases, a-L-arabinofuranosidases, b-D-xyloparanosidases and N-acetyl-b-D-glucosaminidases [66], all of which use a retaining glycosidase mechanism [20,[67][68][69]. In addition to hydrolytic activities, some GH3 enzymes can catalyse glycosidic bond formation either via thermodynamically controlled reverse hydrolysis, or kinetically controlled transglycosylation [70,71].…”

Section: Gh Familymentioning

confidence: 99%

“…Sugar lactones, i.e. glucono-d-lactone, have been known to be potent inhibitors of glycosyl hydrolases [139], especially b-glucosidase [20]. The oxidative cleavage by LPMOs can also be affected by reducing agents such as glutathione or gallate ascorbic acid [102,108,109].…”

Section: Lpmo Auxiliary Activity Familiesmentioning

confidence: 99%

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Enzymatic breakdown of lignocellulosic biomass: the role of glycosyl hydrolases and lytic polysaccharide monooxygenases

Ezeilo

Zakaria

Huyop

et al. 2017

Biotechnology & Biotechnological Equipment

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Lignocellulose constitutes a major component of discarded wastes from various industries viz. agriculture, forestry and municipal waste treatment. The potential use of lignocellulose from such types of biomass can be maximized by enzymatic degradation using glycoside hydrolases (GHs) and oxidative enzymes to produce renewable fuels. Nonetheless, besides the slow rate of degradation and low yields, lignocellulose is also physicochemically recalcitrant and costly to process, further limiting its mass utilization. Therefore, bioprospecting for microorganisms producing efficient lytic polysaccharide monooxygenases (LPMOs) to overcome these drawbacks may prove beneficial. The use of GHs and LPMOs can potentially help to circumvent some limitations in the conversion of lignocellulosic biomass into fermentable sugars. LPMOs are classified as family GH61 or family 33 carbohydrate-binding module (CBM33), whose unusual surface-exposed active site is bound to a copper (II) ion. To date, there are more than 20 known genes encoding cellulose-active LPMOs in bacteria and fungi, with diverse biological activities. Only by thorough comprehension of the diversity, enzymology and role of primary GHs, i.e. celullases and their oxidative machinery can the degradation of lignocellulosic biomass be improved. This review provides insight into the diversity, structure and mechanisms, structural and functional aspects of the oxidative breakdown of cellulose by LPMOs of the cellulose-active GH family.

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