The boosting effect of recombinant hemicellulases on the enzymatic hydrolysis of steam-treated sugarcane bagasse

Cintra, Lorena Cardoso; Costa, Isabelle Cristine da; Oliveira, Izadora Cristina Moreira de; Fernandes, Amanda Gregorim; Faria, Syd Pereira; Jesuino, Rosália Santos Amorim; Ravanal, María Cristina; Eyzaguirre, Jaime; Ramos, Luiz Pereira; Faria, Fabrícia Paula de; Ulhôa, Cirano José

doi:10.1016/j.enzmictec.2019.109447

Cited by 22 publications

(7 citation statements)

References 40 publications

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“…This hydrolysis resulted in 50% increase in glucose release, when added prior to commercial cellulases (Accellerase 1500, Dupont, Rochester, NY, USA) in sequential reactions. In this study, the glucose yield was 14.6% when all enzymes were used simultaneously 20 , 23 . Such results highlight the high biotechnological potential of HXYN2 when employed rationally in different process stages.…”

Section: Introductionmentioning

confidence: 74%

Structural and biochemical analysis reveals how ferulic acid improves catalytic efficiency of Humicola grisea xylanase

Oliveira

Garay

Souza

et al. 2022

Sci Rep

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Humicolagrisea var. thermoidea is an aerobic and thermophilic fungus that secretes the GH11 xylanase HXYN2 in the presence of sugarcane bagasse. In this study, HXYN2 was expressed in Pichiapastoris and characterized biochemically and structurally in the presence of beechwood xylan substrate and ferulic acid (FA). HXYN2 is a thermally stable protein, as indicated by circular dichroism, with greater activity in the range of 40–50 °C and pH 5.0–9.0, with optimal temperature and pH of 50 °C and 6.0, respectively. FA resulted in a 75% increase in enzyme activity and a 2.5-fold increase in catalytic velocity, catalytic efficiency, and catalytic rate constant (kcat), with no alteration in enzyme affinity for the substrate. Fluorescence quenching indicated that FA forms a complex with HXYN2 interacting with solvent-exposed tryptophan residues. The binding constants ranged from moderate (pH 7.0 and 9.0) to strong (pH 4.0) affinity. Isothermal titration calorimetry, structural models and molecular docking suggested that hydrogen bonds and hydrophobic interactions occur in the aglycone region inducing conformational changes in the active site driven by initial and final enthalpy- and entropy processes, respectively. These results indicate a potential for biotechnological application for HXYN2, such as in the bioconversion of plant residues rich in ferulic acid.

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Section: Introductionmentioning

confidence: 74%

Structural and biochemical analysis reveals how ferulic acid improves catalytic efficiency of Humicola grisea xylanase

Oliveira

Garay

Souza

et al. 2022

Sci Rep

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“…Currently, several studies have demonstrated the action of oxidative enzymes, such as lytic polysaccharide monooxygenases (LPMOs) classified as AA, capable of degrading cellulose together with cellulases ( 42 – 44 ). Moreover, a recent study demonstrated the boosting effect of recombinant hemicellulases (endoxylanase-HXYN2 and β-xylosidase-HXYLA) from H. grisea together with an α- l -arabinofuranosidase (AFB3) from Penicillium purpurogenum in the hydrolysis of sugarcane bagasse, exhibiting the potential of these enzymes from H. grisea to compose enzymatic consortiums for biomass hydrolysis ( 45 ).…”

Section: Discussionmentioning

confidence: 99%

Insights into the Lignocellulose-Degrading Enzyme System of Humicola grisea var. thermoidea Based on Genome and Transcriptome Analysis

et al. 2021

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“…Regarding new thermostable hemicellulases, the combination of Accellerase 1500 with a cocktail of recombinant hemicellulases composed of endoxylanase (HXYN2) and β-xylosidase (HXYLA) from Humicola grisea var thermoidea and α-L-arabinofuranosidase (AFB3) from Penicillium pupurogenum enhanced the glucose yield from steam-exploded sugarcane bagasse hydrolysis by 14.6%. This effect was even more evident (up to 50%) in two step-sequential hydrolysis, in which biomass was treated first with hemicellulases and then with commercial cellulases [97]. Similarly, in another study, the synergism between the two xylanases XynZ-C from Clostridium thermocellum and Xyn11A from Thermobifida fusca led to a two-fold increase in the concentration of reducing sugars from pre-treated bagasse hydrolysis, in addition to a commercial cellulase from T. reesei (Sigma-Aldrich) [98].…”

Section: Enzymatic Hydrolysismentioning

confidence: 99%

Biorefinery Gets Hot: Thermophilic Enzymes and Microorganisms for Second-Generation Bioethanol Production

et al. 2021

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To mitigate the current global energy and the environmental crisis, biofuels such as bioethanol have progressively gained attention from both scientific and industrial perspectives. However, at present, commercialized bioethanol is mainly derived from edible crops, thus raising serious concerns given its competition with feed production. For this reason, lignocellulosic biomasses (LCBs) have been recognized as important alternatives for bioethanol production. Because LCBs supply is sustainable, abundant, widespread, and cheap, LCBs-derived bioethanol currently represents one of the most viable solutions to meet the global demand for liquid fuel. However, the cost-effective conversion of LCBs into ethanol remains a challenge and its implementation has been hampered by several bottlenecks that must still be tackled. Among other factors related to the challenging and variable nature of LCBs, we highlight: (i) energy-demanding pretreatments, (ii) expensive hydrolytic enzyme blends, and (iii) the need for microorganisms that can ferment mixed sugars. In this regard, thermophiles represent valuable tools to overcome some of these limitations. Thus, the aim of this review is to provide an overview of the state-of-the-art technologies involved, such as the use of thermophilic enzymes and microorganisms in industrial-relevant conditions, and to propose possible means to implement thermophiles into second-generation ethanol biorefineries that are already in operation.

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The boosting effect of recombinant hemicellulases on the enzymatic hydrolysis of steam-treated sugarcane bagasse

Cited by 22 publications

References 40 publications

Structural and biochemical analysis reveals how ferulic acid improves catalytic efficiency of Humicola grisea xylanase

Structural and biochemical analysis reveals how ferulic acid improves catalytic efficiency of Humicola grisea xylanase

Insights into the Lignocellulose-Degrading Enzyme System of Humicola grisea var. thermoidea Based on Genome and Transcriptome Analysis

Biorefinery Gets Hot: Thermophilic Enzymes and Microorganisms for Second-Generation Bioethanol Production

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