Addition of feruloyl esterase and xylanase produced on-site improves sugarcane bagasse hydrolysis

Braga, Cleiton Márcio Pinto; Delabona, Priscila da Silva; Lima, Deise Juliana da Silva; Paixão, Douglas Antônio Alvaredo; Pradella, José Geraldo da Cruz; Farinas, Cristiane S.

doi:10.1016/j.biortech.2014.07.115

Cited by 54 publications

(28 citation statements)

References 39 publications

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“…These limitations have promoted the development of second-generation biofuels based on the use of wood, grass, agricultural and forest lignocellulosic residues and fiber sludge as resources for obtaining bioethanol [3]. The enormous potential shown by this second wave of biofuels suggests that biomass could become a key resource for renewable energy supply based on future biorefineries [3–6]. …”

Section: Introductionmentioning

confidence: 99%

“…Lignocellulose is a major component of plant cell-wall architecture, consisting of cellulose, hemicellulose and lignin [12]. Hemicellulose, the second most abundant constituent, is mainly composed of xylan, a linear backbone polymer of β- d -xylopyranosyl units linked by β-(1,4) glycosidic bonds, commonly branched with 4- O -methyl-α- d -glucuronopyranosyl units, acetyl groups or α- l -arabinofuranosyl units, in variable proportions [3–6]. Complete depolymerization of xylan requires the joint action of different enzymatic activities, including endo-1,4-β-xylanases (EC 3.2.1.8), β- d -xylosidases (EC 3.2.1.37), α- l -arabinofuranosidases (EC 3.2.1.55), α-glucuronidases (EC 3.2.1.139), acetyl xylan esterases (EC 3.1.1.72), and ferulic/coumaric acid esterases (EC 3.1.1.73) [13].…”

Section: Introductionmentioning

confidence: 99%

“…Complete depolymerization of xylan requires the joint action of different enzymatic activities, including endo-1,4-β-xylanases (EC 3.2.1.8), β- d -xylosidases (EC 3.2.1.37), α- l -arabinofuranosidases (EC 3.2.1.55), α-glucuronidases (EC 3.2.1.139), acetyl xylan esterases (EC 3.1.1.72), and ferulic/coumaric acid esterases (EC 3.1.1.73) [13]. Among them, endo-1,4-β-xylanases play a crucial role for their implication in breaking down the xylan backbone in smaller, less recalcitrant fragments, thereby increasing the overall rate of release of fermentable sugars and making cellulose more accessible for further hydrolysis or fermentation [6, 11, 14]. The complex branching and acetylation patterns so characteristic of plant cell-wall structures give lignocellulosic biomass a recalcitrant nature, which is the main reason responsible for the high cost associated with lignocellulosic conversion [11, 15].…”

Section: Introductionmentioning

confidence: 99%

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Structural and functional characterization of a highly stable endo-β-1,4-xylanase from Fusarium oxysporum and its development as an efficient immobilized biocatalyst

Gómez

Payne

Savko

et al. 2016

Biotechnol Biofuels

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BackgroundReplacing fossil fuel with renewable sources such as lignocellulosic biomass is currently a promising alternative for obtaining biofuel and for fighting against the consequences of climate change. However, the recalcitrant structure of lignocellulosic biomass residues constitutes a major limitation for its widespread use in industry. The efficient hydrolysis of lignocellulosic materials requires the complementary action of multiple enzymes including xylanases and β-xylosidases, which are responsible for cleaving exo- and endoxylan linkages, that release oligocarbohydrates that can be further processed by other enzymes.ResultsWe have identified the endo-β-1,4-xylanase Xyl2 from Fusarium oxysporum as a promising glycoside hydrolase family 11 enzyme for the industrial degradation of xylan. To characterize Xyl2, we have cloned the synthetic optimized gene and expressed and purified recombinant Xyl2 to homogeneity, finally obtaining 10 mg pure Xyl2 per liter of culture. The crystal structure of Xyl2 at 1.56 Å resolution and the structure of a methyl-xylopyranoside Xyl2 complex at 2.84 Å resolution cast a highly detailed view of the active site of the enzyme, revealing the molecular basis for the high catalytic efficiency of Xyl2. The kinetic analysis of Xyl2 demonstrates high xylanase activity and non-negligible β-xylosidase activity under a variety of experimental conditions including alkaline pH and elevated temperature. Immobilizing Xyl2 on a variety of solid supports enhances the enzymatic properties that render Xyl2 a promising industrial biocatalyst, which, together with the detailed structural data, may establish Xyl2 as a platform for future developments of industrially relevant xylanases.Conclusions F. oxysporum Xyl2 is a GH11 xylanase which is highly active in free form and immobilized onto a variety of solid supports in a wide pH range. Furthermore, immobilization of Xyl2 on certain supports significantly increases its thermal stability. A mechanistic rationale for Xyl2's remarkable catalytic efficiency at alkaline pH is proposed on the basis of two crystallographic structures. Together, these properties render Xyl2 an attractive biocatalyst for the sustainable industrial degradation of xylan.Electronic supplementary materialThe online version of this article (doi:10.1186/s13068-016-0605-z) contains supplementary material, which is available to authorized users.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Structural and functional characterization of a highly stable endo-β-1,4-xylanase from Fusarium oxysporum and its development as an efficient immobilized biocatalyst

Gómez

Payne

Savko

et al. 2016

Biotechnol Biofuels

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“…In recent years, feruloyl esterases have been focused as a promising biocatalyst in the fields of biofuel production, pharmaceutical synthesis and organic food making [3,4]. To date, tens of FAEs have been confirmed by screening a diversity of microorganisms, which has provided valuable information for its application and directed evolution [5,6].…”

Section: Introductionmentioning

confidence: 99%

Expression of feruloyl esterase A from Aspergillus terreus and its application in biomass degradation

Zhang

Wang

Lü

et al. 2015

Protein Expression and Purification

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“…Process costs need to be reduced by measures such as on-site enzyme production [11], recycling of fungal pellets, and avoidance of genetic modifications which lowers wastewater treatment costs. On the other hand, the selected fungal strain is of uttermost importance.…”

mentioning

confidence: 99%

Isolation of Filamentous Fungi Exhibiting High Endoxylanase Activity in Lignocellulose Hydrolysate

Ottenheim

Meier

Zimmermann

et al. 2014

Appl Biochem Biotechnol

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For complete degradation of hemicellulose into its monomers from lignocellulose biomass, the synergistic action of a broad range of hydrolytic enzymes is needed. Therefore, production of enzymes from their natural producer is desirable. To obtain a powerful β-1,4-endoxylanase producing fungus, 304 environmental samples were collected from various locations in Singapore, leading to 603 isolates. Among them, 71 exhibiting β-1,4-endoxylanase activity were identified belonging mainly to the genera of Aspergillus, Penicillium, and Trichoderma. Further analysis revealed Aspergillus niger DSM 26641 as a potential and stable β-1,4-endoxylanase producer, being able to grow in hydrothermal lignocellulose hydrolysate exhibiting its maximal β-1,4-endoxylanase activity at pH 4 and 60 °C. This strain is thought to be very suitable for lactic acid production in a simultaneous saccharification and fermentation at pH values below 5.

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Addition of feruloyl esterase and xylanase produced on-site improves sugarcane bagasse hydrolysis

Cited by 54 publications

References 39 publications

Structural and functional characterization of a highly stable endo-β-1,4-xylanase from Fusarium oxysporum and its development as an efficient immobilized biocatalyst

Structural and functional characterization of a highly stable endo-β-1,4-xylanase from Fusarium oxysporum and its development as an efficient immobilized biocatalyst

Expression of feruloyl esterase A from Aspergillus terreus and its application in biomass degradation

Isolation of Filamentous Fungi Exhibiting High Endoxylanase Activity in Lignocellulose Hydrolysate

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