Identification and characterization of a novel AA9-type lytic polysaccharide monooxygenase from a bagasse metagenome

Bunterngsook, Benjarat; Mhuantong, Wuttichai; Kanokratana, Pattanop; Iseki, Yu; Watanabe, Takashi; Champreda, Verawat

doi:10.1007/s00253-020-11002-2

Cited by 7 publications

(2 citation statements)

References 60 publications

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“…Although the experimental conditions used to investigate the DSs of various LPMOs and cellulases differ among the reports, the DSs of Cs LPMO9 and Celluclast 1.5L turned out to be higher than any DSs (0.5–3.4) reported for other LPMOs and cellulases on the degradation of Avicel. ,,− Among those various LPMOs, GH61D from Phanerochaete chrysosporium ( Pc GH61D), which shares ∼70% amino acid sequence identity with Cs LPMO9, had been studied previously . Although, it should be kept in mind that the different conditions (pH, electron donor, and the ratio of LPMO and cellulases) were used when the synergistic effects for Pc GH61D and Cs LPMO9 were obtained, we were able to deduce the DS for Pc GH61D using the reported data, which was calculated to be ca.…”

Section: Resultsmentioning

confidence: 81%

“…This DS value also turned out to be higher than any DSs (0.6−2.8) reported for various LPMOs and cellulases on the degradation of PASC. [34][35][36]40,41 During the revision process of this article, a paper containing studies on activities of two CsLPMOs (CsLPMO9A and CsLPMO9B) and their synergistic effects with cellulase on cellulose degradation had appeared. 10 Although the experimental conditions were not the same as ours, the synergistic effects of CsLPMO9A and CsLPMO9B seem to be lower than our CsLPMO9.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Functional and Structural Characterizations of Lytic Polysaccharide Monooxygenase, Which Cooperates Synergistically with Cellulases, from Ceriporiopsis subvermispora

Nguyen

Kondo

Yagi

et al. 2022

ACS Sustainable Chem. Eng.

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Lignocellulose-degrading fungi use various oxidative enzymes to degrade lignocellulosic biomass. Oxidative cleavage of cellulose by AA9 family lytic polysaccharide monooxygenases (LPMOs), LPMO9s, reportedly enhances cellulose depolymerization catalyzed by hydrolytic enzymes. To improve this enhancement, functional and structural understanding of LPMO9s is needed. Here, we recombinantly expressed an LPMO9 of Ceriporiopsis subvermispora, CsLPMO9, in Pichia pastoris. Simultaneous treatment of microcrystalline cellulose with CsLPMO9 and a commercial cellulase cocktail led to an 8.5-fold higher reducing sugar yield over the sum of the yields on individual treatment with CsLPMO9 and the cellulase cocktail. Similarly, simultaneous treatment of phosphoric acid-swollen cellulose resulted in a 3.2-fold increased yield. We also solved the crystal structure of CsLPMO9. CsLPMO9 takes on a typical LPMO structure having a β-sandwich fold with a copper-coordinating histidine brace. Solvent-exposed residues, including Tyr residues, in the putative substrate-binding surface of CsLPMO9 were deduced to be involved in binding cellulosic substrates. Mutagenesis of two characteristic Tyr residues revealed that they contribute to the affinity of CsLPMO9 with cellulosic substrate. The high synergy of CsLPMO9 and the cellulase cocktail may be promising for efficient biomass utilization.

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Section: Resultsmentioning

confidence: 81%

Section: ■ Results and Discussionmentioning

confidence: 99%

Functional and Structural Characterizations of Lytic Polysaccharide Monooxygenase, Which Cooperates Synergistically with Cellulases, from Ceriporiopsis subvermispora

Nguyen

Kondo

Yagi

et al. 2022

ACS Sustainable Chem. Eng.

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Hyperthermophilic xylanase and thermophilicity analysis by molecular dynamic simulation with quantum mechanics

Boonyapakron,

Keiser,

Prabmark

et al. 2024

Appl Microbiol Biotechnol

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Thermophilic xylanases catalyzing the cleavage of β-1,4-glycosidic bonds in xylan have applications in food, feed, biorefinery, and pulp industries. In this study, a hyperthermophilic endo-xylanase was obtained by further enhancement of thermal tolerance of a thermophilic GH11 xylanase originated from metagenome of bagasse pile based on rational design. Introducing N13F and Q34L to the previously reported X11P enzyme shifted the optimal working temperature to 85 °C and led to 20.7-fold improvement in thermostability at 90 °C along with a marked increase in T m to 93.3 °C. X11PNQ enzyme converted xylan to prebiotic xylooligosaccharides with high specificity on xylobiose to xylohexaose and high operational stability at 85 °C, resulting in 10.3-folds yield improvement compared to the parental enzyme. Molecular dynamic simulation and quantum mechanical analysis revealed improved H-bonding networks within GH11 xylanase principal domains and greater dynamic cross-correlations. A novel thermostabilization mechanism by π-amide interaction with slightly lower interaction energy than the native H-bond, but compensated by increased occurrence frequency was firstly demonstrated for thermophilic enzymes. The enzyme represents one of the most thermostable xylanases ever reported with biotechnological potential. Key points • Hyperthemophilic xylanase X11PNQ was obtained by rational design engineering. • X11PNQ showed specificity to prebiotic xylooligosaccharides (XOS) at 85 °C with improved t 1/2 at 90 °C. • Novel thermostabilization by π-amide interaction was demonstrated by MD/QM. Supplementary information The online version contains supplementary material available at 10.1007/s00253-024-13356-3.

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Synergistic action of lytic polysaccharide monooxygenase with glycoside hydrolase for lignocellulosic waste valorization: a review

Srivastava

Jhariya

Purohit

et al. 2021

Biomass Conv. Bioref.

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Identification and characterization of a novel AA9-type lytic polysaccharide monooxygenase from a bagasse metagenome

Cited by 7 publications

References 60 publications

Functional and Structural Characterizations of Lytic Polysaccharide Monooxygenase, Which Cooperates Synergistically with Cellulases, from Ceriporiopsis subvermispora

Functional and Structural Characterizations of Lytic Polysaccharide Monooxygenase, Which Cooperates Synergistically with Cellulases, from Ceriporiopsis subvermispora

Hyperthermophilic xylanase and thermophilicity analysis by molecular dynamic simulation with quantum mechanics

Synergistic action of lytic polysaccharide monooxygenase with glycoside hydrolase for lignocellulosic waste valorization: a review

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