Penicillium purpurogenum produces two GH family 43 enzymes with β-xylosidase activity, one monofunctional and the other bifunctional: Biochemical and structural analyses explain the difference

Ravanal, María Cristina; Alegría-Arcos, Melissa; González‐Nilo, Fernando; Eyzaguirre, Jaime

doi:10.1016/j.abb.2013.10.017

Cited by 23 publications

(16 citation statements)

References 41 publications

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“…Comparison of the genomic DNA and cDNA sequence, there were not introns in the encoding gene of xyl43 . This case also similar to the β-xylosidase genes derived from other filamentous fungus 19 , 20 . The deduced Xyl43 was encoded 348 residues with a theoretical molecular weight of 38.61 KDa, which is consistent with others of β-xylosidases from Paecilomyces thermophile 17 , 20 .…”

Section: Resultssupporting

confidence: 72%

“…Compared to the β-xylosidases reported from Penicillium sp . strains 19 , 27 and other fungal species 21 , 24 , 28 , this stability of the Xyl43 in the neutral and alkaline pH value was very important because it can be directly used in enzymatic hydrolysis process of neutral- and alkaline- pretreated agro-residues for high efficiency producing fermentable sugars by the synergy with alkali-xylanase 29 .…”

Section: Resultsmentioning

confidence: 99%

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Production and Characteristics of a Novel Xylose- and Alkali-tolerant GH 43 β-xylosidase from Penicillium oxalicum for Promoting Hemicellulose Degradation

Zhao

2017

Sci Rep

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β-xylosidase is a pivotal enzyme for complete degradation of xylan in hemicelluloses of lignocelluloses, and the xylose- and alkali-tolerant β-xylosidase with high catalytic activity is very attractive for promoting enzymatic hydrolysis of alkaline-pretreated lignocellulose. In this study, a novel intracellular glycoside hydrolase family 43 β-xylosidase gene (xyl43) from Penicillium oxalicum 114-2 was successfully high-level overexpressed in Pichia pastoris, and the secreted enzyme was characterized. The β-xylosidase Xyl43 exhibited great pH stability and high catalytic activity in the range of pH 6.0 to 8.0, and high tolerance to xylose with the Ki value of 28.09 mM. The Xyl43 could effectively promote enzymatic degradation of different source of xylan and hemicellulose contained in alkaline-pretreated corn stover, and high conversion of xylan to xylose could be obtained.

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Section: Resultssupporting

confidence: 72%

Section: Resultsmentioning

confidence: 99%

Production and Characteristics of a Novel Xylose- and Alkali-tolerant GH 43 β-xylosidase from Penicillium oxalicum for Promoting Hemicellulose Degradation

Zhao

2017

Sci Rep

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“…The GH43 xylosidases of Enterobacter sp. [33], Lactobacillus brevis [34], Lactobacillus rossiae DSM 15814 T [35], and Penicillium purpurogenum [36] have an optimum pH and temperature of approximately pH 6 and 40 °C, respectively, while the Selenomonas ruminantium enzyme has an optimal temperature of 40 °C but a lower optimum pH of 5.3 [37].…”

Section: General Characterization Of Rswu43amentioning

confidence: 99%

Identification and characterization of the first β-1,3-d-xylosidase from a gram-positive bacterium, Streptomyces sp. SWU10

Phuengmaung

Fujiwara

Sukhumsirichart

et al. 2018

Enzyme and Microbial Technology

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In previous reports, we characterized four endo-xylanases produced by Streptomyces sp. strain SWU10 that degrade xylans to several xylooligosaccharides. To obtain a set of enzymes to achieve complete xylan degradation, a β-d-xylosidase gene was cloned and expressed in Escherichia coli, and the recombinant protein, named rSWU43A, was characterized. SWU43A is composed of 522 amino acids and does not contain a signal peptide, indicating that the enzyme is an intracellular protein. SWU43A was revealed to contain a Glyco_hydro_43 domain and possess the three conserved amino acid residues of the glycoside hydrolase family 43 proteins. The molecular mass of rSWU43A purified by Ni-affinity column chromatography was estimated to be 60kDa. The optimum reaction conditions of rSWU43A were pH 6.5 and 40°C. The enzyme was stable up to 40°C over a wide pH range (3.1-8.9). rSWU43A activity was enhanced by Fe and Mn and inhibited by various metals (Ag, Cd, Co, Cu, Hg, Ni, and Zn), d-xylose, and l-arabinose. rSWU43A showed activity on p-nitrophenyl-β-d-xylopyranoside and p-nitrophenyl-α-l-arabinofuranoside substrates, with specific activities of 0.09 and 0.06U/mg, respectively, but not on any xylosidic or arabinosidic polymers. rSWU43A efficiently degraded β-1,3-xylooligosaccharides to produce xylose but showed little activity towards β-1,4-xylobiose, with specific activities of 1.33 and 0.003U/mg, respectively. These results demonstrate that SWU43A is a β-1,3-d-xylosidase (EC 3.2.1.72), which to date has only been described in the marine bacterium Vibrio sp. Therefore, rSWU43A of Streptomyces sp. is the first β-1,3-xylosidase found in gram-positive bacteria. SWU43A could be useful as a specific tool for the structural elucidation and production of xylose from β-1,3-xylan in seaweed cell walls.

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“…The main chain of xylan is composed of 1,4- d -xylose subunits, which is usually decorated with various side chain residues of 1,2-α- d -glucuronic acid, or its 4- O -methyl ethers, 1,3-α- l -arabinose, and/or O -acetyl groups in the 2 and 3 positions. Due to structural complexity, several xylanolytic enzymes are required to release the substituents and sugars from the various xylans, including endo-1,4-β-xylanases (EC 3.2.1.8) [7], acetyl xylan esterases (EC 3.1.1.72) [8], feruloyl esterases (EC 3.1.1.73) [9], α- l -arabinofuranosidases (EC 3.2.1.55) [10], α-glucuronidases (EC 3.2.1.139) [11], and β- d -xylosidase (EC 3.2.1.37) [12]. Among these enzymes, endo-1,4-β-xylanases are believed to be the most valuable in industrial applications.…”

Section: Introductionmentioning

confidence: 99%

Molecular Modeling and MM-PBSA Free Energy Analysis of Endo-1,4-β-Xylanase from Ruminococcus albus 8

Zhan

Jin

et al. 2014

IJMS

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Endo-1,4-β-xylanase (EC 3.2.1.8) is the enzyme from Ruminococcus albus 8 (R. albus 8) (Xyn10A), and catalyzes the degradation of arabinoxylan, which is a major cell wall non-starch polysaccharide of cereals. The crystallographic structure of Xyn10A is still unknown. For this reason, we report a computer-assisted homology study conducted to build its three-dimensional structure based on the known sequence of amino acids of this enzyme. In this study, the best similarity was found with the Clostridium thermocellum (C. thermocellum) N-terminal endo-1,4-β-d-xylanase 10 b. Following the 100 ns molecular dynamics (MD) simulation, a reliable model was obtained for further studies. Molecular Mechanics/Poisson-Boltzmann Surface Area (MM-PBSA) methods were used for the substrate xylotetraose having the reactive sugar, which was bound in the −1 subsite of Xyn10A in the 4C1 (chair) and 2SO (skew boat) ground state conformations. According to the simulations and free energy analysis, Xyn10A binds the substrate with the −1 sugar in the 2SO conformation 39.27 kcal·mol−1 tighter than the substrate with the sugar in the 4C1 conformation. According to the Xyn10A-2SO Xylotetraose (X4(sb) interaction energies, the most important subsite for the substrate binding is subsite −1. The results of this study indicate that the substrate is bound in a skew boat conformation with Xyn10A and the −1 sugar subsite proceeds from the 4C1 conformation through 2SO to the transition state. MM-PBSA free energy analysis indicates that Asn187 and Trp344 in subsite −1 may an important residue for substrate binding. Our findings provide fundamental knowledge that may contribute to further enhancement of enzyme performance through molecular engineering.

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Penicillium purpurogenum produces two GH family 43 enzymes with β-xylosidase activity, one monofunctional and the other bifunctional: Biochemical and structural analyses explain the difference

Cited by 23 publications

References 41 publications

Production and Characteristics of a Novel Xylose- and Alkali-tolerant GH 43 β-xylosidase from Penicillium oxalicum for Promoting Hemicellulose Degradation

Production and Characteristics of a Novel Xylose- and Alkali-tolerant GH 43 β-xylosidase from Penicillium oxalicum for Promoting Hemicellulose Degradation

Identification and characterization of the first β-1,3-d-xylosidase from a gram-positive bacterium, Streptomyces sp. SWU10

Molecular Modeling and MM-PBSA Free Energy Analysis of Endo-1,4-β-Xylanase from Ruminococcus albus 8

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