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Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-β-xylanase identified in a microbial consortium

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Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-β-xylanase identified in a microbial consortium. / Evangelista, Danilo Elton; de Oliveira Arnoldi Pellegrini, Vanessa; Espirito Santo, Melissa; McQueen Mason, Simon John; Bruce, Neil Charles; Polikarpov, Igor.

In: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, Vol. 103, No. 19, 01.10.2019, p. 8035-8049.

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Harvard

Evangelista, DE, de Oliveira Arnoldi Pellegrini, V, Espirito Santo, M, McQueen Mason, SJ, Bruce, NC & Polikarpov, I 2019, 'Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-β-xylanase identified in a microbial consortium', APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, vol. 103, no. 19, pp. 8035-8049. https://doi.org/10.1007/s00253-019-10033-8

APA

Evangelista, D. E., de Oliveira Arnoldi Pellegrini, V., Espirito Santo, M., McQueen Mason, S. J., Bruce, N. C., & Polikarpov, I. (2019). Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-β-xylanase identified in a microbial consortium. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 103(19), 8035-8049. https://doi.org/10.1007/s00253-019-10033-8

Vancouver

Evangelista DE, de Oliveira Arnoldi Pellegrini V, Espirito Santo M, McQueen Mason SJ, Bruce NC, Polikarpov I. Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-β-xylanase identified in a microbial consortium. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY. 2019 Oct 1;103(19):8035-8049. https://doi.org/10.1007/s00253-019-10033-8

Author

Evangelista, Danilo Elton ; de Oliveira Arnoldi Pellegrini, Vanessa ; Espirito Santo, Melissa ; McQueen Mason, Simon John ; Bruce, Neil Charles ; Polikarpov, Igor. / Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-β-xylanase identified in a microbial consortium. In: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY. 2019 ; Vol. 103, No. 19. pp. 8035-8049.

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@article{79bc0c890a734056bc3953f81d3e1940,
title = "Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-β-xylanase identified in a microbial consortium",
abstract = "Biotechnologies that aim to produce renewable fuels, chemicals, and bioproducts from residual ligno(hemi)cellulosic biomass mostly rely on enzymatic depolymerization of plant cell walls (PCW). This process requires an arsenal of diverse enzymes, including xylanases, which synergistically act on the hemicellulose, reducing the long and complex xylan chains to oligomers and simple sugars. Thus, xylanases play a crucial role in PCW depolymerization. Until recently, the largest xylanase family, glycoside hydrolase family 11 (GH11) has been exclusively represented by endo-catalytic β-1,4- and β-1,3-xylanases. Analysis of a metatranscriptome library from a microbial lignocellulose community resulted in the identification of an unusual exo-acting GH11 β-1,4-xylanase (MetXyn11). Detailed characterization has been performed on recombinant MetXyn11 including determination of its low-resolution small angle Xray scattering (SAXS) molecular envelope in solution. Our results reveal that MetXyn11 is a monomeric globular enzyme that liberates xylobiose from heteroxylans as the only product. MetXyn11 has an optimal activity in a pH range from 6 to 9 and an optimal temperature of 50 oC. The enzyme maintained above 65{\%} of its original activity in the pH range 5 to 6 after being incubated for 72 h at 50 oC. Addition of the enzyme to a commercial enzymatic cocktail (CelicCtec3) promoted a significant increase of enzymatic hydrolysis yields of hydrothermally pretreated sugarcane bagasse (16{\%} after 24 h of hydrolysis).",
keywords = "Biochemical characterization, GH11 exo-β-1,4-xylanase, Metatranscriptome, Small-Angle X-ray scattering, Synergism",
author = "Evangelista, {Danilo Elton} and {de Oliveira Arnoldi Pellegrini}, Vanessa and {Espirito Santo}, Melissa and {McQueen Mason}, {Simon John} and Bruce, {Neil Charles} and Igor Polikarpov",
note = "{\circledC} Springer-Verlag GmbH Germany, part of Springer Nature 2019. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details",
year = "2019",
month = "10",
day = "1",
doi = "10.1007/s00253-019-10033-8",
language = "English",
volume = "103",
pages = "8035--8049",
journal = "APPLIED MICROBIOLOGY AND BIOTECHNOLOGY",
issn = "0175-7598",
publisher = "Springer Verlag",
number = "19",

}

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TY - JOUR

T1 - Biochemical characterization and low-resolution SAXS shape of a novel GH11 exo-1,4-β-xylanase identified in a microbial consortium

AU - Evangelista, Danilo Elton

AU - de Oliveira Arnoldi Pellegrini, Vanessa

AU - Espirito Santo, Melissa

AU - McQueen Mason, Simon John

AU - Bruce, Neil Charles

AU - Polikarpov, Igor

N1 - © Springer-Verlag GmbH Germany, part of Springer Nature 2019. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details

PY - 2019/10/1

Y1 - 2019/10/1

N2 - Biotechnologies that aim to produce renewable fuels, chemicals, and bioproducts from residual ligno(hemi)cellulosic biomass mostly rely on enzymatic depolymerization of plant cell walls (PCW). This process requires an arsenal of diverse enzymes, including xylanases, which synergistically act on the hemicellulose, reducing the long and complex xylan chains to oligomers and simple sugars. Thus, xylanases play a crucial role in PCW depolymerization. Until recently, the largest xylanase family, glycoside hydrolase family 11 (GH11) has been exclusively represented by endo-catalytic β-1,4- and β-1,3-xylanases. Analysis of a metatranscriptome library from a microbial lignocellulose community resulted in the identification of an unusual exo-acting GH11 β-1,4-xylanase (MetXyn11). Detailed characterization has been performed on recombinant MetXyn11 including determination of its low-resolution small angle Xray scattering (SAXS) molecular envelope in solution. Our results reveal that MetXyn11 is a monomeric globular enzyme that liberates xylobiose from heteroxylans as the only product. MetXyn11 has an optimal activity in a pH range from 6 to 9 and an optimal temperature of 50 oC. The enzyme maintained above 65% of its original activity in the pH range 5 to 6 after being incubated for 72 h at 50 oC. Addition of the enzyme to a commercial enzymatic cocktail (CelicCtec3) promoted a significant increase of enzymatic hydrolysis yields of hydrothermally pretreated sugarcane bagasse (16% after 24 h of hydrolysis).

AB - Biotechnologies that aim to produce renewable fuels, chemicals, and bioproducts from residual ligno(hemi)cellulosic biomass mostly rely on enzymatic depolymerization of plant cell walls (PCW). This process requires an arsenal of diverse enzymes, including xylanases, which synergistically act on the hemicellulose, reducing the long and complex xylan chains to oligomers and simple sugars. Thus, xylanases play a crucial role in PCW depolymerization. Until recently, the largest xylanase family, glycoside hydrolase family 11 (GH11) has been exclusively represented by endo-catalytic β-1,4- and β-1,3-xylanases. Analysis of a metatranscriptome library from a microbial lignocellulose community resulted in the identification of an unusual exo-acting GH11 β-1,4-xylanase (MetXyn11). Detailed characterization has been performed on recombinant MetXyn11 including determination of its low-resolution small angle Xray scattering (SAXS) molecular envelope in solution. Our results reveal that MetXyn11 is a monomeric globular enzyme that liberates xylobiose from heteroxylans as the only product. MetXyn11 has an optimal activity in a pH range from 6 to 9 and an optimal temperature of 50 oC. The enzyme maintained above 65% of its original activity in the pH range 5 to 6 after being incubated for 72 h at 50 oC. Addition of the enzyme to a commercial enzymatic cocktail (CelicCtec3) promoted a significant increase of enzymatic hydrolysis yields of hydrothermally pretreated sugarcane bagasse (16% after 24 h of hydrolysis).

KW - Biochemical characterization

KW - GH11 exo-β-1,4-xylanase

KW - Metatranscriptome

KW - Small-Angle X-ray scattering

KW - Synergism

UR - http://www.scopus.com/inward/record.url?scp=85070909182&partnerID=8YFLogxK

U2 - 10.1007/s00253-019-10033-8

DO - 10.1007/s00253-019-10033-8

M3 - Article

VL - 103

SP - 8035

EP - 8049

JO - APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

T2 - APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

JF - APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

SN - 0175-7598

IS - 19

ER -