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1
Thermostable microbial xylanases for pulp and paper industries: trends, applications and further perspectives
Thermostable microbial xylanases for pulp and paper industries: trends, applications and further perspectives
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Thermostable microbial xylanases for pulp and paper industries: trends, applications and further perspectives

World Journal of Microbiology and Biotechnology, 2016-02, Vol.32 (2), p.34, Article 34 [Peer Reviewed Journal]

Springer Science+Business Media Dordrecht 2016 ;ISSN: 0959-3993 ;EISSN: 1573-0972 ;DOI: 10.1007/s11274-015-2005-0 ;PMID: 26754672

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2
Heterologous expression and structure prediction of a xylanase identified from a compost metagenomic library
Heterologous expression and structure prediction of a xylanase identified from a compost metagenomic library
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Heterologous expression and structure prediction of a xylanase identified from a compost metagenomic library

Applied microbiology and biotechnology, 2024-05, Vol.108 (1) [Peer Reviewed Journal]

The Author(s) 2024 ;ISSN: 0175-7598 ;EISSN: 1432-0614 ;DOI: 10.1007/s00253-024-13169-4

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3
Characterization of a novel GH30 non-specific endoxylanase AcXyn30B from Acetivibrio clariflavus
Characterization of a novel GH30 non-specific endoxylanase AcXyn30B from Acetivibrio clariflavus
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Characterization of a novel GH30 non-specific endoxylanase AcXyn30B from Acetivibrio clariflavus

Applied microbiology and biotechnology, 2024-12, Vol.108 (1) [Peer Reviewed Journal]

The Author(s) 2024 ;ISSN: 0175-7598 ;EISSN: 1432-0614 ;DOI: 10.1007/s00253-024-13155-w

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4
Improvement of bread making quality by supplementation with a recombinant xylanase produced by Pichia pastoris
Improvement of bread making quality by supplementation with a recombinant xylanase produced by Pichia pastoris
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Improvement of bread making quality by supplementation with a recombinant xylanase produced by Pichia pastoris

PloS one, 2018-02, Vol.13 (2), p.e0192996-e0192996 [Peer Reviewed Journal]

COPYRIGHT 2018 Public Library of Science ;COPYRIGHT 2018 Public Library of Science ;2018 de Queiroz Brito Cunha et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2018 de Queiroz Brito Cunha et al 2018 de Queiroz Brito Cunha et al ;ISSN: 1932-6203 ;EISSN: 1932-6203 ;DOI: 10.1371/journal.pone.0192996 ;PMID: 29481569

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5
Characterization of a novel xylanase from an extreme temperature hot spring metagenome for xylooligosaccharide production
Characterization of a novel xylanase from an extreme temperature hot spring metagenome for xylooligosaccharide production
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Characterization of a novel xylanase from an extreme temperature hot spring metagenome for xylooligosaccharide production

Applied microbiology and biotechnology, 2020-06, Vol.104 (11), p.4889-4901 [Peer Reviewed Journal]

Springer-Verlag GmbH Germany, part of Springer Nature 2020 ;COPYRIGHT 2020 Springer ;Springer-Verlag GmbH Germany, part of Springer Nature 2020. ;ISSN: 0175-7598 ;EISSN: 1432-0614 ;DOI: 10.1007/s00253-020-10562-7 ;PMID: 32249395

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6
High-Level Heterologous Expression of Endo-1,4-β-Xylanase from Penicillium citrinum in Pichia pastoris X-33 Directed through Codon Optimization and Optimized Expression
High-Level Heterologous Expression of Endo-1,4-β-Xylanase from Penicillium citrinum in Pichia pastoris X-33 Directed through Codon Optimization and Optimized Expression
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High-Level Heterologous Expression of Endo-1,4-β-Xylanase from Penicillium citrinum in Pichia pastoris X-33 Directed through Codon Optimization and Optimized Expression

Molecules (Basel, Switzerland), 2019-09, Vol.24 (19), p.3515 [Peer Reviewed Journal]

2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;Distributed under a Creative Commons Attribution 4.0 International License ;2019 by the authors. 2019 ;ISSN: 1420-3049 ;EISSN: 1420-3049 ;DOI: 10.3390/molecules24193515 ;PMID: 31569777

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7
The contribution of specific subsites to catalytic activities in active site architecture of a GH11 xylanase
The contribution of specific subsites to catalytic activities in active site architecture of a GH11 xylanase
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The contribution of specific subsites to catalytic activities in active site architecture of a GH11 xylanase

Applied microbiology and biotechnology, 2020-10, Vol.104 (20), p.8735-8745 [Peer Reviewed Journal]

Springer-Verlag GmbH Germany, part of Springer Nature 2020 ;COPYRIGHT 2020 Springer ;ISSN: 0175-7598 ;EISSN: 1432-0614 ;DOI: 10.1007/s00253-020-10865-9 ;PMID: 32865611

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8
Microbial diversity analysis and screening for novel xylanase enzymes from the sediment of the Lobios Hot Spring in Spain
Microbial diversity analysis and screening for novel xylanase enzymes from the sediment of the Lobios Hot Spring in Spain
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Microbial diversity analysis and screening for novel xylanase enzymes from the sediment of the Lobios Hot Spring in Spain

Scientific reports, 2019-08, Vol.9 (1), p.11195-12, Article 11195 [Peer Reviewed Journal]

2019. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2019 ;ISSN: 2045-2322 ;EISSN: 2045-2322 ;DOI: 10.1038/s41598-019-47637-z ;PMID: 31371784

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9
Characterization of recombinant endo-1,4-β-xylanase of Bacillus halodurans C-125 and rational identification of hot spot amino acid residues responsible for enhancing thermostability by an in-silico approach
Characterization of recombinant endo-1,4-β-xylanase of Bacillus halodurans C-125 and rational identification of hot spot amino acid residues responsible for enhancing thermostability by an in-silico approach
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Characterization of recombinant endo-1,4-β-xylanase of Bacillus halodurans C-125 and rational identification of hot spot amino acid residues responsible for enhancing thermostability by an in-silico approach

Molecular biology reports, 2019-08, Vol.46 (4), p.3651-3662 [Peer Reviewed Journal]

Springer Nature B.V. 2019 ;Molecular Biology Reports is a copyright of Springer, (2019). All Rights Reserved. ;ISSN: 0301-4851 ;EISSN: 1573-4978 ;DOI: 10.1007/s11033-019-04751-5 ;PMID: 31079316

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10
Design, expression and functional characterization of a thermostable xylanase from Trichoderma reesei
Design, expression and functional characterization of a thermostable xylanase from Trichoderma reesei
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Design, expression and functional characterization of a thermostable xylanase from Trichoderma reesei

PloS one, 2019-01, Vol.14 (1), p.e0210548 [Peer Reviewed Journal]

COPYRIGHT 2019 Public Library of Science ;COPYRIGHT 2019 Public Library of Science ;2019 He et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2019 He et al 2019 He et al ;ISSN: 1932-6203 ;EISSN: 1932-6203 ;DOI: 10.1371/journal.pone.0210548 ;PMID: 30650138

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11
Xylanase production by Thermobacillus xylanilyticus is impaired by population diversification but can be mitigated based on the management of cheating behavior
Xylanase production by Thermobacillus xylanilyticus is impaired by population diversification but can be mitigated based on the management of cheating behavior
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Xylanase production by Thermobacillus xylanilyticus is impaired by population diversification but can be mitigated based on the management of cheating behavior

Microbial cell factories, 2022-03, Vol.21 (1), p.39-39, Article 39 [Peer Reviewed Journal]

2022. The Author(s). ;COPYRIGHT 2022 BioMed Central Ltd. ;Attribution ;The Author(s) 2022 ;ISSN: 1475-2859 ;EISSN: 1475-2859 ;DOI: 10.1186/s12934-022-01762-z ;PMID: 35292016

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12
Development of bio-based xylan composites for food packaging applications
Development of bio-based xylan composites for food packaging applications
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Development of bio-based xylan composites for food packaging applications

Nelson Mandela University

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13
Multimodularity of a GH10 Xylanase Found in the Termite Gut Metagenome
Multimodularity of a GH10 Xylanase Found in the Termite Gut Metagenome
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Multimodularity of a GH10 Xylanase Found in the Termite Gut Metagenome

Applied and environmental microbiology, 2021-01, Vol.87 (3), p.1 [Peer Reviewed Journal]

Copyright © 2021 Wu et al. ;Copyright American Society for Microbiology Feb 2021 ;Attribution ;Copyright © 2021 Wu et al. 2021 Wu et al. ;ISSN: 0099-2240 ;EISSN: 1098-5336 ;DOI: 10.1128/AEM.01714-20 ;PMID: 33187992

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14
Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose
Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose
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Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose

The Journal of biological chemistry, 2017-11, Vol.292 (47), p.19315-19327 [Peer Reviewed Journal]

2017 © 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. 2017 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M117.807768 ;PMID: 28974575

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15
N- and C-terminal truncations of a GH10 xylanase significantly increase its activity and thermostability but decrease its SDS resistance
N- and C-terminal truncations of a GH10 xylanase significantly increase its activity and thermostability but decrease its SDS resistance
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N- and C-terminal truncations of a GH10 xylanase significantly increase its activity and thermostability but decrease its SDS resistance

Applied microbiology and biotechnology, 2016-04, Vol.100 (8), p.3555-3565 [Peer Reviewed Journal]

Springer-Verlag Berlin Heidelberg 2015 ;COPYRIGHT 2016 Springer ;Springer-Verlag Berlin Heidelberg 2016 ;ISSN: 0175-7598 ;EISSN: 1432-0614 ;DOI: 10.1007/s00253-015-7176-y ;PMID: 26621803

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16
Discovery of a Thermostable GH10 Xylanase with Broad Substrate Specificity from the Arctic Mid-Ocean Ridge Vent System
Discovery of a Thermostable GH10 Xylanase with Broad Substrate Specificity from the Arctic Mid-Ocean Ridge Vent System
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Discovery of a Thermostable GH10 Xylanase with Broad Substrate Specificity from the Arctic Mid-Ocean Ridge Vent System

Applied and environmental microbiology, 2019-03, Vol.85 (6) [Peer Reviewed Journal]

Copyright © 2019 American Society for Microbiology. ;Copyright American Society for Microbiology Mar 2019 ;Copyright © 2019 American Society for Microbiology. 2019 American Society for Microbiology ;ISSN: 0099-2240 ;EISSN: 1098-5336 ;DOI: 10.1128/AEM.02970-18 ;PMID: 30635385

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17
Xylanase XYN IV from Trichoderma reesei showing exo‐ and endo‐xylanase activity
Xylanase XYN IV from Trichoderma reesei showing exo‐ and endo‐xylanase activity
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Xylanase XYN IV from Trichoderma reesei showing exo‐ and endo‐xylanase activity

The FEBS journal, 2013-01, Vol.280 (1), p.285-301 [Peer Reviewed Journal]

2012 The Authors Journal compilation © 2012 FEBS ;2012 The Authors Journal compilation © 2012 FEBS. ;ISSN: 1742-464X ;EISSN: 1742-4658 ;DOI: 10.1111/febs.12069 ;PMID: 23167779

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18
Cloning, Purification, and Characterization of Recombinant Thermostable β-Xylanase Tnap_0700 from Thermotoga naphthophila
Cloning, Purification, and Characterization of Recombinant Thermostable β-Xylanase Tnap_0700 from Thermotoga naphthophila
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Cloning, Purification, and Characterization of Recombinant Thermostable β-Xylanase Tnap_0700 from Thermotoga naphthophila

Applied biochemistry and biotechnology, 2019-12, Vol.189 (4), p.1274-1290 [Peer Reviewed Journal]

Springer Science+Business Media, LLC, part of Springer Nature 2019 ;Applied Biochemistry and Biotechnology is a copyright of Springer, (2019). All Rights Reserved. ;ISSN: 0273-2289 ;EISSN: 1559-0291 ;DOI: 10.1007/s12010-019-03068-0 ;PMID: 31240547

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19
A novel bacterial GH30 xylobiohydrolase from Hungateiclostridium clariflavum
A novel bacterial GH30 xylobiohydrolase from Hungateiclostridium clariflavum
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A novel bacterial GH30 xylobiohydrolase from Hungateiclostridium clariflavum

Applied microbiology and biotechnology, 2021, Vol.105 (1), p.185-195 [Peer Reviewed Journal]

Springer-Verlag GmbH Germany, part of Springer Nature 2020 ;COPYRIGHT 2021 Springer ;Springer-Verlag GmbH Germany, part of Springer Nature 2020. ;ISSN: 0175-7598 ;EISSN: 1432-0614 ;DOI: 10.1007/s00253-020-11023-x ;PMID: 33215261

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20
Xylanase Inhibitors: Defense Players in Plant Immunity with Implications in Agro-Industrial Processing
Xylanase Inhibitors: Defense Players in Plant Immunity with Implications in Agro-Industrial Processing
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Xylanase Inhibitors: Defense Players in Plant Immunity with Implications in Agro-Industrial Processing

International journal of molecular sciences, 2022-11, Vol.23 (23), p.14994 [Peer Reviewed Journal]

2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2022 by the authors. 2022 ;ISSN: 1422-0067 ;ISSN: 1661-6596 ;EISSN: 1422-0067 ;DOI: 10.3390/ijms232314994 ;PMID: 36499321

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