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Microbial xylanases and their industrial application in pulp and paper biobleaching: a review

Xylanases are hydrolytic enzymes which cleave the β-1, 4 backbone of the complex plant cell wall polysaccharide xylan. Xylan is the major hemicellulosic constituent found in soft and hard food. It is the next most abundant renewable polysaccharide after cellulose. Xylanases and associated debranchin...

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Autores principales: Walia, Abhishek, Guleria, Shiwani, Mehta, Preeti, Chauhan, Anjali, Parkash, Jyoti
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5385172/
https://www.ncbi.nlm.nih.gov/pubmed/28391477
http://dx.doi.org/10.1007/s13205-016-0584-6
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author Walia, Abhishek
Guleria, Shiwani
Mehta, Preeti
Chauhan, Anjali
Parkash, Jyoti
author_facet Walia, Abhishek
Guleria, Shiwani
Mehta, Preeti
Chauhan, Anjali
Parkash, Jyoti
author_sort Walia, Abhishek
collection PubMed
description Xylanases are hydrolytic enzymes which cleave the β-1, 4 backbone of the complex plant cell wall polysaccharide xylan. Xylan is the major hemicellulosic constituent found in soft and hard food. It is the next most abundant renewable polysaccharide after cellulose. Xylanases and associated debranching enzymes produced by a variety of microorganisms including bacteria, actinomycetes, yeast and fungi bring hydrolysis of hemicelluloses. Despite thorough knowledge of microbial xylanolytic systems, further studies are required to achieve a complete understanding of the mechanism of xylan degradation by xylanases produced by microorganisms and their promising use in pulp biobleaching. Cellulase-free xylanases are important in pulp biobleaching as alternatives to the use of toxic chlorinated compounds because of the environmental hazards and diseases caused by the release of the adsorbable organic halogens. In this review, we have focused on the studies of structural composition of xylan in plants, their classification, sources of xylanases, extremophilic xylanases, modes of fermentation for the production of xylanases, factors affecting xylanase production, statistical approaches such as Plackett Burman, Response Surface Methodology to enhance xylanase production, purification, characterization, molecular cloning and expression. Besides this, review has focused on the microbial enzyme complex involved in the complete breakdown of xylan and the studies on xylanase regulation and their potential industrial applications with special reference to pulp biobleaching, which is directly related to increasing pulp brightness and reduction in environmental pollution.
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spelling pubmed-53851722017-04-20 Microbial xylanases and their industrial application in pulp and paper biobleaching: a review Walia, Abhishek Guleria, Shiwani Mehta, Preeti Chauhan, Anjali Parkash, Jyoti 3 Biotech Review Article Xylanases are hydrolytic enzymes which cleave the β-1, 4 backbone of the complex plant cell wall polysaccharide xylan. Xylan is the major hemicellulosic constituent found in soft and hard food. It is the next most abundant renewable polysaccharide after cellulose. Xylanases and associated debranching enzymes produced by a variety of microorganisms including bacteria, actinomycetes, yeast and fungi bring hydrolysis of hemicelluloses. Despite thorough knowledge of microbial xylanolytic systems, further studies are required to achieve a complete understanding of the mechanism of xylan degradation by xylanases produced by microorganisms and their promising use in pulp biobleaching. Cellulase-free xylanases are important in pulp biobleaching as alternatives to the use of toxic chlorinated compounds because of the environmental hazards and diseases caused by the release of the adsorbable organic halogens. In this review, we have focused on the studies of structural composition of xylan in plants, their classification, sources of xylanases, extremophilic xylanases, modes of fermentation for the production of xylanases, factors affecting xylanase production, statistical approaches such as Plackett Burman, Response Surface Methodology to enhance xylanase production, purification, characterization, molecular cloning and expression. Besides this, review has focused on the microbial enzyme complex involved in the complete breakdown of xylan and the studies on xylanase regulation and their potential industrial applications with special reference to pulp biobleaching, which is directly related to increasing pulp brightness and reduction in environmental pollution. Springer Berlin Heidelberg 2017-04-08 2017-05 /pmc/articles/PMC5385172/ /pubmed/28391477 http://dx.doi.org/10.1007/s13205-016-0584-6 Text en © The Author(s) 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Review Article
Walia, Abhishek
Guleria, Shiwani
Mehta, Preeti
Chauhan, Anjali
Parkash, Jyoti
Microbial xylanases and their industrial application in pulp and paper biobleaching: a review
title Microbial xylanases and their industrial application in pulp and paper biobleaching: a review
title_full Microbial xylanases and their industrial application in pulp and paper biobleaching: a review
title_fullStr Microbial xylanases and their industrial application in pulp and paper biobleaching: a review
title_full_unstemmed Microbial xylanases and their industrial application in pulp and paper biobleaching: a review
title_short Microbial xylanases and their industrial application in pulp and paper biobleaching: a review
title_sort microbial xylanases and their industrial application in pulp and paper biobleaching: a review
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5385172/
https://www.ncbi.nlm.nih.gov/pubmed/28391477
http://dx.doi.org/10.1007/s13205-016-0584-6
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