Literature DB >> 29343191

Thermophilic xylanases: from bench to bottle.

Abdul Basit1, Junquan Liu1, Kashif Rahim2, Wei Jiang1, Huiqiang Lou1.   

Abstract

Lignocellulosic biomass is a valuable raw material. As technology has evolved, industrial interest in new ways to take advantage of this raw material has grown. Biomass is treated with different microbial cells or enzymes under ideal industrial conditions to produce the desired products. Xylanases are the key enzymes that degrade the xylosidic linkages in the xylan backbone of the biomass, and commercial enzymes are categorized into different glycoside hydrolase families. Thermophilic microorganisms are excellent sources of industrially relevant thermostable enzymes that can withstand the harsh conditions of industrial processing. Thermostable xylanases display high-specific activity at elevated temperatures and distinguish themselves in biochemical properties, structures, and modes of action from their mesophilic counterparts. Natural xylanases can be further improved through genetic engineering. Rapid progress with genome editing, writing, and synthetic biological techniques have provided unlimited potential to produce thermophilic xylanases in their natural hosts or cell factories including bacteria, yeasts, and filamentous fungi. This review will discuss the biotechnological potential of xylanases from thermophilic microorganisms and the ways they are being optimized and produced for various industrial applications.

Entities:  

Keywords:  Thermophilic xylanases; expression and engineering; industrial applications

Mesh:

Substances:

Year:  2018        PMID: 29343191     DOI: 10.1080/07388551.2018.1425662

Source DB:  PubMed          Journal:  Crit Rev Biotechnol        ISSN: 0738-8551            Impact factor:   8.429


  7 in total

1.  Characterization of a novel cold-active xylanase from Luteimonas species.

Authors:  Zhenggang Han; Fang Shang-Guan; Jiangke Yang
Journal:  World J Microbiol Biotechnol       Date:  2018-07-27       Impact factor: 3.312

2.  High-temperature behavior of hyperthermostable Thermotoga maritima xylanase XYN10B after designed and evolved mutations.

Authors:  Yawei Wang; Jing Wang; Zhongqiang Zhang; Jiangke Yang; Ossi Turunen; Hairong Xiong
Journal:  Appl Microbiol Biotechnol       Date:  2022-02-16       Impact factor: 4.813

3.  A survey of substrate specificity among Auxiliary Activity Family 5 copper radical oxidases.

Authors:  Maria E Cleveland; Yann Mathieu; David Ribeaucourt; Mireille Haon; Paul Mulyk; Jason E Hein; Mickael Lafond; Jean-Guy Berrin; Harry Brumer
Journal:  Cell Mol Life Sci       Date:  2021-11-05       Impact factor: 9.261

4.  Characterization of a novel thermophilic metagenomic GH5 endoglucanase heterologously expressed in Escherichia coli and Saccharomyces cerevisiae.

Authors:  Juan-José Escuder-Rodríguez; María González-Suarez; María-Eugenia deCastro; Almudena Saavedra-Bouza; Manuel Becerra; María-Isabel González-Siso
Journal:  Biotechnol Biofuels Bioprod       Date:  2022-07-07

5.  Mutagenesis of N-terminal residues confer thermostability on a Penicillium janthinellum MA21601 xylanase.

Authors:  Ke Xiong; Jie Hou; Yuefeng Jiang; Xiuting Li; Chao Teng; Qin Li; Guangsen Fan; Ran Yang; Chengnan Zhang
Journal:  BMC Biotechnol       Date:  2019-07-25       Impact factor: 2.563

6.  Characterization of a new bifunctional endo-1,4-β-xylanase/esterase found in the rumen metagenome.

Authors:  Gabriella Cavazzini Pavarina; Eliana Gertrudes de Macedo Lemos; Natália Sarmanho Monteiro Lima; João Martins Pizauro
Journal:  Sci Rep       Date:  2021-05-17       Impact factor: 4.379

7.  Biochemical characterization of a novel acidophilic β-xylanase from Trichoderma asperellum ND-1 and its synergistic hydrolysis of beechwood xylan.

Authors:  Fengzhen Zheng; Abdul Basit; Huan Zhuang; Jun Chen; Jianfen Zhang; Weiqing Chen
Journal:  Front Microbiol       Date:  2022-09-15       Impact factor: 6.064

  7 in total

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