Cloning of novel bacterial xylanases from lignocellulose-enriched compost metagenomic libraries

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http://hdl.handle.net/10138/305011

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Ellilä , S , Bromann , P , Nyyssönen , M , Itävaara , M , Koivula , A , Paulin , L & Kruus , K 2019 , ' Cloning of novel bacterial xylanases from lignocellulose-enriched compost metagenomic libraries ' , AMB Express , vol. 9 , no. 1 , 124 . https://doi.org/10.1186/s13568-019-0847-9

Title: Cloning of novel bacterial xylanases from lignocellulose-enriched compost metagenomic libraries
Author: Ellilä, Simo; Bromann, Paul; Nyyssönen, Mari; Itävaara, Merja; Koivula, Anu; Paulin, Lars; Kruus, Kristiina
Contributor: University of Helsinki, VTT Technical Research Center of Finland
University of Helsinki, Institute of Biotechnology
Date: 2019-08-05
Language: eng
Number of pages: 12
Belongs to series: AMB Express
ISSN: 2191-0855
URI: http://hdl.handle.net/10138/305011
Abstract: Xylanases are in important class of industrial enzymes that are essential for the complete hydrolysis of lignocellulosic biomass into fermentable sugars. In the present study, we report the cloning of novel xylanases with interesting properties from compost metagenomics libraries. Controlled composting of lignocellulosic materials was used to enrich the microbial population in lignocellulolytic organisms. DNA extracted from the compost samples was used to construct metagenomics libraries, which were screened for xylanase activity. In total, 40 clones exhibiting xylanase activity were identified and the thermostability of the discovered xylanases was assayed directly from the library clones. Five genes, including one belonging to the more rare family GH8, were selected for subcloning and the enzymes were expressed in recombinant form in E. coli. Preliminary characterization of the metagenome-derived xylanases revealed interesting properties of the novel enzymes, such as high thermostability and specific activity, and differences in hydrolysis profiles. One enzyme was found to perform better than a standard Trichoderma reesei xylanase in the hydrolysis of lignocellulose at elevated temperatures.
Subject: 1182 Biochemistry, cell and molecular biology
Xylanase
Metagenomics
Lignocellulose
Compost
Screening
Cloning
HYDROLASE FAMILY
SUBSTRATE SPECIFICITIES
ENZYMES
ENDOXYLANASE
HYDROLYSIS
DOMAINS
ETHANOL
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