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Plant polysaccharide degrading enzyme system of Thermobifida cellulosilytica TB100<sup>T</sup> revealed by de novo genome project data

Tóth, Á. and Baka, E. and Luzics, Sz. and Bata-Vidács, I. and Nagy, I. and Bálint, B. and Herczeg, R. and Olasz, F. and Wilk, T. and Nagy, T. and Kriszt, B. and Nagy, I. and Kukolya, J. (2017) Plant polysaccharide degrading enzyme system of Thermobifida cellulosilytica TB100<sup>T</sup> revealed by de novo genome project data. Acta Alimentaria, 46 (3). pp. 323-335. ISSN 0139-3006

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Abstract

Thermobifidas are thermophilic, aerobic, lignocellulose decomposing actinomycetes. The Thermobifida genus includes four species: T. fusca, T. alba, T. cellulosilytica, and T. halotolerans. T. fusca YX is the far best characterized strain of this taxon and several cellulases and hemicellulases have been cloned from it for industrial purposes targeting paper industry, biofuel, and feed applications. Unfortunately, sequence data of such enzymes are almost exclusively restricted to this single species; however, we demonstrated earlier by zymography that other T. alba and T. cellulosilytica strains encode the same enzyme sets. Recently, the advances in whole genome sequencing by the use of next generation genomics platforms accelerated the selection process of valuable hydrolases from uncharacterized bacterial species for cloning purposes. For this purpose T. cellulosilytica TB100<sup>T</sup> type strain was chosen for de novo genome sequencing. We have assembled the genome of T. cellulosilytica strain TB100<sup>T</sup> into 168 contigs and 19 scaffolds, with reference length of 4 327 869 bps, 3 589 putative coding sequences, 53 tRNAs, and 4 rRNAs. The analysis of the annotated genome revealed the existence of 27 putative hydrolases belonging to 14 different glycoside hydrolase (GH) families. The investigation of identified, cloned, and heterologously multiple cellulases, mannanases, xylanases, and amylases may result in industrial applications beside gaining useful basic research related information.

Item Type: Article
Subjects: Q Science / természettudomány > QD Chemistry / kémia > QD01 Analytical chemistry / analitikai kémia
Depositing User: Erika Bilicsi
Date Deposited: 18 Aug 2017 11:30
Last Modified: 30 Sep 2018 23:15
URI: http://real.mtak.hu/id/eprint/60150

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