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Decoding the complete arsenal for cellulose and hemicellulose deconstruction in the highly efficient cellulose decomposer Paenibacillus O199

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F16%3A00469004" target="_blank" >RIV/61388971:_____/16:00469004 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1186/s13068-016-0518-x" target="_blank" >http://dx.doi.org/10.1186/s13068-016-0518-x</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1186/s13068-016-0518-x" target="_blank" >10.1186/s13068-016-0518-x</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Decoding the complete arsenal for cellulose and hemicellulose deconstruction in the highly efficient cellulose decomposer Paenibacillus O199

  • Original language description

    Background: The search for new enzymes and microbial strains to degrade plant biomass is one of the most important strategies for improving the conversion processes in the production of environment-friendly chemicals and biofuels. In this study, we report a new Paenibacillus isolate, O199, which showed the highest efficiency for cellulose deconstruction in a screen of environmental isolates. Here, we provide a detailed description of the complex multicomponent O199 enzymatic system involved in the degradation of lignocellulose. nnResults: We examined the genome and the proteome of O199 grown on complex lignocellulose (wheat straw) and on microcrystalline cellulose. The genome contained 476 genes with domains assigned to carbohydrate-active enzyme (CAZyme) families, including 100 genes coding for glycosyl hydrolases (GHs) putatively involved in cellulose and hemicellulose degradation. Moreover, 31 % of these CAZymes were expressed on cellulose and 29 % on wheat straw. Proteomic analyses also revealed a complex and complete set of enzymes for deconstruction of cellulose (at least 22 proteins, including 4 endocellulases, 2 exocellulases, 2 cellobiohydrolases and 2 beta-glucosidases) and hemicellulose (at least 28 proteins, including 5 endoxylanases, 1 beta-xylosidase, 2 xyloglucanases, 2 endomannanases, 2 licheninases and 1 endo-beta-1,3(4)-glucanase). Most of these proteins were secreted extracellularly and had numerous carbohydrate-binding domains (CBMs). In addition, O199 also secreted a high number of substrate-binding proteins (SBPs), including at least 42 proteins binding carbohydrates. Interestingly, both plant lignocellulose and crystalline cellulose triggered the production of a wide array of hydrolytic proteins, including cellulases, hemicellulases, and other GHs. nn

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2016

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Biotechnology for Biofuels

  • ISSN

    1754-6834

  • e-ISSN

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    MAY 14

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    12

  • Pages from-to

  • UT code for WoS article

    000375907200001

  • EID of the result in the Scopus database

    2-s2.0-84969248474