Proteomics

Dataset Information

0

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


ABSTRACT: 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 multi-component O199 enzymatic system involved in the degradation of lignocellulose. 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 -glucosidases) and hemicellulose (at least 28 proteins, including 5 endoxylanases, 1 -xylosidase, 2 xyloglucanases, 2 endomannanases, 2 licheninases and 1 endo--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. Our data provide an in-depth analysis of the complex and complete set of enzymes and accessory non-catalytic proteins—GHs, CBMs, transporters, and SBPs—implicated in the high cellulolytic capacity shown by this bacterial strain. The large diversity of hydrolytic enzymes and the extracellular secretion of most of them supports the use of Paenibacillus O199 as a candidate for second-generation technologies using paper or lignocellulosic agricultural wastes.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Paenibacillus Sp.

SUBMITTER: Daniela Zuehlke  

LAB HEAD: Katharina Riedel

PROVIDER: PXD003970 | Pride | 2016-04-26

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
131202_O1_U3_SY_DZ_PAC1-2-3_PAS1-2-3.sf3 Other
131202_O1_U3_SY_DZ_PAC1_01.RAW Raw
131202_O1_U3_SY_DZ_PAC1_02.RAW Raw
131202_O1_U3_SY_DZ_PAC1_03.RAW Raw
131202_O1_U3_SY_DZ_PAC1_04.RAW Raw
Items per page:
1 - 5 of 63
altmetric image

Publications

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

López-Mondéjar Rubén R   Zühlke Daniela D   Větrovský Tomáš T   Becher Dörte D   Riedel Katharina K   Baldrian Petr P  

Biotechnology for biofuels 20160514


<h4>Background</h4>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 multi-component O199 enzymatic system invol  ...[more]

Similar Datasets

2016-05-02 | PXD003844 | Pride
2020-05-22 | GSE151004 | GEO
2024-02-28 | GSE222371 | GEO
2021-09-09 | PXD020215 | Pride
2013-11-27 | GSE42692 | GEO
2013-11-27 | E-GEOD-42692 | biostudies-arrayexpress
2013-04-01 | E-GEOD-44648 | biostudies-arrayexpress
2013-04-01 | GSE44648 | GEO
2015-11-22 | E-GEOD-55086 | biostudies-arrayexpress
2010-12-25 | GSE26092 | GEO