Cargando…

Proteomic data on enzyme secretion and activity in the bacterium Chitinophaga pinensis

The secretion of carbohydrate-degrading enzymes by a bacterium sourced from a softwood forest environment has been investigated by mass spectrometry. The findings are discussed in full in the research article “Proteomic insights into mannan degradation and protein secretion by the forest floor bacte...

Descripción completa

Detalles Bibliográficos
Autores principales: Larsbrink, Johan, Tuveng, Tina R., Pope, Phillip B., Bulone, Vincent, Eijsink, Vincent G.H., Brumer, Harry, McKee, Lauren S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5344218/
https://www.ncbi.nlm.nih.gov/pubmed/28317006
http://dx.doi.org/10.1016/j.dib.2017.02.032
_version_ 1782513493106229248
author Larsbrink, Johan
Tuveng, Tina R.
Pope, Phillip B.
Bulone, Vincent
Eijsink, Vincent G.H.
Brumer, Harry
McKee, Lauren S.
author_facet Larsbrink, Johan
Tuveng, Tina R.
Pope, Phillip B.
Bulone, Vincent
Eijsink, Vincent G.H.
Brumer, Harry
McKee, Lauren S.
author_sort Larsbrink, Johan
collection PubMed
description The secretion of carbohydrate-degrading enzymes by a bacterium sourced from a softwood forest environment has been investigated by mass spectrometry. The findings are discussed in full in the research article “Proteomic insights into mannan degradation and protein secretion by the forest floor bacterium Chitinophaga pinensis” in Journal of Proteomics by Larsbrink et al. ([1], doi: 10.1016/j.jprot.2017.01.003). The bacterium was grown on three carbon sources (glucose, glucomannan, and galactomannan) which are likely to be nutrient sources or carbohydrate degradation products found in its natural habitat. The bacterium was grown on solid agarose plates to mimic the natural behaviour of growth on a solid surface. Secreted proteins were collected from the agarose following trypsin-mediated hydrolysis to peptides. The different carbon sources led to the secretion of different numbers and types of proteins. Most carbohydrate-degrading enzymes were found in the glucomannan-induced cultures. Several of these enzymes may have biotechnological potential in plant cell wall deconstruction for biofuel or biomaterial production, and several may have novel activities. A subset of carbohydrate-active enzymes (CAZymes) with predicted activities not obviously related to the growth substrates were also found in samples grown on each of the three carbohydrates. The full dataset is accessible at the PRIDE partner repository (ProteomeXchange Consortium) with the identifier PXD004305, and the full list of proteins detected is given in the supplementary material attached to this report.
format Online
Article
Text
id pubmed-5344218
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher Elsevier
record_format MEDLINE/PubMed
spelling pubmed-53442182017-03-17 Proteomic data on enzyme secretion and activity in the bacterium Chitinophaga pinensis Larsbrink, Johan Tuveng, Tina R. Pope, Phillip B. Bulone, Vincent Eijsink, Vincent G.H. Brumer, Harry McKee, Lauren S. Data Brief Data Article The secretion of carbohydrate-degrading enzymes by a bacterium sourced from a softwood forest environment has been investigated by mass spectrometry. The findings are discussed in full in the research article “Proteomic insights into mannan degradation and protein secretion by the forest floor bacterium Chitinophaga pinensis” in Journal of Proteomics by Larsbrink et al. ([1], doi: 10.1016/j.jprot.2017.01.003). The bacterium was grown on three carbon sources (glucose, glucomannan, and galactomannan) which are likely to be nutrient sources or carbohydrate degradation products found in its natural habitat. The bacterium was grown on solid agarose plates to mimic the natural behaviour of growth on a solid surface. Secreted proteins were collected from the agarose following trypsin-mediated hydrolysis to peptides. The different carbon sources led to the secretion of different numbers and types of proteins. Most carbohydrate-degrading enzymes were found in the glucomannan-induced cultures. Several of these enzymes may have biotechnological potential in plant cell wall deconstruction for biofuel or biomaterial production, and several may have novel activities. A subset of carbohydrate-active enzymes (CAZymes) with predicted activities not obviously related to the growth substrates were also found in samples grown on each of the three carbohydrates. The full dataset is accessible at the PRIDE partner repository (ProteomeXchange Consortium) with the identifier PXD004305, and the full list of proteins detected is given in the supplementary material attached to this report. Elsevier 2017-02-17 /pmc/articles/PMC5344218/ /pubmed/28317006 http://dx.doi.org/10.1016/j.dib.2017.02.032 Text en © 2017 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Data Article
Larsbrink, Johan
Tuveng, Tina R.
Pope, Phillip B.
Bulone, Vincent
Eijsink, Vincent G.H.
Brumer, Harry
McKee, Lauren S.
Proteomic data on enzyme secretion and activity in the bacterium Chitinophaga pinensis
title Proteomic data on enzyme secretion and activity in the bacterium Chitinophaga pinensis
title_full Proteomic data on enzyme secretion and activity in the bacterium Chitinophaga pinensis
title_fullStr Proteomic data on enzyme secretion and activity in the bacterium Chitinophaga pinensis
title_full_unstemmed Proteomic data on enzyme secretion and activity in the bacterium Chitinophaga pinensis
title_short Proteomic data on enzyme secretion and activity in the bacterium Chitinophaga pinensis
title_sort proteomic data on enzyme secretion and activity in the bacterium chitinophaga pinensis
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5344218/
https://www.ncbi.nlm.nih.gov/pubmed/28317006
http://dx.doi.org/10.1016/j.dib.2017.02.032
work_keys_str_mv AT larsbrinkjohan proteomicdataonenzymesecretionandactivityinthebacteriumchitinophagapinensis
AT tuvengtinar proteomicdataonenzymesecretionandactivityinthebacteriumchitinophagapinensis
AT popephillipb proteomicdataonenzymesecretionandactivityinthebacteriumchitinophagapinensis
AT bulonevincent proteomicdataonenzymesecretionandactivityinthebacteriumchitinophagapinensis
AT eijsinkvincentgh proteomicdataonenzymesecretionandactivityinthebacteriumchitinophagapinensis
AT brumerharry proteomicdataonenzymesecretionandactivityinthebacteriumchitinophagapinensis
AT mckeelaurens proteomicdataonenzymesecretionandactivityinthebacteriumchitinophagapinensis