Proteomic data on enzyme secretion and activity in the bacterium Chitinophaga pinensis
2017 (English)In: Data in Brief, ISSN 1529-4188, E-ISSN 1683-1470, Vol. 11, 484-490 p.Article in journal (Refereed) Published
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. (, 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.
Place, publisher, year, edition, pages
Elsevier, 2017. Vol. 11, 484-490 p.
Bacterium; Carbohydrate-active enzymes; Mass spectrometry; Plant biomass deconstruction; Protein secretion
IdentifiersURN: urn:nbn:se:kth:diva-203316DOI: 10.1016/j.dib.2017.02.032OAI: oai:DiVA.org:kth-203316DiVA: diva2:1081994
QC 201703212017-03-152017-03-152017-03-21Bibliographically approved