Proteomic data on enzyme secretion and activity in the bacteriumChitinophaga 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 bacteriumChitinophaga 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.
Norwegian University of Life Sciences, NMBU, Department of Chemistry, Biotechnology and Food Sciences, PO Box 5003, NO-1432 Ås, Norway; Wallenberg Wood Science Center, Division of Industrial Biotechnology, Department of Biology and Biological Engineering, Chalmers University, 412 96 Gothenburg, Sweden.
Johan
J
Larsbrink
Norwegian University of Life Sciences, NMBU, Department of Chemistry, Biotechnology and Food Sciences, PO Box 5003, NO-1432 Ås, Norway.
Tina R
TR
Tuveng
Norwegian University of Life Sciences, NMBU, Department of Chemistry, Biotechnology and Food Sciences, PO Box 5003, NO-1432 Ås, Norway.
Phillip B
PB
Pope
Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, Sweden; ARC Centre of Excellence in Plant Cell Walls and School of Agriculture, Food and Wine, The University of Adelaide, Waite Campus, Urrbrae, SA 5064, Australia.
Vincent
V
Bulone
Norwegian University of Life Sciences, NMBU, Department of Chemistry, Biotechnology and Food Sciences, PO Box 5003, NO-1432 Ås, Norway.
Vincent G H
VG
Eijsink
Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, Sweden; Michael Smith Laboratories and Department of Chemistry, University of British Columbia, 2185 East Mall, Vancouver, BC, Canada V6T 1Z4; Wallenberg Wood Science Center, Teknikringen 56-58, SE-100 44 Stockholm, Sweden.
Harry
H
Brumer
Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), AlbaNova University Centre, 106 91 Stockholm, Sweden; Wallenberg Wood Science Center, Teknikringen 56-58, SE-100 44 Stockholm, Sweden.
Lauren S
LS
McKee
Bacterium; Carbohydrate-active enzymes; Mass spectrometry; Plant biomass deconstruction; Protein secretion