Proteomic characterization of lignocellulose-degrading enzymes secreted by Phanerochaete carnosa grown on spruce and microcrystalline cellulose
peer-reviewed · Applied Microbiology and Biotechnology · 2010
| Date | 2010-05-01 |
| Type | peer-reviewed |
| Venue | Applied Microbiology and Biotechnology |
| Publisher | Springer Science and Business Media LLC |
| Contribution | downstream-application |
| DOI | 10.1007/s00253-010-2516-4 |
| Citations (OpenAlex) | 49 |
Abstract
Proteins secreted by the white-rot, softwood-degrading fungus Phanerochaete carnosa during growth on cellulose and spruce were analyzed using tandem mass spectrometry and de novo sequencing. Homology-driven proteomics was applied to compare P. carnosa peptide sequences to proteins in Phanerochaete chrysosporium using MS BLAST and non-gapped alignment. In this way, 665 and 365 peptides from cellulose and spruce cultivations, respectively, were annotated. Predicted activities included endoglucanases from glycoside hydrolase (GH) families 5, 16, and 61, cellobiohydrolases from GH6 and GH7, GH3 beta-glucosidases, xylanases from GH10 and GH11, GH2 beta-mannosidases, and debranching hemicellulases from GH43 and CE15. Peptides corresponding to glyoxal oxidases, peroxidases, and glycopeptides that could participate in lignin degradation were also detected. Overall, predicted activities detected in extracellular filtrates of cellulose and spruce cultures were similar, suggesting that the adaptation of P. carnosa to growth on lignocellulose might result from fine tuning the expression of similar enzyme families.
Methods and tools
- Phanerochaete carnosa secretome: Proteomics of lignocellulose-degrading enzymes secreted by an unsequenced white-rot fungus, annotating 665 and 365 de novo peptides by MS BLAST homology search.
Methods it uses
- MS BLAST: Homology search of error-tolerant de novo sequences against a protein database, introduced for charting the proteomes of organisms with unsequenced genomes and later used to validate borderline identifications.