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Isolation, characterization and transcriptome analysis of a novel Antarctic Aspergillus sydowii strain MS-19 as a potential lignocellulosic enzyme source
- Source :
- BMC Microbiology, Vol 17, Iss 1, Pp 1-14 (2017), BMC Microbiology
- Publication Year :
- 2017
- Publisher :
- BMC, 2017.
-
Abstract
- Background With the growing demand for fossil fuels and the severe energy crisis, lignocellulose is widely regarded as a promising cost-effective renewable resource for ethanol production, and the use of lignocellulose residues as raw material is remarkable. Polar organisms have important value in scientific research and development for their novelty, uniqueness and diversity. Results In this study, a fungus Aspergillus sydowii MS-19, with the potential for lignocellulose degradation was screened out and isolated from an Antarctic region. The growth profile of Aspergillus sydowii MS-19 was measured, revealing that Aspergillus sydowii MS-19 could utilize lignin as a sole carbon source. Its ability to synthesize low-temperature lignin peroxidase (Lip) and manganese peroxidase (Mnp) enzymes was verified, and the properties of these enzymes were also investigated. High-throughput sequencing was employed to identify and characterize the transcriptome of Aspergillus sydowii MS-19. Carbohydrate-Active Enzymes (CAZyme)-annotated genes in Aspergillus sydowii MS-19 were compared with those in the brown-rot fungus representative species, Postia placenta and Penicillium decumbens. There were 701CAZymes annotated in Aspergillus sydowii MS-19, including 17 cellulases and 19 feruloyl esterases related to lignocellulose-degradation. Remarkably, one sequence annotated as laccase was obtained, which can degrade lignin. Three peroxidase sequences sharing a similar structure with typical lignin peroxidase and manganese peroxidase were also found and annotated as haem-binding peroxidase, glutathione peroxidase and catalase-peroxidase. Conclusions In this study, the fungus Aspergillus sydowii MS-19 was isolated and shown to synthesize low-temperature lignin-degrading enzymes: lignin peroxidase (Lip) and manganese peroxidase (Mnp). These findings provide useful information to improve our understanding of low-temperature lignocellulosic enzyme production by polar microorganisms and to facilitate research and applications of the novel Antarctic Aspergillus sydowii strain MS-19 as a potential lignocellulosic enzyme source. Electronic supplementary material The online version of this article (doi:10.1186/s12866-017-1028-0) contains supplementary material, which is available to authorized users.
- Subjects :
- 0301 basic medicine
Microbiology (medical)
Lignin peroxidase
030106 microbiology
lcsh:QR1-502
Antarctic Regions
Microbiology
Lignin
lcsh:Microbiology
Low temperature enzyme
Fungal Proteins
03 medical and health sciences
chemistry.chemical_compound
Manganese peroxidase
Botany
Polar organisms
Lignocellulose degradation
Aspergillus sydowii
Laccase
Aspergillus
Fungal protein
biology
Gene Expression Profiling
High-Throughput Nucleotide Sequencing
Molecular Sequence Annotation
biology.organism_classification
Cold Temperature
030104 developmental biology
Biochemistry
chemistry
Peroxidases
biology.protein
Transcriptome
Peroxidase
Research Article
Subjects
Details
- Language :
- English
- ISSN :
- 14712180
- Volume :
- 17
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- BMC Microbiology
- Accession number :
- edsair.doi.dedup.....ef8ad4f83a6a6cc78913148787835290
- Full Text :
- https://doi.org/10.1186/s12866-017-1028-0