Proteomic analysis of temperature dependent extracellular proteins from Aspergillus fumigatus grown under solid-state culture condition

Fungal species of the genus Aspergillus are filamentous ubiquitous saprophytes that play a major role in lignocellulosic biomass recycling and also are considered as cell factories for the production of organic acids, pharmaceuticals, and industrially important enzymes. Analysis of extracellular sec...

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Main Authors: Ravindran, Anita, Sze, Siu Kwan, Adav, Sunil S.
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2013
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Online Access:https://hdl.handle.net/10356/99296
http://hdl.handle.net/10220/17034
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-992962020-03-07T12:18:14Z Proteomic analysis of temperature dependent extracellular proteins from Aspergillus fumigatus grown under solid-state culture condition Ravindran, Anita Sze, Siu Kwan Adav, Sunil S. School of Biological Sciences DRNTU::Science::Biological sciences::Microbiology Fungal species of the genus Aspergillus are filamentous ubiquitous saprophytes that play a major role in lignocellulosic biomass recycling and also are considered as cell factories for the production of organic acids, pharmaceuticals, and industrially important enzymes. Analysis of extracellular secreted biomass degrading enzymes using complex lignocellulosic biomass as a substrate by solid-state fermentation could be a more practical approach to evaluate application of the enzymes for lignocellulosic biorefinery. This study isolated a fungal strain from compost, identified as Aspergillus fumigatus, and further analyzed it for lignocellulolytic enzymes at different temperatures using label free quantitative proteomics. The profile of secretome composition discovered cellulases, hemicellulases, lignin degrading proteins, peptidases and proteases, and transport and hypothetical proteins; while protein abundances and further their hierarchical clustering analysis revealed temperature dependent expression of these enzymes during solid-state fermentation of sawdust. The enzyme activities and protein abundances as determined by exponentially modified protein abundance index (emPAI) indicated the maximum activities at the range of 40–50 °C, demonstrating the thermophilic nature of the isolate A. fumigatus LF9. Characterization of the thermostability of secretome suggested the potential of the isolated fungal strain in the production of thermophilic biomass degrading enzymes for industrial application. 2013-10-30T04:03:01Z 2019-12-06T20:05:30Z 2013-10-30T04:03:01Z 2019-12-06T20:05:30Z 2013 2013 Journal Article Adav, S. S., Ravindran, A., & Sze, S. K. (2013). Proteomic Analysis of Temperature Dependent Extracellular Proteins from Aspergillus fumigatus Grown under Solid-State Culture Condition. Journal of Proteome Research, 12(6), 2715-2731. 1535-3893 https://hdl.handle.net/10356/99296 http://hdl.handle.net/10220/17034 10.1021/pr4000762 en Journal of proteome research
institution Nanyang Technological University
building NTU Library
country Singapore
collection DR-NTU
language English
topic DRNTU::Science::Biological sciences::Microbiology
spellingShingle DRNTU::Science::Biological sciences::Microbiology
Ravindran, Anita
Sze, Siu Kwan
Adav, Sunil S.
Proteomic analysis of temperature dependent extracellular proteins from Aspergillus fumigatus grown under solid-state culture condition
description Fungal species of the genus Aspergillus are filamentous ubiquitous saprophytes that play a major role in lignocellulosic biomass recycling and also are considered as cell factories for the production of organic acids, pharmaceuticals, and industrially important enzymes. Analysis of extracellular secreted biomass degrading enzymes using complex lignocellulosic biomass as a substrate by solid-state fermentation could be a more practical approach to evaluate application of the enzymes for lignocellulosic biorefinery. This study isolated a fungal strain from compost, identified as Aspergillus fumigatus, and further analyzed it for lignocellulolytic enzymes at different temperatures using label free quantitative proteomics. The profile of secretome composition discovered cellulases, hemicellulases, lignin degrading proteins, peptidases and proteases, and transport and hypothetical proteins; while protein abundances and further their hierarchical clustering analysis revealed temperature dependent expression of these enzymes during solid-state fermentation of sawdust. The enzyme activities and protein abundances as determined by exponentially modified protein abundance index (emPAI) indicated the maximum activities at the range of 40–50 °C, demonstrating the thermophilic nature of the isolate A. fumigatus LF9. Characterization of the thermostability of secretome suggested the potential of the isolated fungal strain in the production of thermophilic biomass degrading enzymes for industrial application.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Ravindran, Anita
Sze, Siu Kwan
Adav, Sunil S.
format Article
author Ravindran, Anita
Sze, Siu Kwan
Adav, Sunil S.
author_sort Ravindran, Anita
title Proteomic analysis of temperature dependent extracellular proteins from Aspergillus fumigatus grown under solid-state culture condition
title_short Proteomic analysis of temperature dependent extracellular proteins from Aspergillus fumigatus grown under solid-state culture condition
title_full Proteomic analysis of temperature dependent extracellular proteins from Aspergillus fumigatus grown under solid-state culture condition
title_fullStr Proteomic analysis of temperature dependent extracellular proteins from Aspergillus fumigatus grown under solid-state culture condition
title_full_unstemmed Proteomic analysis of temperature dependent extracellular proteins from Aspergillus fumigatus grown under solid-state culture condition
title_sort proteomic analysis of temperature dependent extracellular proteins from aspergillus fumigatus grown under solid-state culture condition
publishDate 2013
url https://hdl.handle.net/10356/99296
http://hdl.handle.net/10220/17034
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