Data for iTRAQ secretomic analysis of Aspergillus fumigatus in response to different carbon sources

Here, we provide data related to the research article entitled “Quantitative proteomics study of Aspergillus fumigatus secretome revealed deamidation of secretory enzymes” by Adav et al. (J. Proteomics (2015) [1]). Aspergillus sp. plays an important role in lignocellulosic biomass recycling. To expl...

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Bibliographic Details
Main Authors: Adav, Sunil S., Ravindran, Anita, Sze, Siu Kwan
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2017
Subjects:
Online Access:https://hdl.handle.net/10356/85003
http://hdl.handle.net/10220/42058
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Institution: Nanyang Technological University
Language: English
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Summary:Here, we provide data related to the research article entitled “Quantitative proteomics study of Aspergillus fumigatus secretome revealed deamidation of secretory enzymes” by Adav et al. (J. Proteomics (2015) [1]). Aspergillus sp. plays an important role in lignocellulosic biomass recycling. To explore biomass hydrolyzing enzymes of A. fumigatus, we profiled secretome under different carbon sources such as glucose, cellulose, xylan and starch by high throughput quantitative proteomics using isobaric tags for relative and absolute quantification (iTRAQ). The data presented here represents the detailed comparative abundances of diverse groups of biomass hydrolyzing enzymes including cellulases, hemicellulases, lignin degrading enzymes, and peptidases and proteases; and their post translational modification like deamidation.