dc.contributor.authorAdav, Sunil S.
dc.contributor.authorRavindran, Anita
dc.contributor.authorSze, Siu Kwan
dc.date.accessioned2015-04-27T01:27:00Z
dc.date.available2015-04-27T01:27:00Z
dc.date.copyright2015en_US
dc.date.issued2015
dc.identifier.citationAdav, S. S., Ravindran, A., & Sze, S. K. (2015). Quantitative proteomic study of Aspergillus fumigatus secretome revealed deamidation of secretory enzymes. Journal of proteomics, 119, 154-168.en_US
dc.identifier.issn1874-3919en_US
dc.identifier.urihttp://hdl.handle.net/10220/25457
dc.description.abstractAspergillus sp. plays an essential role in lignocellulosic biomass recycling and is also exploited as cell factories for the production of industrial enzymes. This study profiled the secretome of Aspergillus fumigatus when grown with cellulose, xylan and starch by high throughput quantitative proteomics using isobaric tags for relative and absolute quantification (iTRAQ). Post translational modifications (PTMs) of proteins play a critical role in protein functions. However, our understanding of the PTMs in secretory proteins is limited. Here, we present the identification of PTMs such as deamidation of secreted proteins of A. fumigatus. This study quantified diverse groups of extracellular secreted enzymes and their functional classification revealed cellulases and glycoside hydrolases (32.9%), amylases (0.9%), hemicellulases (16.2%), lignin degrading enzymes (8.1%), peptidases and proteases (11.7%), chitinases, lipases and phosphatases (7.6%), and proteins with unknown function (22.5%). The comparison of quantitative iTRAQ results revealed that cellulose and xylan stimulates expression of specific cellulases and hemicellulases, and their abundance level as a function of substrate. In-depth data analysis revealed deamidation as a major PTM of key cellulose hydrolyzing enzymes like endoglucanases, cellobiohydrolases and glucosidases. Hemicellulose degrading endo-1,4-beta-xylanase, monosidases, xylosidases, lignin degrading laccase, isoamyl alcohol oxidase and oxidoreductases were also found to be deamidated.en_US
dc.format.extent52 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesJournal of proteomicsen_US
dc.rights© 2015 Elsevier B.V. This is the author created version of a work that has been peer reviewed and accepted for publication by Journal of Proteomics, Elsevier B.V. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [Article DOI: http://dx.doi.org/10.1016/j.jprot.2015.02.007].en_US
dc.subjectDRNTU::Science::Biological sciences
dc.titleQuantitative proteomic study of Aspergillus fumigatus secretome revealed deamidation of secretory enzymesen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1016/j.jprot.2015.02.007
dc.description.versionAccepted versionen_US


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