Investigating Aspergillus nidulans secretome during colonisation of cork cell walls

Publication date

2016-05-06T11:28:00Z

2016-05-06T11:28:00Z

2013-12-04

2016-05-06T11:28:05Z

Abstract

Cork, the outer bark of Quercus suber, shows a unique compositional structure, a set of remarkable properties, including high recalcitrance. Cork colonisation by Ascomycota remains largely overlooked. Herein, Aspergillus nidulans secretome on cork was analysed (2DE). Proteomic data were further complemented by microscopic (SEM) and spectroscopic (ATRFTIR) evaluation of the colonised substrate and by targeted analysis of lignin degradation compounds (UPLC-HRMS). Data showed that the fungus formed an intricate network of hyphae around the cork cell walls, which enabled polysaccharides and lignin superficial degradation, but probably not of suberin. The degradation of polysaccharides was suggested by the identification of few polysaccharide degrading enzymes (β-glucosidases and endo-1,5--L-arabinosidase). Lignin degradation, which likely evolved throughout a Fenton-like mechanism relying on the activity of alcohol oxidases, was supported by the identification of small aromatic compounds (e.g. cinnamic acid and veratrylaldehyde) and of several putative high molecular weight lignin degradation products. In addition, cork recalcitrance was corroborated by the identification of several protein species which are associated with autolysis. Finally, stringent comparative proteomics revealed that A. nidulans colonisation of cork and wood share a common set of enzymatic mechanisms. However the higher polysaccharide accessibility in cork might explain the increase of β-glucosidase in cork secretome

Document Type

Article


Accepted version

Language

English

Subjects and keywords

Suro; Roures; Fongs; Cork; Oak; Fungi

Publisher

Elsevier B.V.

Related items

Versió postprint del document publicat a: http://dx.doi.org/10.1016/j.jprot.2013.11.023

Journal of Proteomics, 2013, vol. 98, p. 175-188

http://dx.doi.org/10.1016/j.jprot.2013.11.023

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Rights

(c) Elsevier B.V., 2013

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