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Morphology and enzyme production of Trichoderma reesei Rut C-30 are affected by the physical and structural characteristics of cellulosic substrates

Ausra Peciulyte (Institutionen för kemi- och bioteknik, Industriell Bioteknik ) ; George Anasontzis (Institutionen för kemi- och bioteknik, Industriell Bioteknik ) ; Katarina Karlström ; Per Tomas Larsson ; Lisbeth Olsson (Institutionen för kemi- och bioteknik, Industriell Bioteknik )
Fungal Genetics and Biology (1087-1845). Vol. 72 (2014), p. 64-72.
[Artikel, refereegranskad vetenskaplig]

The industrial production of cellulolytic enzymes is dominated by the filamentous fungus Trichoderma reesei (anamorph of Hypocrea jecorina). In order to develop optimal enzymatic cocktail, it is of importance to understand the natural regulation of the enzyme profile as response to the growth substrate. The influence of the complexity of cellulose on enzyme production by the microorganisms is not understood. In the present study we attempted to understand how different physical and structural properties of cellulose-rich substrates affected the levels and profiles of extracellular enzymes produced by T. reesei. Enzyme production by T. reesei Rut C-30 was studied in submerged cultures on five different cellulose-rich substrates, namely, commercial cellulose Avicel® and industrial-like cellulosic pulp substrates which consist mainly of cellulose, but also contain residual hemicellulose and lignin. In order to evaluate the hydrolysis of the substrates by the fungal enzymes, the spatial polymer distributions were characterised by cross-polarization magic angle spinning carbon-13 nuclear magnetic resonance (CP/MAS 13C-NMR) in combination with spectral fitting. Proteins in culture supernatants at early and late stages of enzyme production were labeled by Tandem Mass Tags (TMT) and protein profiles were analysed by liquid chromatography-tandem mass spectrometry. In total 124 proteins were identified and quantified in the culture supernatants, including cellulases, hemicellulases, other glycoside hydrolases, lignin-degrading enzymes, auxiliary activity 9 (AA9) family (formerly GH61), supporting activities of proteins and enzymes acting on cellulose, proteases, intracellular proteins and several hypothetical proteins. Surprisingly, substantial differences in the enzyme profiles were found even though there were minor differences in the chemical composition between the cellulose-rich substrates.

Nyckelord: Cellulose I structure, Trichoderma reesei Rut C-30, submerged cultivation, biomass degrading enzymes, TMT, quantitative proteomics



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Denna post skapades 2014-12-08. Senast ändrad 2015-04-13.
CPL Pubid: 207616

 

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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Industriell Bioteknik (2008-2014)

Ämnesområden

Livsvetenskaper
Pappers-, massa- och fiberteknik
Biokatalys och enzymteknik

Chalmers infrastruktur

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