Proteomics

Dataset Information

0

Trichoderma RUT C-30 secretome after growth on different cellulosic substrates


ABSTRACT: Enzyme production by T. reesei Rut C-30 was studied in submerged cultures on five different cellulose-rich substrates, namely, commercial cellulose AvicelĀ® 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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Trichoderma Reesei Rut C-30

TISSUE(S): Culture Supernatant, Fungal Cell

SUBMITTER: George Anasontzis  

LAB HEAD: Lisbeth Olsson

PROVIDER: PXD001304 | Pride | 2014-09-11

REPOSITORIES: Pride

Dataset's files

Source:
altmetric image

Publications

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

Peciulyte Ausra A   Anasontzis George E GE   Karlstrƶm Katarina K   Larsson Per Tomas PT   Olsson Lisbeth L  

Fungal genetics and biology : FG & B 20140802


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 pr  ...[more]

Similar Datasets

2007-03-31 | E-MEXP-638 | biostudies-arrayexpress
2018-10-22 | PXD011309 | Pride
2022-05-09 | PXD031886 | Pride
2009-03-30 | GSE14734 | GEO
2009-01-09 | GSE12540 | GEO
2011-03-23 | E-GEOD-28131 | biostudies-arrayexpress
2022-05-09 | PXD031881 | Pride
2009-04-29 | E-GEOD-5073 | biostudies-arrayexpress
2015-05-19 | GSE69004 | GEO
2010-12-15 | E-GEOD-22426 | biostudies-arrayexpress