Additional file 5: Tables S3âS5. Table S3. Top 20 detected proteins in the secretome of Aspergillus nidulans during growth on wheat starch at day 3, 4 and 5. Table S4. Top 20 detected proteins in the secretome of Aspergillus nidulans during growth on high-amylose maize starch at day 3, 4 and 5. Table S5. Top 20 detected proteins in the secretome of Aspergillus nidulans during growth on pea starch at day 3, 4 and 5

Birte Svensson

Gustav Vaaje-Kolstad

Laura Nekiunaite

Magnus Ø. Arntzen

Maher Abou Hachem

Biotechnology for Biofuels

PubMed

Nekiunaite, L

Arntzen, Magnus Øverlie

Svensson, B.

Vaaje-Kolstad, Gustav

Hachem, Maher Abou

Brage NMBU

English

Lytic polysaccharide monooxygenases and other oxidative enzymes are abundantly secreted by Aspergillus nidulans grown on different starches

Additional file 3: Figure S2. A trending heat map of proteins predicted to be secreted during growth of Aspergillus nidulans on high-amylose (HA) maize, pea or wheat starch. Two main clusters are indicated in the graph, proteins with decreasing levels over time (I) and proteins with increasing levels over time (II). The intensities are z-score normalized per row, separately for each substrate, to emphasize the trend of protein amount during growth independent of total level and substrate-level differences. Proteins showing no change over time (ANOVA, permutation-based FDR >0.1) were removed from the plot. Missing values (protein level less than detection limit of mass spectrometer) are colored white. Highlighted in green are AA13s, in purple—AA9s and AA11s, in blue—AA3s and AA7s, in red—hydrolytic enzymes associated with starch degradation, in gray—proteases, and in brown—cell wall-degrading enzymes

Laura Nekiunaite (3582110)

Magnus Arntzen (3582113)

Birte Svensson (102167)

Gustav Vaaje-Kolstad (188321)

Maher Abou Hachem (134843)

The Francis Crick Institute

MOESM3 of Lytic polysaccharide monooxygenases and other oxidative enzymes are abundantly secreted by Aspergillus nidulans grown on different starches

MOESM5 of Lytic polysaccharide monooxygenases and other oxidative enzymes are abundantly secreted by Aspergillus nidulans grown on different starches

Additional file 1: Table S1. Proteins identified in the secretome of Aspergillus nidulans. The table shows the MaxQuant output of identified proteins and the quantitative LFQ intensities associated with all replicates and conditions. Prediction of secretion was done as a combination of SignalP, Phobius and WoLF PSORT. CAZy annotation was done with dbCAN

MOESM1 of Lytic polysaccharide monooxygenases and other oxidative enzymes are abundantly secreted by Aspergillus nidulans grown on different starches

Crossref

Springer - Publisher Connector

Starch is the second most abundant plant-derived biomass and a major feedstock in non-food industrial applications and first generation biofuel production. In contrast to lignocellulose, detailed insight into fungal degradation of starch is currently lacking. This study explores the secretomes of Aspergillus nidulans grown on cereal starches from wheat and high-amylose (HA) maize, as well as legume starch from pea for 5 days. Aspergillus nidulans grew efficiently on cereal starches, whereas growth on pea starch was poor. The secretomes at days 3-5 were starch-type dependent as also reflected by amylolytic activity measurements. Nearly half of the 312 proteins in the secretomes were carbohydrate-active enzymes (CAZymes), mostly glycoside hydrolases (GHs) and oxidative auxiliary activities (AAs). The abundance of the GH13 α-amylase (AmyB) decreased with time, as opposed to other starch-degrading enzymes, e.g., the GH13 AmyF, GH15 glucoamylases (GlaA and GlaB), and the GH31 α-glucosidase (AgdE). Two AA13 LPMOs displayed similar secretion patterns as amylolytic hydrolases and were among the most abundant CAZymes. The starch-active AnLPMO13A that possesses a CBM20 carbohydrate-binding module dominated the starch-binding secretome fraction. A striking observation is the co-secretion of several redox-active enzymes with the starch-active AA13 LPMOs and GHs, some at high abundance. Notably nine AA9 LPMOs, six AA3 sub-family 2 (AA_2) oxidoreductases, and ten AA7 glyco-oligosaccharide oxidases were identified in the secretomes in addition to other non-CAZyme oxidoreductases. The co-secretion and high abundance of AA13 LPMOs are indicative of a key role in starch granule deconstruction. The increase in AA13 LPMO abundance with culture time may reflect accumulation of a more resistant starch fraction towards the later stages of the culture. The identification of AmyR sites upstream AA13 LPMOs unveils co-regulation of LPMOs featuring in starch utilization. Differential deployment of amylolytic hydrolases and LPMOs over time suggests additional regulatory mechanisms. The abundant co-secretion of distinct AA3 and AA7 oxidoreductases merits further studies into their roles and possible interplay with LPMOs and other enzymes in the deconstruction of starchy substrates. The study reports for the first time the biological significance of LPMOs in starch degradation and the temporal interplay between these and amylolytic hydrolases

Nekiunaite, Laura

Arntzen, Magnus Ø.

Svensson, Birte

Abou Hachem, Maher

Online Research Database In Technology

Lytic polysaccharide monooxygenases and other oxidative enzymes are abundantly secreted by <i>Aspergillus nidulans </i>grown on different starches

Additional file 4: Table S2. Comparison of detected CAZymes in the secretome of Aspergillus nidulans during growth on wheat, high-amylose maize and pea starch at day 3, 4 and 5

MOESM4 of Lytic polysaccharide monooxygenases and other oxidative enzymes are abundantly secreted by Aspergillus nidulans grown on different starches

https://figshare.com/articles/MOESM3_of_Lytic_polysaccharide_monooxygenases_and_other_oxidative_enzymes_are_abundantly_secreted_by_Aspergillus_nidulans_grown_on_different_starches/4469969

Lytic polysaccharide monooxygenases and other oxidative enzymes are abundantly secreted by Aspergillus nidulans grown on different starches

Abstract

Similar works

Full text

Available Versions

Brage NMBU

The Francis Crick Institute

The Francis Crick Institute

The Francis Crick Institute

Crossref

Springer - Publisher Connector

Online Research Database In Technology

The Francis Crick Institute