7 research outputs found
The <em>Penicillium echinulatum</em> Secretome on Sugar Cane Bagasse
<div><p>Plant feedstocks are at the leading front of the biofuel industry based on the potential to promote economical, social and environmental development worldwide through sustainable scenarios related to energy production. <em>Penicillium echinulatum</em> is a promising strain for the bioethanol industry based on its capacity to produce large amounts of cellulases at low cost. The secretome profile of <em>P. echinulatum</em> after grown on integral sugarcane bagasse, microcrystalline cellulose and three types of pretreated sugarcane bagasse was evaluated using shotgun proteomics. The comprehensive chemical characterization of the biomass used as the source of fungal nutrition, as well as biochemical activity assays using a collection of natural polysaccharides, were also performed. Our study revealed that the enzymatic repertoire of <em>P. echinulatum</em> is geared mainly toward producing enzymes from the cellulose complex (endogluganases, cellobiohydrolases and β-glucosidases). Glycoside hydrolase (GH) family members, important to biomass-to-biofuels conversion strategies, were identified, including endoglucanases GH5, 7, 6, 12, 17 and 61, β-glycosidase GH3, xylanases GH10 and GH11, as well as debranching hemicellulases from GH43, GH62 and CE2 and pectinanes from GH28. Collectively, the approach conducted in this study gave new insights on the better comprehension of the composition and degradation capability of an industrial cellulolytic strain, from which a number of applied technologies, such as biofuel production, can be generated.</p> </div
Distribution of peptide ions with similarity to CAZy enzymes, proteins with predicted function (PF) and proteins with hypothetical function (HYP).
<p>The tandem mass spectrometry analyses of the <i>P. echinulatum</i> secretome allowed the unambiguous assignment of 206 unique peptides, which were distributed across 18 CAZy families. The bar size indicates the percentage of total peptide matches in each condition.</p
Chemical composition of the substrates derived from sugar cane bagasse (SCB, SAT, SET and HDT) and cellulose (MCL) before and after <i>P. echinulatum</i> growth.
<p>Chemical composition of the substrates derived from sugar cane bagasse (SCB, SAT, SET and HDT) and cellulose (MCL) before and after <i>P. echinulatum</i> growth.</p
Heat map showing the relative abundance of the unique peptide ions in the different secretomes analyzed.
<p>Rows of the heat map correspond to the protein families, and columns correspond to the carbon sources used for fungal growth: SCB, HDT, SET, SAT and MCL. The peptide matches were categorized based on their similarity to CAZy families, proteins with predicted function (PF) and hypothetical proteins (HYP). The color of each protein families related to unique peptides matches abundance in the different growth conditions, varying from a minimum (red) to maximum (green) abundance.</p
The distribution of protein matches identified in each growth condition with the respect to their classification in CAZy families of cellulases (Blue), hemicellulases and other GH family members (Red), proteins of predicted function (Green) and hypothetical proteins (Purple).
<p>The distribution of protein matches identified in each growth condition with the respect to their classification in CAZy families of cellulases (Blue), hemicellulases and other GH family members (Red), proteins of predicted function (Green) and hypothetical proteins (Purple).</p
Scanning electron microscopy of substrates used for fungal growth. Samples of substrates derived from sugar cane bagasse (SCB, SAT, SET and HDT) and cellulose (MCL) were lyophilized (LabconcoFreezone 6 Benchtop) and stored at −80°C.
<p>The lyophilized samples were coated with a thin layer of gold in a sputter coater and examined in a JSM-5900 LV scanning electron microscope at acceleration voltages of 10 kV.</p