Fig. 5

Comparative proteomics of aspergilli during growth on wheat bran (a) and sugar beet pulp (b). Results are summarized by the polysaccharide that the enzymes act upon. Only CAZy families specific for one polysaccharide are included in the comparison. Cellulose-active enzymes: GH6, GH7, GH12, GH45, GH74, AA9; xylan-active enzymes: CE1, CE15, GH10, GH11, GH62, GH67, GH115; pectin-active enzymes: CE8, CE12, GH28, GH35, GH51, GH53, GH54, GH78, GH88, GH93, GH105, PL1, PL3, PL4, PL9, PL11; starch-active enzymes: GH13, GH15; other (CAZy families with multiple activities or minor activities on the substrates): CE16, GH1, GH2, GH3, GH5, GH26, GH27, GH31, GH32, GH36, GH43, GH95. Extracellular proteins following trypsin digestion were analyzed by LC-MS/MS using a LTQ-Orbitrap Velos mass analyzer (Thermo-Fisher). Quantification was based on MS precursor ion signal. Extracted ion chromatograms were used to determine the peptide area value associated to each identified precursor ion. A protein area value was calculated as the average of the three most intense, distinct peptides assigned to a protein. The amounts of proteins associated with each enzyme activity were expressed as percentage of the amount of total extracellular proteins present in each culture condition