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Table 2 Identified cellulose-degradation/modifying enzymes and spectrum counts in different carbon sources by wild-type 2HH and mutant S1M29 of Penicillium echinulatum at 96 h during submerged cultivation

From: Penicillium echinulatum secretome analysis reveals the fungi potential for degradation of lignocellulosic biomass

Accession number Identified proteins CAZyme Organism MW (kDa) Secretionb Spectral counta
2HH S1M29
Glu Gly SCB Cel Glu Gly SCB Cel
g2773 Cellobiohydrolase I GH7 (CBM1) Penicillium decumbens 56 Y 0 0 81 107 0 2 202 80
g8068 Cellobiohydrolase II GH6 (CBM1) Penicillium decumbens 49 Y 0 0 16 4 0 0 46 62
g8473 Endoglucanase 1 GH5 (CBM1) Penicillium echinulatum 44 Y 0 0 19 27 0 1 75 59
g5809 Endoglucanase Cel5C GH5 (CBM1, CBM46) Penicillium decumbens 69 Y 0 1 28 30 0 1 56 58
g2788 Endoglucanase I GH7 (CBM1) Penicillium decumbens 50 Y 0 0 5 4 0 0 14 10
g2291 Endoglucanase II GH5 (CBM1) Penicillium decumbens 44 Y 0 0 4 4 0 0 13 7
g2659 Endo-β-1,4-glucanase GH5 (CBM1) Penicillium oxalicum 52 Y 27 0 0 3 49 1 0 6
g3996 Endo-β-1,4-glucanase GH12 Penicillium oxalicum 26 Y 0 0 9 10 0 0 12 8
g7274 Endo-β-1,4-glucanase GH5 Penicillium oxalicum 55 N 0 0 5 1 0 0 0 0
g6766 β-glucosidase I GH3 Penicillium decumbens 93 Y 0 7 2 1 1 17 2 0
g8479 Related to β-glucosidase GH132 Colletotrichum gloeosporioides 46 Y 0 2 0 22 4 0 0 0
g3303 Cellulose monooxygenase Cel61A AA9 Penicillium oxalicum 26 Y 0 0 3 0 0 0 20 11
g8342 Cellulose monooxygenase AA9 Penicillium oxalicum 45 Y 0 0 3 0 0 0 0 0
g5167 Swollenin CBM1, CBM63 Penicillium oxalicum 52 Y 0 0 1 4 0 0 9 6
g1074 GMC oxidoreductase AA3 Neosartorya fischeri 70 Y 0 0 0 0 0 1 0 0
g3947 GMC oxidoreductase AA3 Penicillium roqueforti 67 N 0 4 0 0 0 0 0 0
  1. aSecretomic analysis based on spectral counting. A quantitative analysis was conducted for samples grown on cellulose or SCB (mean of triplicates), while a semiquantitative analysis for samples grown on glucose or glycerol (one replicate) was performed. The complete protein reports are given in Additional file 3
  2. bThe secretion of each protein was verified by the softwares SignalP, SecretomeP, and YLoc. When at least two of three softwares give a positive result, the protein was considered secreted