Modulation of Penicillium echinulatum glycoside hydrolases

Culture media containing combinations of pretreated sugarcane bagasse, soybean flour, wheat bran, sucrose, and yeast extract as inductor carbon sources were investigated using Design of Experiments in order to maximize FPase, xylanase, pectinase, and β-glucosidase production by Penicillium echinulatum. Mass spectrometry analyses showed that most of the identified protein consisted of cellobiohydrolase (GH6 and GH7 Cazy family), endoglucanase (GH5 Cazy family), and endo-1,4-β-xylanase (GH10 Cazy family). The greatest number of spectral counts of GH7, GH5, and GH10 Cazy family enzymes was found for the supernatant of the culture medium designed to enhance β-glucosidase activity, followed by the supernatant of the medium modulated to increase the activities of FPase and pectinase. Moreover proteome of culture medium designed to enhance β-glucosidase activity presented protein CBM1 analogous to swollenin of P. decumbens. Enzymatic hydrolysis of standard pretreated sugarcane bagasse corroborated these data, as the supernatant from the culture medium tuned to maximize β-glucosidase activity provided statistically significant better performance than those obtained using media modulated to enhance FPase, pectinase, or xylanase activities. It was possible to increase the secretion of glycoside hydrolases by P. echinulatum, by adjusting the culture medium composition, which then influenced the yield achieved in the enzymatic hydrolysis of pretreated sugarcane bagasse.