The GH11 endo-xylanase ScXyn22 from Schizophyllum commune was expressed in Pichia pastoris. Then, its enzymatic properties and its effect on the baking quality of whole wheat bread were characterized. The optimal pH and temperature for the purified recombinant enzyme were 4.5 and 55 ℃, respectively. Under these conditions, the specific activity, K_m and V_max of ScXyn22 were (5964.1 ± 429.4) U/mg, (3.25 ± 0.27) mg/mL and (1288 ± 9.14) μmol/(min mg), respectively. In the reaction system containing 1-5 mol/L NaCl, the activity of ScXyn22 toward birch xylan was significantly enhanced by 1.64, 2.13, 2.31, 2.39 and 2.3 folds, respectively. The activity of ScXyn22 toward wheat arabinoxylan was enhanced by 1.21, 1.46, 1.58, 1.48 and 1.16 folds, respectively. However, the activity of ScXyn22 toward oat β-glucan decreased by 19.31%, 47.72%, 55.97%, 45.99% and 38.18%, respectively, compared with that in the absence of NaCl. In simulated intestinal fluid, the remaining enzyme activity was 81% after 20 min and 65.77% after 120 min. Addition of xylanase had a significant effect on the quality of whole wheat bread. Addition of xylanase at 300 U/kg increased the specific volume of whole wheat bread by 19.7%, and at 150 U/kg decreased its firmness by 57.3%. These results showed that the xylanase has good application potential in whole wheat bread production.

In order to produce enzyme cocktails with an advantage in hemicellulose degradation for enzymatic hydrolysis of corn bran fiber (CBF) to produce oligoarabinoxylan, Aspergillus niger and Phanerochaete carnosa were cultured on CBF (containing 50.97% xylose and 28.47% arabinose) under submerged fermentation. The maximum xylanase activity of A. niger and P. carnosa during fermentation was found to be 246.58 (72 h) and 367.21 U/mL (60 h), and the highest activity of α-L-arabinofuranosidase of A. niger and P. carnosa was 57.90 (144 h) and 8.26 U/mL (192 h), respectively. Label-free proteomic analysis revealed that a total of 109 and 105 proteins were identified from the fermentation broths of P. carnosa and A. niger, respectively. The number of glycoside hydrolases secreted by A. niger (82) was more than that produced by P. carnosa (53), and there was also a great difference in the distribution of the glycoside hydrolase family between the two strains, while the number of oxidases secreted by P. carnosa (6) was higher than that secreted by A. niger (2). The results showed that A. niger and P. carnosa could grow on CBF as a carbon source and secrete enzyme cocktails with different compositions but similar catalytic function and efficiency, suggesting that A. niger and P. carnosa use different multienzyme synergetic strategies to degrade CBF.