Characterization of feruloyl esterases from Pecoramyces sp. F1 and the synergistic effect in biomass degradation

Feruloyl esterase (FAE; EC 3.1.1.73) cleaves the ester bond between ferulic acid (FA) and sugar, to assist the release of FAs and degradation of plant cell walls. In this study, two FAEs (Fae13961 and Fae16537) from the anaerobic fungus Pecoramyces sp. F1 were heterologously expressed in Pichia pastoris (P. pastoris). Compared with Fae16537, Fae13961 had higher catalytic efficiency. The optimum temperature and pH of both the FAEs were 45 ℃ and 7.0, respectively. They showed good stability-Fae16537 retained up to 80% activity after incubation at 37 ℃ for 24 h. The FAEs activity was enhanced by Ca²⁺ and reduced by Zn²⁺, Mn²⁺, Fe²⁺ and Fe³⁺. Additionally, the effect of FAEs on the hydrolytic efficiency of xylanase and cellulase was also determined. The FAE Fae13961 had synergistic effect with xylanase and it promoted the degradation of xylan substrates by xylanase, but it did not affect the degradation of cellulose substrates by cellulase. When Fae13961 was added in a mixture of xylanase and cellulase to degrade complex agricultural biomass, it significantly enhanced the mixture's ability to disintegrate complex substrates. These FAEs could serve as superior auxiliary enzymes for other lignocellulosic enzymes in the process of degradation of agricultural residues for industrial applications.