Abstract Pectin-degrading enzymes play a crucial role in various biotechnological applications, including food processing, lignocellulosic biomass deconstruction for biofuel production, and biorefinery processes. In recent years, there has been increasing demand for novel enzymes capable of efficiently hydrolyzing plant biomass. In this context, the present study investigated the production of pectinases by the filamentous fungus Trichoderma harzianum TR274. The enzymes produced were biochemically characterized, exhibiting optimal activity within a pH range of 5.0–6.0 and at a temperature of 50 °C. Although the pectinase-enriched enzymatic cocktail showed reduced thermal stability at 50 °C, it retained 55% of its activity at 40 °C after 4 h. Remarkably, plant cell wall-associated phenolic compounds, typically reported as enzyme inhibitors, such as trans-ferulic acid, p -coumaric acid, and syringic acid, significantly enhanced the activity of T. harzianum TR274 enzymes against apple pectin, leading to improved pectin hydrolysis. This result was not observed with a commercial enzyme. When applied to the hydrolysis of orange peel, the pectinase cocktail demonstrated an additive effect when combined with a thermostable xylanase. The findings reported here contribute valuable insights for the development of new pectinase-rich enzyme cocktails tailored for the deconstruction of fruit residues, with promising potential for future applications in biorefineries. Graphical Abstract
Hamann et al. (Thu,) studied this question.