2026-07-19T17:28:02Zhttps://riubu.ubu.es/oai/request

oai:riubu.ubu.es:10259/85962024-02-07T01:05:22Zcom_10259.4_2516com_10259_5086com_10259_2604col_10259.4_2517

00925njm 22002777a 4500 dc García-Calvo, Laura author Rodríguez-Castro, Raquel author Ullán, Ricardo V. author Albillos García, Silvia María author Fernández-Aguado, Marta author Vicente, Cláudia M. author Degnes, Kristin F. author Sletta, Sletta author Barreiro, Carlos author 2023-02 Plant biomass is a promising substrate for biorefinery, as well as a source of bioactive compounds, platform chemicals, and precursors with multiple industrial applications. These applications depend on the hydrolysis of its recalcitrant structure. However, the effective biological degradation of plant cell walls requires several enzymatic groups acting synergistically, and novel enzymes are needed in order to achieve profitable industrial hydrolysis processes. In the present work, a feruloyl esterase (FAE) activity screening of Penicillium spp. strains revealed a promising candidate (Penicillium rubens Wisconsin 54–1255; previously Penicillium chrysogenum), where two FAE-ORFs were identified and subsequently overexpressed. Enzyme extracts were analyzed, confirming the presence of FAE activity in the respective gene products (PrFaeA and PrFaeB). PrFaeB-enriched enzyme extracts were used to determine the FAE activity optima (pH 5.0 and 50–55 °C) and perform proteome analysis by means of MALDI-TOF/TOF mass spectrometry. The studies were completed with the determination of other lignocellulolytic activities, an untargeted metabolite analysis, and upscaled FAE production in stirred tank reactors. The findings described in this work present P. rubens as a promising lignocellulolytic enzyme producer. 0175-7598 http://hdl.handle.net/10259/8596 10.1007/s00253-022-12335-w 1432-0614 Fungi Penicillium rubens Penicillium chrysogenum Lignocellulose Feruloyl esterase Extracellular proteome Penicillium chrysogenum as a fungal factory for feruloyl esterases