biostudies-literatureOkereke OEDepartment of Biotechnology, Ministry of Science and Technology, Indiae0070423https://www.ebi.ac.uk/biostudies/studies/S-EPMC10537656biostudies-literatureUnknown89(9)The enzymatic conversion of lignocellulosic biomass to bioethanol depends on efficient enzyme systems with β-glucosidase as one of the key components. In this study, we performed in-depth profiling of the various β-glucosidases present in the genome of the hypercellulolytic fungus <i>Penicillium funiculosum</i> using genomics, transcriptomics, proteomics, and molecular dynamics simulation approaches. Of the eight β-glucosidase genes identified in the <i>P. funiculosum</i> genome, three were predicted to be extracellular based on signal peptide prediction and abundance in the secretome. Among the three secreted β-glucosidases, two belonged to the GH3 family and one belonged to the GH1 family. Homology models of these proteins predicted a deep and narrow active site for the GH3 β-glucosidaseApplied and environmental microbiologyProfiling of the β-glucosidases identified in the genome of <i>Penicillium funiculosum</i>: insights from genomics, transcriptomics, proteomics, and homology-modeling studies.PMC10537656BT/PR/Centre/03/2011-Phase IISinha TKapoor SSharma KOkereke OEGupta MOgunyewo OAYazdani SSfalseProfiling of the β-glucosidases identified in the genome of <i>Penicillium funiculosum</i>: insights from genomics, transcriptomics, proteomics, and homology-modeling studies.The enzymatic conversion of lignocellulosic biomass to bioethanol depends on efficient enzyme systems with β-glucosidase as one of the key components. In this study, we performed in-depth profiling of the various β-glucosidases present in the genome of the hypercellulolytic fungus <i>Penicillium funiculosum</i> using genomics, transcriptomics, proteomics, and molecular dynamics simulation approaches. Of the eight β-glucosidase genes identified in the <i>P. funiculosum</i> genome, three were predicted to be extracellular based on signal peptide prediction and abundance in the secretome. Among the three secreted β-glucosidases, two belonged to the GH3 family and one belonged to the GH1 family. Homology models of these proteins predicted a deep and narrow active site for the GH3 β-glucosidase2023-01-01T00:00:00Z2023 Sep2026-05-29T00:53:23.252Z2024-11-06T22:16:29.003ZS-EPMC105376563761023310.1128/aem.00704-23