Laccases are valuable enzymes as an excellent ecological alternative for bioremediation issues because they can oxidize persistent xenobiotic compounds. The production and characterization of extracellular laccases from saprotrophic fungi from disturbed environments have been scarcely explored, even though this could diversify their functional characteristics and expand the conditions in which they carry out their catalysis. Agrocybe pediades, isolated from a disturbed forest, produces an extracellular laccase in liquid culture. The enzyme was purified, identified and characterized. Copper and hexachlorobenzene do not function as inducers for the laccase produced. Partial amino acid sequences were obtained by LC-MS/MS that share similarity with laccases from other fungi. Purified laccase is a monomer with a molecular mass between 55–60 kDa and had an optimum activity at pH 5.0 and the optimum temperature at 45 °C using 2,6-dimethoxyphenol (2,6-DMP) as substrate. The K_m and V_max also determined with 2,6-DMP were 100 μM and 285 μmol∙min⁻¹∙mg⁻¹, respectively, showing that the laccase of A. pediades has a higher affinity for this substrate than that of other Agaricales. These features could provide a potential catalyst for different toxic substrates and in the future laccase could be used in environmental recovery processes.

Background: Protein EpiScores are DNA methylation (DNAm)-derived predictors of circulating protein levels that may provide accessible biomarkers of disease-related molecular variation. However, because these models were developed in blood, it remains unclear whether they preserve interindividual variation when applied to other tissues. We evaluated the cross-tissue concordance of blood-trained protein EpiScores in matched donors from the Genotype-Tissue Expression (GTEx) project. Methods: We applied 109 published protein EpiScores to DNAm from whole blood and six matched non-blood tissues in 54 donors contributing 158 blood–tissue pairs. Fifteen scores had unusable variation, leaving 94 estimable scores per tissue and 564 comparisons. Positive concordance required Pearson r and Spearman ρ ≥0.50; strong concordance required both ≥0.70. Benjamini–Hochberg false-discovery-rate (FDR) correction was applied separately across all comparisons for each method. Leave-one-out analyses assessed donor influence, and partial Pearson correlations evaluated sensitivity to available covariates. Protein annotations, composites, and donor strata were examined descriptively. Results: Ninety-seven of 564 comparisons (17.2%) met the positive-concordance criterion, and 73 of these (75.3%) met the leave-one-out stability criteria. Lung showed the broadest correspondence: median absolute Pearson r was 0.594, 56/94 scores were concordant, and 49 were stable. After covariate adjustment, median absolute partial r in lung was 0.522 and 68/94 scores had global q <0.05. Among initially concordant pairs, 48/56 in lung retained partial r ≥0.50 and q <0.05, compared with 3/10 in colon, 1/2 in kidney cortex, and 0/3 in prostate. Breast and ovary were too small for adjusted analyses. Exploratory donor-cohort differences did not survive FDR correction. Conclusions: Blood-trained protein EpiScores showed broad correspondence in lung that persisted after adjustment for available covariates. Initially concordant findings in the other tissues eligible for adjustment were mostly covariate-sensitive. These results prioritize score–tissue combinations for replication and molecular validation; they do not establish that blood EpiScores measure local tissue protein abundance.