Yields of purified enzymes were determined using absorbance at 280 nm and each sample's purity was confirmed using SDS-PAGE. Of the 46 enzymes tested, 25 produced at least 1.5 mg/L of culture, with 10 of the 12 enzymes with yields higher than 5 mg/L of culture coming from mining efforts in Brenda database's expression and activity data. The Brenda database is highly curated and draws its information from experimental results rather than predictions, so it is expected that these enzymes would express if their data has been collected. Because all of the enzymes had a C-terminal 6 histidine tag attached to enable purification, the tag may have interfered with copper binding which could impact enzyme folding. We attempted to avoid this by saturating the induced cells with CuSO4, but the effectiveness of this treatment for each laccase will need to be probed in future studies. To evaluate if the enzymes were produced in an active state, each enzyme was assessed against a broad-specificity, commonly-used laccase reporter substrate, 2,2'-azino-bis(3-ethylbenzothiazoline-6sulfonic acid) (ABTS). Assays were conducted at pH 7.5 with 1.8 mM ABTS and increase of absorbance indicating oxidation was measured at 420 nm (Figure and Table ). Of the 46 assayed enzymes, 14 had ABTS activity of over 2E-2 µmol min -1 mg -1 which is more than 10 times higher than the median and 50 times higher than the lowest activity seen (3.81E-4 µmol min -1 mg -1 ). For our assay conditions, expression did not relate to activity, as can be seen with A0A0H3PBA4 and P36649, which are in the top 5 highest yielding enzymes while being in the bottom 6 for ABTS activity. Additionally, the laccase with the highest activity on the reporter substrate (>92 times the median activity), A0A268P1S4, had a yield lower than the median of the dataset. The differences between the yields and specific activity of the laccases could imply that qualities that improve an enzyme's expression do not necessarily increase its binding or turnover rate.