Yellow laccase-like multicopper oxidase that is able to oxidize a variety of phenolic compounds including standard laccase substrates such as 2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) and 2,6-dimethoxyphenol (2,6-DMP) (PubMed:30529567). Can be used for the bioconversion of 2',3,4-trihy-droxychalcone to 3',4'-dihydroxy-aurone, a bioactive aurone recently shown to possess inhibitory activity against several isoforms of the histone deacetylase complex (HDAC) (PubMed:30529567). 2 2',3,4-trihydroxy-trans-chalcone + 2 H(+) + O2 = 2 3',4'-dihydroxyaurone + 2 H2O Retains almost half of its activity in presence of high salt concentrations up to 100 mM NaCl (PubMed:30529567). Retains also more than 85% of its original activity in the presence of 1 mM EDTA, indicating a satisfactory resistance towards chelators, which is rare among metal-containing enzyme (PubMed:30529567). The activity drops significantly in the presence of NaN(3) or SDS (PubMed:30529567). Appears more active in the presence of methanol compared to ethanol, but acetone or DMSO addition severely affect remaining laccase activity (PubMed:30529567). Optimum pH is 4.0. Optimum temperature is 50 degrees Celsius. The thermophilic yellow LMCO1 presents a number of superior properties with potential use in industrial biocatalysis via its ability to oxidize a variety of phenolic compounds. Belongs to the multicopper oxidase family.