Temporal profiles of intra- and extracellular laccase isoenzymes from Pleurotus ostreatus produced in submerged and solid-state cultures

Abstract

Laccases are enzymes that have a great potential for use in breaking down toxic compounds Fungal laccases show high enzymic activity, especially those produced by basidiomycetes. Depending on the culture conditions and the strain used, a variety of isoenzymes and/or enzymic activities can be obtained. In this study, extracellular laccase enzymes produced by Pleurotus ostreatus was identified in a submerged culture (SmF), with and without copper sulfate as a chem. inducer, and in a solidstate culture (SSF), using wheat straw as natural inducer. This study was conducted to observe the expression of the enzymes produced under the culture conditions tested and their persistence during the culture, as well as the extracellular activity produced and the correspondence that the isoenzymes presented between the intracellular and extracellular media. A pos. effect of the inducers on the specific laccase activity was observed either in SmF with copper sulfate or SSF (41.11 and 40.43 UI/mg protein, resp.), compared with that obtained in SmF without copper sulfate (2.87 UI/mg protein). This effect was different only at the time when the highest activity appeared (360 and 120 h, resp.), showing advantages in SSF. The same three isoenzymes were observed in the three kinds of cultures. The main differences among the laccase profiles reside in the time when they appeared in each culture and only an addnl. form of lower mol. weight was observed in SSF. The laccase enzymes in the intracellular extracts were equal to those in the extracellular ones. The laccase isoenzymes profiles suggest that the presence of inducers helps in maintaining the activity through the culture time.