Purification and characterization of a laccase from Cerrena unicolor and its reactivity in lignin degradation

Abstract

For efficient biopulping process, very active and stable lignase is essential. Laccase is one of the best enzyme in terms of environmentally benign processes, since the enzyme uses oxygen as an oxidant to degrade lignin and produces no hamful products. We could purify a laccase homogeneously from Cerrena unicolor in a very active state. It shows characteristic absorption feature with blue band at λmax = 604 nm. Molecular weight of the enzyme is 57,608 which could be accurately determined by MALDI/TOF MS. The enzyme has 2.8 copper ions per enzyme implying apoenzymes might exist together. The enzyme is active in lignin degradation and the activity increases 4 times in the presence of ABTS as a mediator.