Escherichia coli as a production host for novel enzymes from basidiomycota

•The potential biotechnological applications of the enzymes from basidiomycota are summarized.•Recent advances in the heterologous expression of basidiomycetous enzymes in Escherichia coli are evaluated.•Strategies for the efficient production of the soluble functionally active recombinant basidiomycetous proteins are reviewed.•Research efforts towards the refolding of recombinant oxidoreductases and hydrolases from basidiomycota are presented.

Many enzymes from basidiomycota have been identified and more recently characterized on the molecular level. This report summarizes the potential biotechnological applications of these enzymes and evaluates recent advances in their heterologous expression in Escherichia coli. Being one of the most widely used hosts for the production of recombinant proteins, there are, however, recurrent problems of recovering substantial yields of correctly folded and active enzymes. Various strategies for the efficient production of recombinant proteins from basidiomycetous fungi are reviewed including the current knowledge on vectors and expression strains, as well as methods for enhancing the solubility of target expression products and their purification. Research efforts towards the refolding of recombinant oxidoreductases and hydrolases are presented to illustrate successful production strategies.