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Updated: Apr 24, 2026

High Throughput Screening of Fungal Endoglucanase Activity in Escherichia coli
Published on: August 13, 2011
Escherichia coli as a production host for novel enzymes from basidiomycota
Katerina Zelena1, Nadine Eisele1, Ralf G Berger1
1Gottfried Wilhelm Leibniz University Hannover, Institute of Food Chemistry, Callinstr. 5, D-30167 Hannover, Germany.
Abstract:
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.
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