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Updated: Jun 3, 2026
High Throughput Screening of Fungal Endoglucanase Activity in Escherichia coli
Published on: August 13, 2011
A new Penicillium echinulatum strain with faster cellulase secretion obtained using hydrogen peroxide mutagenesis and
A J P Dillon1, M Bettio, F G Pozzan
1Enzyme and Biomass Laboratory, Institute of Biotechnology, University of Caxias do Sul, Caxias do Sul, RS, Brazil. ajpdillo@ucs.br
Aims:
The aim of this study is to improve cellulase production and secretion by Penicillium echinulatum using mutagenesis and selection in association with microfermentation and microanalysis methods.
Methods And Results:
A new genetic variant was isolated from strain 9A02S1 and named S1M29. It was obtained by mutagenesis with H₂O₂ and two screening steps, which involved selection in Petri dishes using the medium supplemented with 2-deoxyglucose and microfermentations in submerged culture. The mutant showed higher cellulase productivity than 9A02S1 based on the Filter Paper Activity assay and endoglucanase; the peak activities for these enzymes were reached significantly faster than for the parent strain.
Conclusions:
The mutant obtained after mutagenesis and selection could produce and secrete cellulase faster than the parent strain.
Significance And Impact Of The Study:
Mutagenesis followed by selection is a useful tool for rapidly generating new cellulase-producing phenotypes in fungi. Faster production and higher titers of cellulases in mutant strains contribute to reduce the production costs for enzymatic complexes that hydrolyse lignocellulose residues and form fermented syrups, thus contributing to the economic production of bioethanol.
