In the search for novel biomass-degrading enzymes through mining microbial genomes, it is necessary to apply functional tests during high-throughput screenings, which are capable of detecting enzymatic activities directly by way of plate assay. Using the most efficient expression systems of Escherichia coli and Pichia pastoris, the production of a high amount of His-tagged recombinant proteins could be thrived, allowing the one-step isolation by affinity chromatography. Here, we describe simple and efficient assay techniques for the detection of various biomass-degrading enzymatic activities on agar plates, such as cellulolytic, hemicellulolytic, and ligninolytic activities and their isolation using immobilized-metal affinity chromatography.
CITATION STYLE
Karnaouri, A., Zerva, A., Christakopoulos, P., & Topakas, E. (2021). Screening of recombinant lignocellulolytic enzymes through rapid plate assays. In Methods in Molecular Biology (Vol. 2178, pp. 479–503). Humana Press Inc. https://doi.org/10.1007/978-1-0716-0775-6_30
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