Stepwise engineering of a Pichia pastoris D-amino acid oxidase whole cell catalyst |
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| Authors: | Sandra Abad Jozef Nahalka Gabriele Bergler S Alison Arnold Robert Speight Ian Fotheringham Bernd Nidetzky Anton Glieder |
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| Affiliation: | 1.Austrian Centre of Industrial Biotechnology,c/o Applied Biocatalysis Research Centre, c/o Institute of Molecular Biotechnology, Graz University of Technology,Graz,Austria;2.Institute of Biotechnology and Biochemical Engineering,Graz University of Technology,Graz,Austria;3.Institute of Chemistry, Center of Glycomics,Slovak Academy of Sciences,Bratislava,Slovak Republic;4.Ingenza Ltd.,Wallace Building, Roslin BioCentre,Roslin,UK |
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| Abstract: | Background Trigonopsis variabilis D -amino acid oxidase (Tv DAO) is a well characterized enzyme used for cephalosporin C conversion on industrial scale. However, the demands on the enzyme with respect to activity, operational stability and costs also vary with the field of application. Processes that use the soluble enzyme suffer from fast inactivation of Tv DAO while immobilized oxidase preparations raise issues related to expensive carriers and catalyst efficiency. Therefore, oxidase preparations that are more robust and active than those currently available would enable a much broader range of economically viable applications of this enzyme in fine chemical syntheses. A multi-step engineering approach was chosen here to develop a robust and highly active Pichia pastoris Tv DAO whole-cell biocatalyst. |
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