Purification and Characterisation of Benzaldehyde Dehydrogenase I from Acinetobacter calcoaceticus and the TOL Plasmid Encoded Benzaldehyde Dehydrogenase and Benzyl Alcohol Dehydrogenase from Pseudomonas putida

Chalmers, Ronald M (1990) Purification and Characterisation of Benzaldehyde Dehydrogenase I from Acinetobacter calcoaceticus and the TOL Plasmid Encoded Benzaldehyde Dehydrogenase and Benzyl Alcohol Dehydrogenase from Pseudomonas putida. PhD thesis, University of Glasgow.

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Abstract

1 Acinetobacter calcoaceticus can grow on either mandelate or benzyl alcohol as sole sources of carbon and energy. L(+)-Mandelate is metabolised to benzoate with phenylglyoxylate and benzaldehyde as intermediates, whereas benzyl alcohol is converted to benzoate with benzaldehyde as the only intermediate. Although the intermediates of the mandelate and benzyl alcohol pathways converge at the level of benzaldehyde, the enzymes of the pathways are quite separate because of the presence of two different benzaldehyde dehydrogenases. This thesis is concerned primarily with the purification and characterisation of benzaldehyde dehydrogenase I which is induced during growth on mandelate. This was intended to complete the characterisation of all of the enzymes of the mandelate and benzyl alcohol pathways in A. calcoaceticus. The project was subsequently enlarged to include the purification and characterisation of the benzaldehyde dehydrogenase and the benzyl alcohol dehydrogenase encoded by the TOL plasmid pWW53 in Pseudomonas putida MT53, because this would allow a more broadly-based comparison of five aldehyde and alcohol dehydrogenases, including a comparison of chromosomal and plasmid encoded enzymes.

Item Type: Thesis (PhD)
Qualification Level: Doctoral
Keywords: Biochemistry
Date of Award: 1990
Depositing User: Enlighten Team
Unique ID: glathesis:1990-76910
Copyright: Copyright of this thesis is held by the author.
Date Deposited: 14 Jan 2020 09:28
Last Modified: 14 Jan 2020 09:28
URI: http://theses.gla.ac.uk/id/eprint/76910

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