Biocatalysis is a useful tool in the provision of chiral technology and extremophilic enzymes are just one component in that toolbox. Their role is not always attributable to their extremophilic properties; as with any biocatalyst certain other criteria should be satisfied. Those requirements for a useful biocatalyst will be discussed including issues of selectivity, volume efficiency, security of supply, technology integration, intellectual property and regulatory compliance. Here we discuss the discovery and commercialization of an l-aminoacylase from Thermococcus litoralis, the product of a LINK project between Chirotech Technology and the University of Exeter. The enzyme was cloned into Escherichia coli to aid production via established mesophilic fermentation protocols. A simple downstream process was then developed to assist in the production of the enzyme as a genetically modified-organism-free reagent. The fermentation and downstream processes are operated at the 500 litre scale. Characterization of the enzyme demonstrated a substrate preference for N-benzoyl groups over N-acetyl groups. The operational parameters have been defined in part by substrate-concentration tolerances and also thermostabilty. Several examples of commercial biotransformations will be discussed including a process that is successful by virtue of the enzyme's thermotolerance.
Application of thermophilic enzymes in commercial biotransformation processes
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I.N. Taylor, R.C. Brown, M. Bycroft, G. King, J.A. Littlechild, M.C. Lloyd, C. Praquin, H.S. Toogood, S.J.C. Taylor; Application of thermophilic enzymes in commercial biotransformation processes. Biochem Soc Trans 1 April 2004; 32 (2): 290–292. doi: https://doi.org/10.1042/bst0320290
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