Thermophilic Enzymes and Applications as Industrial Biocatalyts

There is an increasing demand for new thermostable enzymes with enhanced performance and/or novel functionalities that provide savings in time, money and energy for industrial processes in the areas of high value chemical production and other "white" biotechnology applications. Two projects HOTZYME and THERMOGENE have been carried out to identify novel hydrolase and transferase enzymes respectively from microorganisms inhabiting naturally hot environments.

A selection of these identified ‘high priority’ enzymes and their applications for industrial applications will be discussed. These include carboxylesterases, lactonases, aminoacylase, expoxide hydrolases, transaminases and transketolases. These enzymes have been identified in thermophilic genomes and metagenomes and have been cloned and over-expressed in Escherichia coli.

The biochemical and structural properties of the enzymes have been determined in order to understand their stability and potential applications for commercial biocatalysis.

References

Crystal structure and substrate specificity of the thermophilic serine:pyruvate aminotransferase from Sulfolobus solfataricus

Sayer, C, Bommer, M, Isupov, M. Ward, J. and Littlechild. J. (2012) Acta Cryst. D68, 63-72.

Characterization of a phosphotriesterase-like lactonase from the hyperthermoacidophilic crenarchaeon Vulcanisaeta moutnovskia. Kallnik V, Bunescu A, Sayer C, Bräsen C, Wohlgemuth R, Littlechild J, Siebers B. (2014) J. Biotechnology, 190, 11-17.

Structural studies of a thermophilic esterase from a new Planctomycetes species, Thermogutta terrifontis. Sayer,C, Isupov,M.N, Bonch-Osmolovskaya, E and Littlechild, J. (2015)  Febs Journal, in press.

Discovery and characterization of thermophilic limonene-1,2-epoxide hydrolases from hot spring metagenomic libraries. Ferrandi,E. Sayer,C. Michail Isupov,N. Annovazzi,C. Marchesi,C, Lacobone,G. Peng, X. Bonch-Osmolovskaya,E. Wohlgemuth,R. Littlechild, J and Monti, D.(March 2015) ^.Submitted to Febs Journal.