Abstract
In the last decade, the genes encoding hyperthermophilic proteins and enzymes have been extensively expressed in heterologous organisms such as Escherichia coli, and their good productions have been achieved. However, some difficulties are often encountered when attempting to produce these proteins in the mesophilic hosts. This chapter focuses on the recent efforts made to overcome problems in heterologous production of hyperthermophilic enzymes: (1) successful production of hetero-oligomeric dye-linked l-proline dehydrogenases by use of effective promoters, (2) a typical procedure for the in vitro refolding of inclusion bodies composed of several hyperthermophilic enzymes (malate dehydrogenase, lysine dehydrogenase, and agmatinase), and (3) heat-induced structural conversion of hyperthermophilic glutamate dehydrogenase. This information could be useful in successful production of hyperthermophilic proteins and enzymes.
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Sakuraba, H., Ohshima, T. (2013). Heterologous Production of Thermostable Proteins and Enzymes. In: Satyanarayana, T., Littlechild, J., Kawarabayasi, Y. (eds) Thermophilic Microbes in Environmental and Industrial Biotechnology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5899-5_15
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