Abstract
In recent years, many stable enzymes have been isolated from thermophilic bacteria. These thermostable enzymes may have tremendous potential in enzyme technology. We isolated thermophilic bacteria from the Kawamata Hot Springs in Japan. One of the isolated bacteria, named Thermus caldophilus GK-24, was chosen as a good source of stable enzymes, including an extracellular protease. The purification and properties of lactate dehydrogenases have been reported for some thermophilic bacteria (1–3), but little is known about the enzyme from Thermus strains. Extremely heat-stable L-lactate dehydrogenase (EC 1.1.1.27) has been purified from T. caldophilus GK-24.
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References
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© 1982 Plenum Press, New York
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Ohta, T., Taguchi, H., Matsuzaswa, H. (1982). Heat-Stable L-Lactate Dehydrogenase and its Application to an Enzyme Reactor. In: Chibata, I., Fukui, S., Wingard, L.B. (eds) Enzyme Engineering. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9290-7_30
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DOI: https://doi.org/10.1007/978-1-4615-9290-7_30
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4615-9292-1
Online ISBN: 978-1-4615-9290-7
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