Pressure-Induced Thermostabilization of Glutamate Dehydrogenase from the Hyperthermophiles Pyrococcus furiosus and Thermococcus litoralis
作者： M. M. Sun , N. Tolliday , C. Vetriani , F. T. Robb , D. S. Clark
DOI: 10.1007/978-3-642-60196-5_37
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摘要: The thermostabilities of glutamate dehydrogenases (GDH) from the hyperthermophiles Pyrococcus furiosus and Thermococcus litoralis were studied at pressures up to 500 atm. At 109 °C, P. GDH was stabilized 18-fold atm, one largest degrees pressure stabilization reported date. Addition glycerol also furiosus, albeit a lesser extent. Based on known effects protein structure, two possible mechanisms proposed. Thermoinactivation studies with highly homologous T. indicated that it is less thermostable than GDH. However, application atm enzyme degree similar
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