Influence of hydrostatic pressure on L-glutamate dehydrogenase from the Antarctic fish Chaenocephalus aceratus

The influence of hydrostatic pressure on the stability and activity of glutamate dehydrogenase (GDH) from the liver of the Antarctic fish Chaenocephalus aceratus (Notothenioidei: Channichthyidae) has been investigated using the homologous bovine enzyme for comparison. At gradually increasing pressure, the fish GDH retains all activity up to 140 MPa, whereas in the same pressure range the bovine enzyme is slightly inactivated. The kinetics of pressure-induced inactivation of Antarctic GDH displays an exponentially decreasing residual activity as a function of the incubation time, whereas the bovine enzyme shows a complex pattern of behaviour in the first 20 min of incubation, attributable to the transient formation of aggregates. The coenzyme NAD increases the stability of both enzymes. The activation volume calculated for the reaction catalysed under pressure by fish GDH is higher than that of the bovine enzyme. These results indicate that the molecular properties of fish and bovine GDH are affected differently by hydrostatic pressure. A common mode of inactivation under extreme conditions of pressure and temperature of the cold-adapted Antarctic fish and mesophilic bovine GDH is deduced and discussed.