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dc.contributor.authorMore, N.
dc.contributor.authorDaniel, Roy M.
dc.contributor.authorPetach, Helen H.
dc.identifier.citationMore, N., Daniel, R.M., Petach, H.H. (1995). The effect of low temperatures on enzyme activity. Biochemical Journal, 305(1), 17-20.en_NZ
dc.description.abstractThe stability of two enzymes from extreme thermophiles (glutamate dehydrogenase from Thermococcales strain AN1 and beta-glucosidase from Caldocellum saccharolyticum expressed in Escherichia coli) has been exploited to allow measurement of activity over a 175 degrees C temperature range, from +90 degrees C to -85 degrees C for the glutamate dehydrogenase and from +90 degrees C to -70 degrees C for the beta-glucosidase. The Arrhenius plots of these enzymes, and those for two mesophilic enzymes (glutamate dehydrogenase from bovine liver and beta-galactosidase from Escherichia coli), exhibit no downward deflection corresponding to the glass transition, found by biophysical measurements of several non-enzymic mesophilic proteins at about -65 degrees C and reflecting a sharp decrease in protein flexibility as the overall motion of groups of atoms ceases.en_NZ
dc.titleThe effect of low temperatures on enzyme activityen_NZ
dc.typeJournal Articleen_NZ

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