THE GLYCEROL DEHYDROGENASES OF PSEUDOMONAS SALINARIA, VIBRIO COSTICOLUS, AND ESCHERICHIA COLI IN RELATION TO BACTERIAL HALOPHILISM

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Abstract
Glycerol dehydrogenases from the extremely halophilic Pseudomonas salinaria and the moderately halophilic Vibrio costicolus are described and compared with the corresponding enzyme from the nonhalophilic Escherichia coli. The properties of all three enzymes are similar except their responses to salt concentration. The enzymes from E. coli and V. costicolus are most active at sodium chloride concentrations of about 0.25 M and 0.5 M respectively; that from P. salinaria is not only most active in the presence of 1.5 M NaCl but is irreversibly inactivated in the absence of salt. All three enzymes are more active in the presence of potassium chloride than of sodium chloride at any given molar concentration. These results suggest that the extremely halophilic bacteria contain high concentrations of salt and that their enzymes function maximally at these high concentrations. In contrast the moderately halophilic organisms contain relatively little salt and their enzymes are more comparable with those of nonhalophiles.