HALOPHILIC ALDOSE DEHYDROGENASE

I. SUBSTRATE SPECIFICITY AND PROPERTIES OF THE ENZYME

Abstract

Halophilic aldose dehydrogenase from halophilic Pseudomonas sp. was partially purified by fractionation with ammonium sulfate. The particle free enzyme showed typical halophilic nature in respects both to stability and to activity.
The soluble enzyme, which appeared to be specific with regard to the C-2 configuration of the aldose chain (i.e., the hydroxyl should be to the right), catalysed dehydrogenation of aldohexoses, aldopcntoses and disac-charides in the presence of 2, 6-dichlorophenolindophenol.
We are greatly indebted to Prof. F. Egami for his invaluable advice and discussion throughout the course of this work.