Purification of Glycerol Dehydrogenases from Saccharomyces cerevisiae and the Substrate Specificity of Bacterial Enzymes

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  • Saccharomyces cerevisiae由来グリセロール脱水素酵素の精製と細菌由来酵素の基質特異性
  • Saccharomyces cerevisiae ユライ グリセロール ダツスイソ コウソ ノ セイセイ ト サイキン ユライ コウソ ノ キシツ トクイセイ

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Abstract

We have obtained the dehydrogenases being specific for mannitol and arabitol with the gene cloning and over-expression in yeast cells, in order to measure the content of various sugar alcohols by using the dehydrogenases. In this study, we carried out the isolations of glycerol dehydrogenases from Saccharomyces cerevisiae and determined its substrate specificities. Target proteins were purified by affinity chromatography with the addition of 'tag' at N-terminus or C-terminus by gene recombination. The obtained enzymes showed the low specificity for sugar alcohols. However, we found the bacterial enzymes that showed the high specificity for glycerol in commercial products. These glycerol dehydrogenases could be available in the enzymatic analysis of glycerol content.

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