Studies on microbial glycerol dehydrogenase. Part V. Alternation of the dissimilation pathway for glycerol and amplification of glycerol dehydrogenase in mutant strains of Cellulomonas sp. NT3060.

Abstract

Mutant strain ME544, which is able to grow on glycerol slowly, was derived from glycerolnegative mutant strain G011, which is a derivative strain of Cellulomonas sp. NT3060 and is defective in both the enzyme activities of glycerol kinase and glycerol 3-phosphate dehydrogenase. The mutant strain still lacked both the enzyme activities involved in the dissimilation of glycerol and had the same level of glycerol dehydrogenase activity as the parent strain. Dihydroxyacetone kinase activity in mutant strain ME544 was inducibly formed, reaching 4-fold the level in mutant strain G011 in glycerol medium. Thus, the mutant strain seemed to dissimilate glycerol by means of glycerol dehydrogenase followed by an increase in dihydroxyacetone kinase. Subsequently, a mutant strain, GP1807, which was resistant to the inhibition of growth on glycerol by 1, 2-propanediol, was derived from mutant strain ME544. Glycerol dehydrogenase activity of the mutant strain was amplified about 6-fold compared to that of the wild type strain.