Occurrence of an L(+)-Alanine-Dehydrogenase in Bacillus subtilis

Abstract

THE metabolic analysis of mutant strains of B. subtilis has shown that the ability to use the ammonium ion as the sole source of nitrogen for growth corresponds to the presence of a glutamic-dehydrogenase¹. However, a mutant unable to use the ammonium ion (strain S⁻), lacking glutamic-dehydrogenase, oxidizes glutamic acid very actively. This strain may grow, with aeration, in a culture medium containing: l(+)-glutamate 0.01 M, ammonium sulphate 0.01 M, phosphate buffer (KH₂PO₄–Na₂HPO₄) 0.02 M, pH 7.5, sodium chloride 0.01 M, potassium sulphate 0.01 M, magnesium sulphate 0.001 M and ferric citrate 0.0004 M.