Synthesis of the arginine dihydrolase pathway enzymes in Lactobacillus buchneri

The formation of the arginine dihydrolase pathway enzymes in Lactobacillus buchneri NCDO sub(110), a heterofermentative organism, was investigated. The specific activites of arginine deiminase, ornithine transcarbamylase, and carbamate kinase were higher in galactose-grown cells than in glucose- or sucrose-grown cells in the early stationary phase of growth. The addition of arginine to growing cells increased the spacific activity of these three enzymes with all growth sugars. The specific activities of the enzymes decreased during the stationary phase of growth when the sugar-grown cells was galactose. When glucose was virtually exhausted from the medium, the activities of the three enzymes were not altered. This enzymic system was not repressed by glucose, and these results are different from those obtained with L. leichmanni , homofermentative organism.