Screening for a novel enzyme hydrolysing l-carnitine amide

In an extended screening using d,l-carnitine amide as carbon or nitrogen source about 1300 strains were obtained by enrichment culture. Of these, 65 strains possessed carnitine amidase activities. A single strain was identified as containing an enzyme able to hydrolyse only l-carnitine amide and yield carnitine of high enantiomeric purity (97) when incubated with the racemic substrate. During the initial optimisation of the culture conditions the volume activity could be improved 6.7-fold whereas the specific activity increased 3.6-fold. The enzyme is inducible by l-carnitine amide and carnitine and to a lesser degree also by -butyrobetaine and dehydrocarnitine. As judged by the fatty acids and quinone composition the strain belongs into the -subgroup of purple bacteria but has not yet been classified by the German Culture Collection into a known genus of bacteria. Correspondence to: M.-R. Kula