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Isoleucine 2-epimerase (ILEP) is a novel branched-chain amino acid racemase isolated from  Lactobacillus buchneri . In this study, we examined production of free  d -branched-chain amino acids such as  d -valine,  d -leucine, and  d - allo -isoleucine, using lactic acid bacteria carrying homologs to ILEP. Twelve selected strains of lactic acid bacteria were grown at optimal growth temperatures and accumulation of  d -branched-chain amino acids in the medium was monitored in exponential, early stationary, and stationary phases. To analyze the  d -branched-chain amino acids, enantiomers in the medium were initially converted into diastereomers using pre-column derivatization with  o -phthaldialdehyde plus  N -isobutyryl- l -cysteine. The resultant fluorescent isoindole derivatives were analyzed on an octadecylsilyl stationary phase using ultra-high performance liquid chromatography. The analyses revealed that the seven following lactic acid bacteria carrying homologs showing 53–60% amino acid sequence identity to the  L. buchneri  ILEP accumulate  d -branched-chain amino acids:  Lactobacillus fermentum  and  Weissella paramesenteroides  produce  d -valine,  d -leucine, and  d - allo -isoleucine;  Lactobacillus reuteri, Leuconostoc mesenteroides  subsp.  mesenteroides , and  Leuconostoc gelidum  subsp.  gasicomitatum  accumulate  d -leucine and  d - allo -isoleucine; and  Lactobacillus vaginalis  and  Leuconostoc pseudomesenteroides  produce  d - allo -isoleucine. These results suggest that  d -branched-chain amino acids are produced by a variety of lactic acid bacteria species, particularly those carrying homologs to the ILEP.

Production of d-Branched-Chain Amino Acids by Lactic Acid Bacteria Carrying Homologs to Isoleucine 2-Epimerase of Lactobacillus buchneri