Abstract
The acylase activities in the glutamic acid-producing bacteria and related strains, Brevibacterium sp., Corynebacterium sp. and Micrococcus sp., were investigated.
1) The acylase activities toward acetyl-DL-methionine were distributed among these bacteria, while a few strain hydrolyzed acetyl-DL-phenylalanine. The highest activity toward acetyl-DL-methionine was detected in a glutamic acid-producing strain, Corynebacterium glutamicum 9632.
2) Some enzymatic properties of this Corynebacterium glutamicum were studied with the crude preparation, lyophilized cells ; a) This preparation was found to be able to hydrolyze a number of the acyl-derivatives, such as acetyl, chloroacetyl and benzoyl derivatives of aliphatic neutral amino acid, but neither derivatives of basic, acidic nor aromatic amino acid were hydrolyzed. b) The activation of this preparation by some metal ions such as Co2+, was not observed, but the activity was inhibited by Cu2+and Hg2+. c) The optimal pH was observed to be around 6.5_??_7.0, and the optimal temperature was 40_??_45°C for the hydrolysis of acetyl-methionine. d) The experiments with acetyl-DL-methionine indicated that this preparation had optical specificity and hydrolyzed only L-isomer, but no D-isomer. Therefore, this preparation can be used for the optical resolution of acetyl-DL-aliphatic amino acid.
