Studies on Acylase Activity and Microorganisms. XIX. Optical Resolution of Threonine, Lysine, Tryptophan, and Methionine by Acylase of Soil Bacteria.

概要

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Fifteen strains (KT 202,KT 205,KT 207,etc.) of soil bacteria capable of asymmetric hydrolysis of N-benzoyl-DL-threonine, 2,6-di-N-benzoyl-DL-lysine, N-acetyl-DL-lysine, N-acetyl-DL-tryptophan or N-acetyl-DL-methionine were isolated by using a synthetic medium containing N-acyl-derivatives of amino acids as the sole source of carbon (Table I). N-Benzoyl-DL-threonine was asymmetrically hydrolyzed to L-threonine, N-benzoyl-D-threonine and benzoic acid by the acylase of KT 218,KT 229,and KT 83,while 2,6-di-N-benzoyl-DL-lysine, to 6-N-benzoyl-L-lysine, 2,6-di-N-benzoyl-D-lysine and benzoic acid by KT 218 and KT 229. KT 241 and KT 224 hydrolyzed asymmetrically N-acetyl-DL-tryptophan and N-acetyl-DL-methionine to L-tryptophan and N-acetyl-D-tryptophan, and L-methionine and N-acetyl-D-methionine, respectively. It was observed that N-acetyl-D-tryptophan and N-acetyl-D-methionine were hydrolyzed by several strains (KT 229,KT 83,KT 222,etc.) of soil bacteria. It seems of interest to note that N-acetyl-L-methionine was more easily hydrolyzed by KT 224 or KT 218 than N-acetyl-L-tryptophan, while the latter was more easily hydrolyzed by KT 241,and that the N-acetyl derivative of L-methionine was more easily hydrolyzed by KT 224 or KT 241 than the N-benzoyl derivative, while the latter was more easily hydrolyzed by KT 218.
社団法人日本薬学会の論文
1962-12-25