抄録
Decarboxylase activity of 12 kinds of microorganisms on 21 kinds of amino acid was examined by paper electrophoresis. It was thereby found that Escherichia coli No.1 effected decarboxylation of arginine, glutamic acid, lysine, ornithine, histidine, aspartic acid, and canavanine, E. coli K12 that of arginine, glutamic acid, lysine, ornithine, histidine, tyrosine, aspartic acid, and canavanine, Streptococcus faecalis ATCC-8043 that of tyrosine, Proteus vulgaris HX 19 and Lactobacillus arabinosus 17-5 that of glutamic acid, Lact. fermenti 36 that of glutamic acid and histidine, Aerobacter aerogenes No.3059 and Proteus morganii No.3168 that of glutamic acid and ornithine, and Clostridium welchii SR 12 that of glutamic and aspartic acids.
Carbon dioxide formed by decarboxylation of glutamic acid by Lact. arabinosus 17-5 was approximately 90% of the calculated amount in 1 hour so that this cannot be used for the determination of glutamic acid.
Microbiological determination of the decarboxylatlon product of aspartic acid by E. coli No.1 showed that the amount of α-alanine formed is only about 1% of the calculated and the main decarboxylation product is assumed to be β-alanine.
