Studies on Acylase Activity and Micro-organisms. XXVII. Purification and Properties of Phenylacetyl DL-Acylase (N-Phenylacetyl-DL-amino-acid Amidohydrolase) from AAA 6020 (Pseudomonas sp.)

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Screening experiment in soil bacteria have been carried out for the purpose of finding out new acylases. As a result, AAA 6020 (Pseudomonas sp.) which produces a new acylase (tentatively called phenylacetyl-DL-acylase) was isolated. AAA 6020 was incubated in the synthetic medium containing of phenylacetyl-D-leucine and the bacterial cells were harvested. The phenylacetyl-DL-acylase was extracted from AAA 6020 by means of sonic oscillation and purified by ammonium sulfate fractionation, DEAE cellulose chromatography and Sephadex G-200 gelfiltration. The purified enzyme was represented about 29 fold purification over the cell free extract and the specific activity toward N-phenylacetyl-D-leucine was 124 units/mg. The homogeneity of purified enzyme was demonstrated by means of disc electrophoresis and analytical ultracentrifugation. A molecular weight of the enzyme was estimated to be about 115000 by gelfiltration. The optimal pH toward N-phenylacetyl-D-leucine was 8.0. This enzyme hydrolysed not only N-phenylacetyl-D-amino acids but also N-phenylacetyl-L-amino acids. However N-benzoyl and N-acetyl derivatives of D- and L-amino acids were not hydrolyzed. Thus this DL-acylase has specificity toward phenyl-acetyl-amino acids but has not optical specificity.
社団法人日本薬学会の論文
1978-09-25