Studies on acylase activity and micro-organisms. XXVI. Purification and properties of D-acylase (N-acyl-D-amino-acid amidohydrolase) from AAA 6029 (Pseudomonas sp.).

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Abstract
AAA 6029 (Pseudomonas sp.) was isolated from soil by using the synthetic medium containing N-benzoyl-D-phenylalanine as a sole C source. The bacteria produce a D-acylase which hydrolyzes N-acyl-D-amino acids. The D-acylase was extracted by means of sonic oscillation and purified by (NH4)2SO4 fractionation, DEAE cellulose chromatography and Sephadex G-100 gelfiltration. The purified enzyme was represented about 900-fold purification over the cell free extract. The MW of this enzyme was about 45,000 by gelfiltration. This enzyme can hydrolyze N-benzoyl and N-acetyl derivatives of the D-form of phenylalanine methionine, leucine, alanine and valine. The acylase cannot hydrolyze N-acyl derivatives of L-amino acids.

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