Studies on continuous enzyme reactions. IV. Preparation of a DEAE‐sephadex–aminoacylase column and continuous optical resolution of acyl‐DL‐amino acids

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Abstract

Abstract Conditions for the preparation of an aminoacylase column using DEAE‐Sephadex as a carrier were investigated. The aminoacylase column having the highest activity was obtained when 7500 μmoles/hr. of partially purified aminoacylase was charged into a column packed with 9 ml. of DEAE‐Sephadex A‐25 (bead type, hydroxy form). By employing a DEAE‐Sephadex–aminoacylase column, conditions for continuous optical resolution of acyl‐ DL ‐amino acids were investigated. When a solution of 0.2 M acetyl‐ DL ‐methionine (pH 7.0, containing 5 × 10 −4 M Co 2+ ) or 0.2 M acetyl‐ DL ‐phenylalanine (pH 6.0, containing 5 × 10 −4 M Co 2+ ) was passed through the aminoacylase column at the flow rate of SV = 2.5 or 2.0, respectively, at 50°C., the highest rate of hydrolysis of both substrates was attained. From the column effluents, enzymatically hydrolyzed L ‐methionine and L ‐phenylalanine were isolated in a good yield.

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