A Rapid Purification of D ‐Oxynitrilase from Almond Meal by Affinity Chromatography Oxynitrilase from almond meal is capable of catalyzing the stereospecific addition of cyanide to a variety of aldehydes. Thus, the enzyme is potentially useful in the synthesis of optically active cyanohydrins on a preparative scale [1]. As the currently available purification procedures for this enzyme [2] are rather tedious, we have elaborated a simple and rapid procedure based on affinity chromatography. An inhibitor for the enzyme, methyl p ‐(3‐aminopropoxy)benzoate (4) , has been synthesized and attached covalently to Sepharose 4B as a solid matrix (5) . With this affinity gel it was possible to prepare the D ‐oxynitrilase in a simple procedure with high yields.
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Erich Hochuli (1983) studied this question.
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