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Reinigung der D ‐Oxynitrilase aus Mandeln mit Hilfe der Affinitäts‐Chromatographie
Author(s) -
Hochuli Erich
Publication year - 1983
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19830660210
Subject(s) - chemistry , affinity chromatography , chromatography , enzyme , sepharose , covalent bond , stereospecificity , immobilized enzyme , organic chemistry , catalysis
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.