Purification and Properties of Lipoamide Dehydrogenase from Yeast, Candida krusei

Abstract
Lipoamide dehydrogenase [EC 1.6.4.3] was purified 310-fold and obtained in crystalline form from a yeast, Candida krusei. Purification and crystallization of the enzyme was accomplished by the following steps; disruption of cells by autolysis with ethyl acetate, precipitation by ammonium sulfate, absorption and elution on calcium phosphate gel, chromatography on TEAE-cellulose at pH 7.0 and crystallization by dialysis. This enzyme showed very similar properties to the enzymes from various sources.

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