Abstract
AbstractIn Sm. lipolytica one NAD+‐dependent and three NADP+‐dependent alcohol dehydrogenases are detectable by polyacrylamide gelelectrophoresis.The NAD+‐dependent ADH (ADH I), with a molecular weight of 240,000 daltons, reacts more intensively with long‐chain alcohols (octanol) than with short‐chain alcohols (methanol, ethanol). The ADH I is not or only minimally subject to glucose repression. Besides the ADH I band no additional inducible NAD+‐dependent ADH band is gel‐electrophoretically detectable during growth of yeast cells in medium containing ethanol or paraffin. The ADH I band is very probably formed by two ADH enzymes with the same electrophoretic mobility. The NADP+‐dependent alcohol dehydrogenases (ADH II–IV) react with methanol, ethanol and octanol with different intensity. In polyacrylamide gradients two bands of NADP+‐dependent ADH are detectable: one with a molecular weight of 70,000 daltons and the other with 120,000 daltons. The occurrence of the three NADP+‐dependent alcohol dehydrogenases is regulated by the carbon source of the medium.Sm. lipolytica shows a high tolerance against allylalcohol. Resistant mutants can be isolated only at concentrations of 1 M allyalcohol in the medium. All isolates of allylalcohol‐resistant mutants show identical growth in medium containing ethanol as the wild type strain.
Published Version
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