[Enzymatic conversion of tetradecanol in heterogenous phase by yeast-alcohol dehydrogenase].
Alcohol dehydrogenase from yeast converts long-chain primary alcohols not only in the dissolved state, but also at the surface of undissolved particles. Tetradecanol beads with a defined surface can be produced and employed as model substrate. The reaction rate was determined by the proton release accomplished in the reaction. The initial reaction rate depends on the enzyme concentration. The relation is nonlinear (vi = k-[e]0,4); the numerical value of the exponent (n = 0.4) argues in favour of a reaction occurring at the interface. The Lineweaver-Burk plots become linear if the substrate concentrations are based on the molar surface concentrations of the particles. The pH optimum for the reaction at the surface is displaced by 0.25 pH units towards the alkaline region (compared with ethanol as substrate). The activation energy of the reaction with tetradecanol beads as substrate is 30% lower than that for the ethanol oxydation.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D009226:Myristates / Q000378:metabolism*; D009227:Myristic Acids / Q000378:metabolism*; D015003:Yeasts
D009226:Myristates; D009227:Myristic Acids; D000429:Alcohol Oxidoreductases
Enzymatischer Umsatz von Tetradekanol in heterogener Phase durch Hefe-Alkoholdehydrogenase