Abstract
A thermostable α-amylase catalyzed the exothermal hydrolysis of cyclodextrins. It was immobilized covalently via a spacer on controlled pore glass (CPG-10) or Silicagel. The temperature signal caused by the reaction heat of the cyclodextrin hydrolysis was determined in a one-column calorimetric system (enzyme thermistor). It was correlated to the cyclodextrin concentration and depended on the type of enzyme carrier and kind of cyclodextrin hydrolyzed. The proposed technique offers a direct route to the determination of α-amylase activity, and the results are of importance for analysis of cyclodextrin concentration.
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