A thermostable alpha-amylase catalyzed the exothermal hydrolysis of cy
clodextrins. 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 t
he cyclodextrin concentration and depended on the type of enzyme carri
er and kind of cyclodextrin hydrolyzed. The proposed technique offers
a direct route to the determination of alpha-amylase activity, and the
results are of importance for analysis of cyclodextrin concentration.