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Analysis of cyclodextrins using a calorimetric biosensor
Author(s) -
Kolb Michael,
Zentgraf Brigitte,
Arvidsson Peer,
Mattiasson Bo,
Danielsson Bengt
Publication year - 1996
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/(sici)1097-4660(199605)66:1<15::aid-jctb454>3.0.co;2-0
Subject(s) - cyclodextrin , hydrolysis , chemistry , immobilized enzyme , chromatography , biosensor , thermistor , covalent bond , organic chemistry , enzyme , biochemistry , electrical engineering , engineering
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.