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Enzymatic activities and infrared studies of glutamate dehydrogenase immobilized on Langmuir-Blodgett films

A technique is described for the immobilization of active glutamate dehydrogenase (GDH) on behenic acid Langmuir-Blodgett (LB) films. The optimization of the immobilization conditions shows that the activities of GDH bound on hydrophobic and hydrophilic LB films were similar and decreased dramatical...

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Bibliographic Details
Published in:Biotechnology techniques 1995-09, Vol.9 (9), p.643-648
Main Authors: HOURDOU, M.-L, BESSON, F
Format: Article
Language:English
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Summary:A technique is described for the immobilization of active glutamate dehydrogenase (GDH) on behenic acid Langmuir-Blodgett (LB) films. The optimization of the immobilization conditions shows that the activities of GDH bound on hydrophobic and hydrophilic LB films were similar and decreased dramatically when the immobilized enzyme was dried. The GDH binding was followed by Fourier transform infrared (FTIR) spectroscopy. Modifications of GDH conformation and LB film structure were observed during the enzyme binding. After GDH activity test, a partial dissociation of behenic acid occurred and the beta -sheet band of the enzyme increased by comparison with the alpha -helix band.
ISSN:0951-208X
1573-6784
DOI:10.1007/BF00156349