Author(s):
Murtinho, D. 
; Lagoa, A. R. ; Garcia, F. A. P. ; Gil, M. H.
Date: 1998
Persistent ID: http://hdl.handle.net/10316/7771
Origin: Estudo Geral - Universidade de Coimbra
Document details
Cellulose Derivatives Membranes as Supports for Immobilisation of Enzymes
Description
Cellulosic derivatives (cellulose acetate, cellulose propionate and cellulose acetate-butyrate) as membranes, were prepared in different ways. These were then characterised by differential scanning calorimetry (DSC), scanning electron microscopy (SEM) and contact angle evaluation. Subsequently, catalase (H2O2:H2O2 oxireductase; EC 1.11.1.6), alcohol oxidase (Alcohol:oxygen oxireductase; EC 1.1.3.13) and glucose oxidase (ß-D- Glucose:oxygen 1-oxireductase; EC 1.1.3.4) were covalently linked to these membranes. The catalytic activity and stability of these enzymes, when immobilised, were examined. The results obtained showed that the immobilisation efficiency and the stability of the coupled enzymes could be correlated with the studied properties of the supports. The cellulose acetate membrane which was prepared by evaporation gave the more active conjugate support-enzyme. Membranes prepared by the immersion technique were more crystalline and therefore less suitable for enzyme immobilisation. The highly hydrophobic membranes, obtained from the propionate and the butyrate esters of cellulose reduced the activities but gave better storage stability. http://dx.doi.org/10.1023/A:1009255126274
Cellulosic derivatives (cellulose acetate, cellulose propionate and cellulose acetate-butyrate) as membranes, were prepared in different ways. These were then characterised by differential scanning calorimetry (DSC), scanning electron microscopy (SEM) and contact angle evaluation. Subsequently, catalase (H2O2:H2O2 oxireductase; EC 1.11.1.6), alcohol oxidase (Alcohol:oxygen oxireductase; EC 1.1.3.13) and glucose oxidase (ß-D- Glucose:oxygen 1-oxireductase; EC 1.1.3.4) were covalently linked to these membranes. The catalytic activity and stability of these enzymes, when immobilised, were examined. The results obtained showed that the immobilisation efficiency and the stability of the coupled enzymes could be correlated with the studied properties of the supports. The cellulose acetate membrane which was prepared by evaporation gave the more active conjugate support-enzyme. Membranes prepared by the immersion technique were more crystalline and therefore less suitable for enzyme immobilisation. The highly hydrophobic membranes, obtained from the propionate and the butyrate esters of cellulose reduced the activities but gave better storage stability. http://dx.doi.org/10.1023/A:1009255126274
Document Type
Article
Language English
Language English
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