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    Novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin G acylase via covalent technique

    Access Status
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    Authors
    Elnashar, Magdy
    Yassin, M.
    Kahil, T.
    Date
    2008
    Type
    Journal Article
    
    Metadata
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    Citation
    Elnashar, M. and Yassin, M. and Kahil, T. 2008. Novel thermally and mechanically stable hydrogel for enzyme immobilization of penicillin G acylase via covalent technique. Journal of Applied Polymer Science. 109 (6): pp. 4105-4111.
    Source Title
    Journal of Applied Polymer Science
    DOI
    10.1002/app.28379
    ISSN
    0021-8995
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/48366
    Collection
    • Curtin Research Publications
    Abstract

    ?-Carrageenan hydrogel crosslinked with protonated polyethyleneimine (PEI+) and glutaraldehyde (GA) was prepared and evaluated as a novel biocatalytic support for covalent immobilization of penicillin G acylase (PGA). The method of modification of the carrageenan biopolymer is clearly illustrated using a schematic diagram and was verified by FTIR, elemental analysis, DSC, and INSTRON using the compression mode. Results showed that the gels' mechanical strength was greatly enhanced from 3.9 kg/cm2 to 16.8 kg/cm 2 with an outstanding improvement in the gels thermal stability. It was proven that, the control gels were completely dissolved at 35°C, whereas the modified gels remained intact at 90°C. The DSC thermogram revealed a shift in the endothermic band of water from 62 to 93°C showing more gel-crosslinking. FTIR revealed the presence of the new functionality, aldehydic carbonyl group, at 1710 cm-1 for covalent PGA immobilization. PGA was successfully immobilized as a model industrial enzyme retaining 71% of its activity. The enzyme loading increased from 2.2 U/g (control gel) to 10 U/g using the covalent technique. The operational stability showed no loss of activity after 20 cycles. The present support could be a good candidate for the immobilization of industrial enzymes rich in amino groups, especially the thermophilic ones. © 2008 Wiley Periodicals, Inc.

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