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Entrapment of β-galactosidase in polyvinylalcohol hydrogel

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Abstract

β-Galactosidase isolated from Aspergillus oryzae was immobilized in lens-shaped polyvinylalcohol capsules (with activity 25 U g−1) giving 32% of its original activity. Immobilization did not change the pH optimum (4.5) of lactose hydrolysis. The relative enzyme activity during product inhibition testing was, in average, 10% higher for immobilized enzyme. No decrease of activity was observed after 35 repeated batch runs and during 530 h of continuous hydrolysis of lactose (10%, w/v) at 45°C. The immobilized enzyme was stable for 14 months without any change of activity during the storage at 4°C and pH 4.5.

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Acknowledgements

The work was supported by Lentikat Inc., Praha, Czech Republic (www.lentikats.eu), and Vega Grant No.1/4452/07 from the Slovak Grant Agency of Ministry of Education, Slovak Republic.

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Authors and Affiliations

  1. Institute of Biotechnology and Food Science, Faculty of Chemical and Food Technology, Slovak University of Technology, Radlinského 9, 812 37, Bratislava, Slovak Republic

    Zuzana Grosová, Michal Rosenberg, Martin Rebroš, Matej Šipocz & Barbora Sedláčková

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  1. Zuzana Grosová
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  2. Michal Rosenberg
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  3. Martin Rebroš
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  4. Matej Šipocz
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  5. Barbora Sedláčková
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Correspondence to Michal Rosenberg.

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Grosová, Z., Rosenberg, M., Rebroš, M. et al. Entrapment of β-galactosidase in polyvinylalcohol hydrogel. Biotechnol Lett 30, 763–767 (2008). https://doi.org/10.1007/s10529-007-9606-0

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  • DOI: https://doi.org/10.1007/s10529-007-9606-0

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