Abstract
Highly porous activated carbon (HPAC) was used as carrier matrix for immobilization of acid protease (AP). Immobilization of acid protease on mesoporous activated carbon (AP-HPAC) performs as best enzyme carrier. At pH 6.0, 250 mg acid protease g−1 HPAC was immobilized. The optimum temperature for both free and immobilized AP activities were 50 °C. After incubation at 50 °C, the immobilized AP maintained about 50% of its initial activity, while the free enzyme was completely inactivated. When testing the reusability of AP-HPAC combination immobilized system, a significant catalytic efficiency was maintained along more than five consecutive reaction cycles. The highly porous nature of the carbon permits significant higher loadings of enzyme, which results in a higher enzyme-support strength and increased stability. The changes in the AP, HPAC and AP-HPAC were confirmed by Fourier Transform Infrared spectroscopy (FT-IR). Furthermore, scanning electron microscopy (SEM) allowed us to observe that the morphology of the surface of HPAC and the AP-HPAC.
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Acknowledgements
The author A. Ganesh Kumar is thankful to Council of Scientific and Industrial Research (CSIR), Central Leather Research Institute (CLRI), Sathyabama University, India, for awarding a Research Fellowship and providing the facilities needed to carry out this work.
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Ganesh Kumar, A., Swarnalatha, S., Kamatchi, P. et al. Immobilization of proteolytic enzyme on highly porous activated carbon derived from rice bran. J Porous Mater 16, 439–445 (2009). https://doi.org/10.1007/s10934-008-9216-9
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DOI: https://doi.org/10.1007/s10934-008-9216-9