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Updated: Feb 14, 2026

Preparation and Evaluation of Hybrid Composites of Chemical Fuel and Multi-walled Carbon Nanotubes in the Study of Thermopower Waves
Published on: April 10, 2015
Covalent immobilization of phytase on the multi-walled carbon nanotubes via diimide-activated amidation: structural
Mohammad Pooya Naghshbandi1, Hamid Moghimi1, Babak Latif2
1a Department of Microbial Biotechnology, School of Biology, College of Science , University of Tehran , Tehran , Iran.
Abstract:
Phytase is the most widely used feed enzyme in the world. This enzyme inactivates under pelleting conditions such as temperatures above 80 °C. The present study reported covalent attachment of phytase onto functionalized multi-walled carbon nanotubes (F-MWNT). The optimum enzyme loading and immobilization efficiency were 110 µg/mg of functionalized multi-walled carbon nanotubes and 62%, respectively. Characterization, structural changes and immobilization of phytase were studied by scanning electron microscopy (SEM), circular dichroism (CD), zeta potential measurement and Fourier transform infrared (FTIR) spectroscopy. Immobilized phytase exhibited improved stability towards temperature than the free phytase. The free phytase retain 3% and 27% of relative activity at 90 and 80 °C, respectively after 2 min of incubations. While immobilized phytase retained about 33% and 51% at the same condition. Also the results showed that the presence of small quantities of NaCl (<1 M) in the reaction media increased enzyme activity of immobilized phytase up to 78% but free phytase activity was not significantly changed until 1 M NaCl which increased by 30%. Higher concentrations of 1 M NaCl drastically reduced both free and immobilized phytase activities.
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