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covalent immobilization of purified enzyme HjLAD onto glutaraldehyde-activated silicon oxide nanoparticles shows the a high immobilization efficiency of 94.7%, comparative characterization of free and immobilized enzyme HjLAD, including its thermostability and kinetic parameters, overview. Thermostability of immobilized enzyme is 14.2-fold higher than for free HjLAD, the t1/2 of HjLAD at 25°C is enhanced from 190 min (free) to 45 h (immobilized). The immobilized HjLAD retains 94% of its initial activity after 10 cycles. Immobilization efficiencies of HjLAD onto different supports, silicon oxide nanoparticles (4830HT) show the highest efficiency, method optimization, overview |
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