| چکیده
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Immobilization of enzymes is a promising approach for the cost-e ective application
of enzymes. Among others, noncovalent but unleachable approaches for immobilization are
one of the most favorable and crucial approaches. Herein, silica nanoparticles are modified by
(3-aminopropyl)triethoxysilane (APTES) to generate amino-functionalized silica nanoparticles. Then,
the amine functionalities are converted to bifunctional amino acid via post-modification that has
zwitterionic properties. This nanostructure with the new functional theme is employed to immobilize
Yarrowia lipolytica lipase at room temperature with no further post-modification or cross-linking.
This immobilization method is further compared with the metal chelate-based immobilization
approach on the same support. The biocatalytic activity of the immobilized lipase is examined
under various conditions. The encapsulation of lipase through amino acid-functionalized silica
nanoparticles exhibited enhanced stability for the immobilized lipase at higher temperatures and
unneutral pHs.
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