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Turkish Journal of Chemistry

DOI

10.55730/1300-0527.3469

Abstract

The conversion of fumaric acid into L-malate by fumarase immobilized on silanized nanostructures was analyzed experimentally. The enzyme was bound to the silanized nanostructures. We carried out scanning electron microscopy (SEM), fourier transform infrared spectroscopy (FTIR) analysis, zeta size analysis and surface area calculation for the characterization of the nanostructures. The effect of initial enzyme concentration and pH on immobilization procedure were investigated and the change of Michaelis-Menten constants (Km and Vmax) with immobilization was examined. The change in the storage stability of the enzyme by immobilization was also investigated. The stability of the immobilized enzyme was very good. We observed that the fumarase was bound to silanized nanostructures [p(HEMA)-3-MTES] in much greater amounts. We have compared the activities of free fumarase and immobilized fumarase and we have observed a significant increase in the activity of the fumarase after immobilization for L-malate production. Moreover, we came to the conclusion that this activity can be better preserved for 30 days compared to free fumarase.

First Page

1661

Last Page

1668

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