Immobilization of lactoperoxidase on graphene oxide nanosheets with improved activity and stability
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The purpose of this study was to develop a facile and efficient method to enhance the stability and activity of lactoperoxidase (LPO) by using its immobilization on graphene oxide nanosheets (GO-NS).
Following the LPO purification from bovine whey, it was immobilized onto functionalized GO-NS using glutaraldehyde as cross-linker. Kinetic properties and stability of free and immobilized LPO were investigated.
LPO was purified 59.13 fold with a specific activity of 5.78 U/mg protein. The successful immobilization of LPO on functionalized GO-NS was confirmed by using dynamic light scattering (DLS) and Fourier transform infrared spectroscopy (FT-IR). The overall results showed that the stability of the immobilized LPO was considerably improved compared to free LPO. Apparent Km and Vmax of LPO also indicated that the immobilized enzyme had greater affinity to the substrate than the native enzyme.
Graphene oxide nanosheets are effective means for immobilization of LPO.
KeywordsLactoperoxidase Immobilization Activity Stability Glutaraldehyde Graphene oxide nanosheets
The present work was supported by the Grant no. 393740 from Isfahan University of Medical Sciences.
Compliance with ethical standard
Conflict of interest
The authors declare no conflict of interest.
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