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Immobilization of Lactoperoxidase on Graphene Oxide Nanosheets With Improved Activity and Stability Publisher Pubmed



Shariat SZAS1 ; Borzouee F1 ; Mofid MR1 ; Varshosaz J2
Authors
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Authors Affiliations
  1. 1. Department of Clinical Biochemistry, Bioinformatics Research Center, School of Pharmacy and Pharmaceutical Sciences, Isfahan University of Medical Sciences, Esfahan, Iran
  2. 2. Department of Pharmaceutics, School of Pharmacy and Novel Drug Delivery Systems Research Centre, Isfahan University of Medical Sciences, Esfahan, Iran

Source: Biotechnology Letters Published:2018


Abstract

Objectives: 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). Methods: 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. Results: 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. Conclusions: Graphene oxide nanosheets are effective means for immobilization of LPO. © 2018, Springer Science+Business Media B.V., part of Springer Nature.
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