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Stabilization of glucose oxidase on glycation induced nano-fibrils: New insight in enzyme immobilization

Sara Farahi1 ,MehranHabibi-Rezaei, Azadeh Ebrahim-Habibi, AmirArasteh, Nader Sheibani, AliAkbarMoosavi-Movahedi

Amyloids are interestingbiomaterialswith useful properties includinghigh strength and resistance to degradation. These characteristicsmake amyloids suitable nano-structure candidates for bio-applications, includingenzymeimmobilizationscaffoldatnano-scale dimensions.Here, glycation induced bovine serumalbumin (BSA) nano-fibrilswere used as a scaffold for glucose oxidase (GOx) immobilization and the kinetic parameters optimumtemperature and pH of the free and immobilizedGOxwere compared.The covalently boundGOx onBSAamyloid nano-fibers oxidized glucose to release hydrogen peroxide that offers a significant antimicrobial property against E. coli to the immobilized enzyme product.However, the enzymeÂ’s catalytic performance (kcat/Km)was decreased due to the covalent immobilizationon nanofibrils. In addition, a broadening and an alkaline shift in the temperature and pHprofiles of the enzymewas observed. These changeswere concomitantwith improved stability of the GOx upon immobilization. Together our results showthat BSAnano-fibrils provide a suitable nanostructure for immobilization ofGOxwithenhancedstabilityand conserved catalytic activity.