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This interview explores the systematic immobilization of L-lactate oxidase on various porous carriers, revealing that hydrophilic agarose supports with amine groups yield the highest activity. Key discussion points include the unexpected efficiency and stability achieved through simple adsorption versus covalent binding, and the crucial role of ionic interactions governing the enzyme's attachment to different functionalized surfaces.
By This podcasts have been AI generated.This interview explores the systematic immobilization of L-lactate oxidase on various porous carriers, revealing that hydrophilic agarose supports with amine groups yield the highest activity. Key discussion points include the unexpected efficiency and stability achieved through simple adsorption versus covalent binding, and the crucial role of ionic interactions governing the enzyme's attachment to different functionalized surfaces.