Abstract

• Mt LPMO9H is immobilized and direct electron transfer is achieved. • The interaction of Mt LPMO9H with PASC is studied with FTacV. • The kinetic model for the interaction of Mt LPMO9H with PASC with FTacV is developed. • The kinetic constant for the interaction of Mt LPMO9H with PASC is extracted. In this work, a lytic polysaccharide monooxygenase (LPMO) belonging to the AA9 family from the filamentous fungus Thermothelomyces thermophilus , Mt LPMO9H, is immobilized on cobalt functionalized multi-walled carbon nanotubes modified glassy carbon electrode. The step of the binding of phosphoric acid swollen cellulose on this LPMO is studied using large amplitude fast Fourier transform alternating current voltammetry (FTacV) at different temperatures, extracting the corresponding kinetic constants, based on a model developed for the interaction of immobilized enzyme with free, in the solution, species.

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