In situ H2O2 Generation by Choline Oxidase and Its Application in Amino Polysaccharide Degradation by Coupling to Lytic Polysaccharide Monooxygenase

Author:

Hoang Nam‐Hai123ORCID,Golten Ole4ORCID,Forsberg Zarah4ORCID,Eijsink Vincent G. H.4ORCID,Richter Michael1ORCID

Affiliation:

1. Bioinspired Chemistry Fraunhofer Institute for Interfacial Engineering and Biotechnology IGB Branch BioCat Schulgasse 11a 94315 Straubing Germany

2. Department of Food Technology Ho Chi Minh City University of Technology (HCMUT) 268 Ly Thuong Kiet Street, District 10 72409 Ho Chi Minh Vietnam

3. Vietnam National University-Ho Chi Minh City (VNU-HCM) Linh Trung Ward, Thu Duc District 71308 Ho Chi Minh Vietnam

4. Faculty of Chemistry, Biotechnology and Food Science Norwegian University of Life Sciences (NMBU) 1432 Ås Norway

Abstract

AbstractChitin, the most abundant amino polysaccharide in Nature, has many applications in different fields. However, processing of this recalcitrant biopolymer in an environmentally friendly manner remains a major challenge. In this context, lytic polysaccharide monooxygenases (LPMOs) are of interest, as they can act on the most recalcitrant parts of chitin and related insoluble biopolymers such as cellulose. Efficient LPMO catalysis can be achieved by feeding reactions with H2O2, but careful control of H2O2 is required to avoid autocatalytic enzyme inactivation. Herein, we present a coupled enzyme system in which a choline oxidase from Arthrobacter globiformis is employed for controlled in situ generation of H2O2 that fuels LPMO‐catalyzed oxidative degradation of chitin. We show that the rate, stability and extent of the LPMO reaction can be manipulated by varying the amount of choline oxidase and/or its substrate, choline chloride, and that efficient peroxygenase reactions may be achieved using sub‐μM concentrations of the H2O2‐generating enzyme. This coupled system requires only sub‐stoichiometric amounts of the reductant that is needed to keep the LPMO in its active, reduced state. It is conceivable that this enzyme system may be used for bioprocessing of chitin in choline‐based natural deep eutectic solvents.

Funder

Alexander von Humboldt-Stiftung

Horizon 2020 Framework Programme

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

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