## 1 Introduction  
The exploitation of lignocellulosic biomass, such as wood and agricultural residues, towards the production of fermentable sugars for the production of second-generation biofuels in an environmentally friendly way, requires of enzymatic degradation. This step has low energy requirements, selectivity, mild processing environment and no need of harsh chemicals, in contrast to classical chemical methods, and it is catalyzed by a combination of hydrolytic and oxidative enzymes [1, 2]. Regarding the oxidation reactions, performing these steps in an electrochemical reactor, i.e., electroenzymatic synthesis of sugars, is a promising approach for the production of such chemicals. In principle, when electrolysis is combined with enzyme reactions, a redox enzyme is maintained in its active state through an electrode process. This can be achieved by oxidation of or a reduction in a cofactor or a mediator on the electrode surface, or by direct electron transfer to the enzyme. Therefore, applying enzyme immobilization onto the electrode and combining bioelectrocatalysis with traditional enzymatic hydrolysis offer perspectives for developing novel processes for the production of biofuels and other value-added materials from lignocellulosic. Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that have the capacity to cleave polysaccharides via an oxidative mechanism [3]. They are classified as Auxiliary Activities (AAs) in the Carbohydrate Active enZyme database (CAZy). More specifically, they are divided into seven families (AA9-11 and AA13-16) based on their sequence similarities, with the majority of those that are studied thoroughly belonging to the AA9 and AA10 families [4]. LPMOs act synergistically with other biomass-degrading enzymes and significantly boost the hydrolytic performance of cellulase and hemicellulose cocktails, primarily by improving the accessibility of the enzymes to the substrate [5, 6]. Until recently, the main theory regarding the mechanism of action of LPMOs involved the introduction of a single oxygen atom from molecular oxygen into the substrate, while taking electrons from an external electron donor for their action [7]. More recently, [PERSON] et al., while examining an LPMO belonging to the AA10 family, supported the idea that the chemically relevant co-substrate of LPMO catalyzed oxidation is H\({}_{2}\)O\({}_{2}\)[8]. Regardless of the mechanism of the oxidative cleavage of the polysaccharide substrate, in both cases, the reaction is initiated when the active center of the enzyme takes an electron from an external electron donor. The nature of the donors used in laboratory experimental setups include ascorbic acid, cysteine and reduced glutathione, but also a wide range of plant-derived phenols [9; 10], lignin compounds [11] and photocatalytic and enzymatic systems [12]. The reported mechanisms for the initial reduction in LPMOs do not implicate any chemical steps other than a one-step, one-electron reaction. One interesting point regarding these enzymes, which could possibly be an advantage for their electrochemical exploitation, is that their copper-containing active center is not \"buried\" inside their structure but can be found on a solvent-exposed, flat surface [13]. This could facilitate their use as electrode coatings, by directly providing them with electrons from an electrode surface, while immobilized on the electrode surface. Other than their study, this characteristic could lead to the exploitation of the bioelectrocatalytic action of LPMOs towards the production of oxidised products (oligosaccharides and glucans) from biomass, in concert with hydrolytic enzymes, in the absence of any external reducing agent. This means that by providing electrons directly from an electrode surface to an immobilised LPMO, the enzyme could be utilised in bioconversions through bioelectrocatalysis focusing on product life cycles.