Abstract
Lytic polysaccharide monooxygenases (LPMOs) have recently been shown to significantly enhance the degradation of recalcitrant polysaccharides and are of interest for the production of biochemicals and bioethanol from plant biomass. The copper-containing LPMOs utilize electrons, provided by reducing agents, to oxidatively cleave polysaccharides. Here, we report the development of a β-glucosidase-assisted method to quantify the release of C1-oxidized gluco-oligosaccharides from cellulose by two C1-oxidizing LPMOs from Myceliophthora thermophila C1. Based on this quantification method, we demonstrate that the catalytic performance of both MtLPMOs is strongly dependent on pH and temperature. The obtained results indicate that the catalytic performance of LPMOs depends on the interaction of multiple factors, which are affected by both pH and temperature.
Highlights
The enzymatic degradation of plant biomass is considered to be a green and sustainable approach for the production of biochemicals and biofuels
We describe a procedure for quantifying the catalytic performance of MtLPMO9B and MtLPMO9D that oxidize cellulose at the C1 position in which the MtLPMO9B domain is appended to a CBMI, whereas MtLPMO9C is composed of the Lytic polysaccharide monooxygenases (LPMOs) domain only
The area under the curve (AUC) of this blank peak was subtracted from the AUC of the determined peak deriving from the MtLPMO incubation to assure the correct quantification of released gluconic acid
Summary
The enzymatic degradation of plant biomass is considered to be a green and sustainable approach for the production of biochemicals and biofuels. Plant biomass contains a substantial amount of the plant cell wall material lignocellulose, which is resistant for hydrolytic enzymatic degradation. Forsberg et al 2011), whereas they have been initially characterized to enhance the decomposition of chitin (VaajeKolstad et al 2005a; Vaaje-Kolstad et al 2005b; VaajeKolstad et al 2010). Based on their amino acid sequences, LPMOs are classified as auxiliary activity (AA) families AA9, AA10, AA11, and AA13 in the Carbohydrate-Active enZyme database (CAZy, Lombard et al 2014). Hydrogen peroxide has been shown to be a co-substrate of LPMOs (Bissaro et al 2017)
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