ArticleApplied biochemistry and biotechnology2026
Enhanced Oxidative Degradation of β-O-4 Lignin Model Compound Using Robust Lytic Polysaccharide Monooxygenase-Cobalt Phosphate Hybrid Nanoflowers.
Article in Applied biochemistry and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Lignin is a heteropolymer component of ligno-cellulosic biomass made up of monomers connected together by various linkages, the most common of which is the β-O-4 bond. As previously demonstrated, lytic polysaccharide monooxygenase (LPMO) can catalyse the oxidative cleavage of β-O-4 linkage of lignin model compound guaiacyl glycerol-β guaiacyl ether (GGE). But the enhancement of enzymatic activity and stability remains a critical challenge for biocatalytic lignin valorization. In this study, an LPMO-cobalt phosphate organic-inorganic hybrid nanoflower (Co@LPMO-HNF) was developed as a robust biocatalyst for the cleavage of β-O-4 bond. The Co@LPMO-HNF was biochemically and morphologically characterized. Co@LPMO-HNF displayed an optimum temperature of 100 °C and pH 8, exhibiting 1.65-fold higher activity than free LPMO. The Michaelis-Menten kinetic parameters indicated that the Co@LPMO-HNF had 20 fold higher V
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