Oxidized Product Profiles of AA9 Lytic Polysaccharide Monooxygenases Depend on the Type of Cellulose
Autor: | Pimvisuth Chunkrua, Peicheng Sun, Willem J. H. van Berkel, Susana V. Valenzuela, Christophe V. F. P. Laurent, Mirjam A. Kabel, Roland Ludwig, F.I.J. Pastor |
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Rok vydání: | 2021 |
Předmět: |
Lytic polysaccharide monooxygenase (LPMO)
General Chemical Engineering Context (language use) Cellobiose Polysaccharide Cleavage (embryo) chemistry.chemical_compound Carbohydrate-binding module (CBM) Levensmiddelenchemie Environmental Chemistry Biomass Cellulose VLAG chemistry.chemical_classification biology Food Chemistry Renewable Energy Sustainability and the Environment Auxiliary Activity (AA) General Chemistry Monooxygenase biology.organism_classification Oxidized cello-oligosaccharide Biorefinery chemistry Biochemistry Product profile Bacterial cellulose Myceliophthora thermophila Research Article |
Zdroj: | ACS Sustainable Chemistry & Engineering ACS Sustainable Chemistry and Engineering, 9(42), 14124-14133 ACS Sustainable Chemistry and Engineering 9 (2021) 42 |
ISSN: | 2168-0485 |
Popis: | Lytic polysaccharide monooxygenases (LPMOs) are essential for enzymatic conversion of lignocellulose-rich biomass in the context of biofuels and platform chemicals production. Considerable insight into the mode of action of LPMOs has been obtained, but research on the cellulose specificity of these enzymes is still limited. Hence, we studied the product profiles of four fungal Auxiliary Activity family 9 (AA9) LPMOs during their oxidative cleavage of three types of cellulose: bacterial cellulose (BC), Avicel PH-101 (AVI), and regenerated amorphous cellulose (RAC). We observed that attachment of a carbohydrate-binding module 1 (CBM1) did not change the substrate specificity of LPMO9B from Myceliophthora thermophila C1 (MtLPMO9B) but stimulated the degradation of all three types of cellulose. A detailed quantification of oxidized ends in both soluble and insoluble fractions, as well as characterization of oxidized cello-oligosaccharide patterns, suggested that MtLPMO9B generates mainly oxidized cellobiose from BC, while producing oxidized cello-oligosaccharides from AVI and RAC ranged more randomly from DP2–8. Comparable product profiles, resulting from BC, AVI, and RAC oxidation, were found for three other AA9 LPMOs. These distinct cleavage profiles highlight cellulose specificity rather than an LPMO-dependent mechanism and may further reflect that the product profiles of AA9 LPMOs are modulated by different cellulose types. AA9 LPMOs generate mainly oxidized cellobiose from bacterial cellulose but more evenly distributed oxidized cello-oligosaccharides from regenerated amorphous cellulose. |
Databáze: | OpenAIRE |
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