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Fig. 7 | Biotechnology for Biofuels

Fig. 7

From: A thermostable bacterial lytic polysaccharide monooxygenase with high operational stability in a wide temperature range

Fig. 7

Synergy between mgLPMO10 and mgCBHs and product profiles for the mgCBHs. a, b show product profiles after degradation of cello-oligosaccharides and Avicel for mgCel6B and mgCel48A, respectively. The enzymes (0.5 µM) were incubated with 0.1 g/L cello-oligosaccharide (DP 2–5) in 50 mM sodium phosphate pH 6.0 at 60 °C. The chromatograms for the oligomeric substrates are from HPEAC-PAD analysis of samples taken after 10 min reaction time for mgCel6B and 30 min reaction time for mgCel48A. The chromatograms for Avicel degradation are the 2 h samples in the experiment shown in c. Note the background signal for glucose in the Avicel-only control and the fact that glucose production by the enzymes was very low. Panel c shows product formation over time during degradation of Avicel by various enzyme combinations. Reaction mixtures were incubated at 60 °C and contained 10 g/L Avicel in 50 mM sodium phosphate buffer pH 6.0, 1 mM AscA and 1 µM of each enzyme. Prior to quantification of native and oxidized solubilized products by HPEAC-PAD, these products were treated with mgCel6A to simplify the product mixture, and the amounts of the various products were converted to cellobiose equivalents. Error bars represent standard deviations with n = 3. Panel d shows the degree of synergy calculated from data in c. Error bars represent propagated standard deviations from c

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