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Figure 4 | Biotechnology for Biofuels

Figure 4

From: A new generation of versatile chromogenic substrates for high-throughput analysis of biomass-degrading enzymes

Figure 4

Direct comparison of the output from CPH substrates with the measurement of reducing ends. (A) Each well in the reaction plate contained one of the four different CPH substrates: blue CPH-arabinoxylan (ARAXYLAN); yellow CPH-xylan, (XYLAN); red CPH-β-glucan (BETAGLC) and green CPH-galactomannan (GALMAN). The substrates were treated with the enzymes: xylanase nz1; xylanase nz2; glucanase nz3 or mannanase (nz4) as shown to the right (note that all wells in one row contained the enzymes or control buffer indicted). All enzymes were used at 5 μg/mL in 50 mM sodium acetate buffer, pH 5.5 and incubated at 50°C for 10 min. (B) Product plate containing the product of the reaction shown in (A). (C) Table showing the relative activities of the enzymes nz1 to nz4 as determined by the production of reducing ends when native versions of the polysaccharides shown in (A) were treated with enzymes nz1 to nz4 used at 5 μg/mL in 50 mM sodium acetate buffer, pH 5.5 at 50°C for 10 min. The highest value was set to 100, and all other values adjusted accordingly. In this case, the PAHBAH reducing end assay was used. See Tables 1 and 2 for details of the substrates and enzyme used.

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