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Figure 7 | Biotechnology for Biofuels

Figure 7

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

Figure 7

Using CPH substrates to analyse LPMO and protease activities. (A) The LPMO NcLPMO9C was tested using three different CPH substrates, from left to right; blue CPH-HE cellulose; blue CPH-lichenan and blue CPH-xylan. NcLPMO9C was tested with and without ascorbic acid (AA, used at 3.2 mM), and ascorbic acid alone was used as a control. Note that activity was observed for the two CPH substrate that contained β-linked glucan (blue CPH-HE cellulose; blue CPH-lichenan) but not blue CPH-xylan. All incubations were in 100 mM potassium phosphate buffer, pH 7.0 incubated for 1 h at 50°C. (B) Blue CPH-casein was treated with 0.1 U/mL trypsin, elastase and proteinase K (containing 10 mM Ca2+) in 100 mM sodium phosphate pH 7.0 for 20 min at room temperature. See Tables 1 and 2 for details of the substrates and enzyme used.

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