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Fig. 7 | Biotechnology for Biofuels

Fig. 7

From: A novel GH10 xylanase from Penicillium sp. accelerates saccharification of alkaline-pretreated bagasse by an enzyme from recombinant Trichoderma reesei expressing Aspergillus β-glucosidase

Fig. 7

Characterization of PspXyn10ΔCBM. a SDS-PAGE of cellulose-binding and nonbinding fractions, fractionated from limited (papain) degraded PspXyn10. Lanes: 1, purified PspXyn10; 2, nonbinding fraction 1; 3, nonbinding fraction 2; 4, binding fraction 1; 5, binding fraction 2; M, Precision Plus Protein Unstained Standard. b Specific xylanase activities of PspXyn10 and PspXyn10ΔCBM. The enzyme reaction was carried out in 50 mM sodium acetate buffer (pH 5.0) for 5 min for 1% (w/v) beechwood xylan with 1 mg/L enzyme at 50 °C. The values of specific activity are the means of three replicates. Error bars indicate standard deviations. c Adsorption rates of PspXyn10 and PspXyn10ΔCBM to microcrystalline cellulose. 5 μg of protein were incubated with or without 5.0% (w/v) microcrystalline cellulose Avicel PH 101 in 50 mM sodium acetate buffer (pH 5.0) for 30 min at 50 °C under shaking at 150 rpm. Then the supernatant was separated by centrifugation, and subjected to xylanase activity assay. The adsorption rate was measured by subtracting the xylanase activity in supernatant from the total activity loaded. The values of adsorption rate are the means of three replicates. Error bars indicate standard deviations

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