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• W2079063800 abstract "A major β-glucosidase I and a minor β-glucosidase II were purified from culture filtrates of the fungus Trichoderma reesei grown on wheat straw. The enzymes were purified using CM-Sepharose CL-6B cation-exchange and DEAE Bio-Gel A anion-exchange chromatography steps, followed by Sephadex G-75 gel filtration. The isolated enzymes were homogeneous in SDS-polyacrylamide gel electrophoresis and isoelectric focusing. β-Glucosidase I (71 kDa) was isoelectric at pH 8.7 and contained 0.12% carbohydrate: β-glucosidase II (114 kDa) was isoelectric at pH 4.8 and contained 9.0% carbohydrate. Both enzymes catalyzed the hydrolysis of cellobiose and p-nitrophenyl-β-d-glucoside (pNPG). The Km and kcat/Km values for cellobiose were 2.10 mM, 2.45 · 104 s−1 M−1 (β-glucosidase I) and 11.1 mM, 1.68 · 103 s−1 M−1 (β-glucosidase II). With pNPG as substrate the Km and kcat/Km values were 182 μM, 7.93 · 105 s−1 M−1 (β-glucosidase I) and 135 μM, 1.02 · 106 s−1 M−1 (β-glucosidase II). The temperature optimum was 65–70°C for β-glucosidase I and 60°C for β-glucosidase II, the pH optimum was 4.6 and 4.0, respectively. Several inhibitors were tested for their action on both enzymes. β-Glucosidase I and II were competitively inhibited by desoxynojirimycin, gluconolactone and glucose." @default.
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• W2079063800 date "1992-05-01" @default.
• W2079063800 modified "2023-10-17" @default.
• W2079063800 title "Purification and characterization of two extracellular β-glucosidases from Trichoderma reesei" @default.
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• W2079063800 doi "https://doi.org/10.1016/0167-4838(92)90336-c" @default.
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