Laboratoire de Biologie Cellulaire Fongique, UMR Centre National de la Recherche Scientifique 106, Université de Lyon 1, Bâtiment 405-43, Boulevard du 11 Novembre 1918, 69622 Villeurbanne Cedex, France.
Appl Environ Microbiol. 1990 Oct;56(10):3164-9. doi: 10.1128/aem.56.10.3164-3169.1990.
A glycoside hydrolase characterized by beta-fucosidase (EC 3.2.1.38) and beta-glucosidase (EC 3.2.1.21) activities was purified from the culture medium of the anaerobic ruminal phycomycete Neocallimastix frontalis grown on 0.5% Avicel. The enzyme had a molecular mass of 120 kilodaltons and a pI of 3.85. Optimal activity against p-nitrophenyl-beta-d-fucoside and p-nitrophenyl-beta-D-glucoside occurred at pH 6.0 and 50 degrees C. The beta-fucosidase and beta-glucosidase activities were stable from pH 6.0 to pH 7.8 and up to 40 degrees C. They were both inhibited by gluconolactone, sodium dodecyl sulfate, p-chloromercuribenzoate, and Hg cation. The enzyme had K(m)s of 0.26 mg/ml for p-nitrophenyl-beta-d-fucoside and 0.08 mg/ml for p-nitrophenyl-beta-d-glucoside. The purified protein also had low beta-galactosidase activity.
一种糖苷水解酶，具有β-岩藻糖苷酶（EC 3.2.1.38）和β-葡萄糖苷酶（EC 3.2.1.21）活性，从在 0.5%Avicel 上生长的厌氧瘤胃真菌 Neocallimastix frontalis 的培养液中纯化得到。该酶的分子量为 120 千道尔顿，等电点为 3.85。对 p-硝基苯-β-d-岩藻糖苷和 p-硝基苯-β-D-葡萄糖苷的最佳活性发生在 pH6.0 和 50°C。β-岩藻糖苷酶和β-葡萄糖苷酶活性在 pH6.0 到 pH7.8 和高达 40°C 时稳定。它们都被葡萄糖酸内酯、十二烷基硫酸钠、对氯汞苯甲酸酯和 Hg 阳离子抑制。该酶对 p-硝基苯-β-d-岩藻糖苷的 K(m)为 0.26mg/ml，对 p-硝基苯-β-d-葡萄糖苷的 K(m)为 0.08mg/ml。纯化的蛋白质还具有低的β-半乳糖苷酶活性。
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