A novel GH1 β-glucosidase gene (bgla) from marine bacterium was sequenced and expressed in Escherichia coli. After purification by Ni²⁺ affinity chromatography, the recombinant protein was characterized. The purified recombinant enzyme showed maximum activity at 40 °C, pH 7.5 and was stable between temperatures that range from 4 to 30 °C and over the pH range of 6–10. The enzyme displayed a high tolerance to glucose and maximum stimulation at the presence of 100 mM glucose. To improve glucose tolerance of the enzyme, a site-directed mutation (f171w) was introduced into β-glucosidase. The recombinant F171W showed a higher glucose tolerance than the wild type and maintained more than 40% residual activity at the presence of 4 M glucose. Additionally, the recombinant enzymes showed notable tolerance to ethanol. These properties suggest the enzymes may have potential applications for the fermentation of lignocellulosic sugars and the production of biofuels.

对海洋细菌的GH1β-葡萄糖苷酶基因（bgla）进行了测序，并在大肠杆菌中表达。通过Ni ²⁺亲和层析纯化后，表征重组蛋白。纯化的重组酶在40°C，pH 7.5时显示最大活性，并且在4至30°C的温度和6-10的pH范围内稳定。该酶在100 mM葡萄糖存在下显示出对葡萄糖的高度耐受性和最大刺激。为了提高酶的葡萄糖耐量，定点突变（f171w）被引入β-葡萄糖苷酶。重组F171W显示出比野生型更高的葡萄糖耐量，并在存在4 M葡萄糖时保持超过40％的残留活性。另外，重组酶显示出对乙醇的显着耐受性。这些性质表明，这些酶对于木质纤维素糖的发酵和生物燃料的生产可能具有潜在的应用。