两相体系中固定化黏红酵母CCZU-G5催化合成 (R)-2-羟基-4-苯基丁酸乙酯

通过筛选得到一株高立体选择性还原2-氧代-4-苯基丁酸乙酯（OPBE）合成(R)-2-羟基-4-苯基丁酸乙酯[(R)-HPBE]的菌株并鉴定为黏红酵母。研究了在异辛烷/水两相体系中固定化黏红酵母CCZU-G5不对称还原OPBE合成(R)-HPBE的反应条件。结果表明最适的反应条件为：在异辛烷比例为10%条件下,底物浓度为100 mmol/L,催化剂用量为0.45 g/mL,辅底物为40 g/L的葡萄糖。在建立的反应体系中反应16 h,(R)-HPBE产率最高,达83.5%,e.e.值99%以上。固定化酵母经7次重复使用后,产率和e.e.值分别维持在70%和99%以上。     

Production of a halotolerant lipase from Halomonas sp. strain C2SS100: Optimization by response-surface methodology and application in detergent formulations

The aim of this work was to optimize the production of a new lipase by a halotolerant bacterial strain Halomonas sp. C2SS100, by means of the response-surface methodology (RSM). The process parameters having the most significant effect on lipase production were identified using the Plackett–Burman screening design-of-experiments. Then, Box–Behnken design was applied to optimize lipase activity and the quadratic regression model of the lipase production was built. Indeed, the lipase yield was increased, and the value obtained experimentally (39 ± 2 U/ml) was very close to the rate predicted by the model (40.3 U/ml). Likewise, optimization of parameters by RSM resulted in 2.78-fold increase in lipase activity. These findings provide the first report on lipase production and optimization by a halotolerant bacterial strain belonging to Halomonas genus. Afterward, the biochemical properties of the produced lipase were studied for apply in oil stains removal. The crude lipase showed a maximum activity at 60°C and at pH ranging from 7 to 10. It displayed an important stability at high temperature, pH, and NaCl. Interestingly, this bacterial lipase exhibited a prominent stability toward some commercial solid and liquid detergents after 30 min of incubation at 50°C. The capability of the crude lipase to eliminate stain was ascertained on polycotton fabric pieces stained with lubricating oil. Whether with the addition of hot water alone or of a commercially available detergent, lipase is able to considerably boost the elimination of oil stains. The actual findings highlight the capacity of Halomonas sp. lipase for energy-efficient biocatalytic application.