State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; Jiangxi Province Key Laboratory of Edible and Medicinal Resources Exploitation, Nanchang University, Nanchang 330031, China; School of Food Science and Technology, Nanchang University, Nanchang 330031, China.
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China; Jiangxi Province Key Laboratory of Edible and Medicinal Resources Exploitation, Nanchang University, Nanchang 330031, China; School of Resource and Environmental and Chemical Engineering, Nanchang University, Nanchang 330031, China.
Int J Biol Macromol. 2021 Apr 15;176:126-136. doi: 10.1016/j.ijbiomac.2021.01.214. Epub 2021 Feb 3.
Enzymatic degradation has become the most promising approach to degrading organic ester compounds. In this study, Bacillus licheniformis NCU CS-5 was isolated from the spoilage of Cinnamomum camphora seed kernel, and its extracellular lipase was purified, with a specific activity of 192.98 U/mg. The lipase was found to be a trimeric protein as it showed a single band of 27 kDa in SDS-PAGE and 81 kDa in Native-PAGE. It was active in a wide range of temperatures (5-55 °C) and pH values (6.0-9.0), and the optimal temperature and pH value were 40 °C and 8.0, respectively. The enzyme was active in the presence of various organic solvents, metal ions, inhibitors and surfactants. Both crude and purified lipase retained more than 80% activity after 5 h in the presence of commercial detergents, suggesting its great application potential in detergent industry. The highest activity was found to be towards medium- and long-chain fatty acids (C-C). Peptide mass spectrometric analysis of the purified lipase showed similarity to the lipase family of B. licheniformis. Furthermore, it degraded more than 90% 2,4-D butyl ester to its hydrolysate 2,4-D within 24 h, indicating that the novel lipase may be applied to degrade organic ester pesticides.
酶降解已成为降解有机酯化合物最有前途的方法。本研究从肉桂种子仁腐败中分离出地衣芽孢杆菌 NCU CS-5，并对其胞外脂肪酶进行了纯化，比活为 192.98 U/mg。脂肪酶在 SDS-PAGE 中显示出 27 kDa 的单条带，在 Native-PAGE 中显示出 81 kDa 的单条带，表明其为三聚体蛋白。该酶在较宽的温度（5-55°C）和 pH 值（6.0-9.0）范围内具有活性，最适温度和 pH 值分别为 40°C 和 8.0。该酶在各种有机溶剂、金属离子、抑制剂和表面活性剂存在下均具有活性。粗酶和纯化酶在商业洗涤剂存在下 5 小时后保留超过 80%的活性，表明其在洗涤剂工业中具有巨大的应用潜力。对纯化脂肪酶的肽质量光谱分析显示与地衣芽孢杆菌的脂肪酶家族具有相似性。此外，它在 24 小时内将 2,4-D 丁酯降解超过 90%，生成其水解产物 2,4-D，表明该新型脂肪酶可能应用于降解有机酯类农药。
