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首页> 美国卫生研究院文献>International Journal of Molecular Sciences >New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25 Isolated from Signy Island Antarctica
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New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25 Isolated from Signy Island Antarctica

机译：嗜冷假单胞菌sp。的新的重组的冷适应和有机溶剂耐受的脂肪酶。 LSK25与南极洲Signy Island隔离

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摘要

In recent years, studies on psychrophilic lipases have become an emerging area of research in the field of enzymology. The study described here focuses on the cold-adapted organic solvent tolerant lipase strain Pseudomonas sp. LSK25 isolated from Signy Station, South Orkney Islands, maritime Antarctic. Strain LSK25 lipase was successfully cloned, sequenced, and over-expressed in an Escherichia coli system. Sequence analysis revealed that the lipase gene of Pseudomonas sp. LSK25 consists of 1432 bp, lacks an N-terminal signal peptide and encodes a mature protein consisting of 476 amino acids. The recombinant LSK25 lipase was purified by single-step purification using Ni-Sepharose affinity chromatography and had a molecular mass of approximately 65 kDa. The final recovery and purification fold were 44% and 1.3, respectively. The LSK25 lipase was optimally active at 30 °C and at pH 6. Stable lipolytic activity was reported between temperatures of 5–30 °C and at pH 6–8. A significant enhancement of lipolytic activity was observed in the presence of Ca2+ ions, the organic lipids of rice bran oil and coconut oil, a synthetic C12 ester and a wide range of water immiscible organic solvents. Overall, lipase strain LSK25 is a potentially desirable candidate for biotechnological application, due to its stability at low temperatures, across a range of pH and in organic solvents.
机译：近年来，对嗜冷性脂肪酶的研究已成为酶学领域的新兴研究领域。这里描述的研究集中于耐冷有机溶剂的脂肪酶菌株假单胞菌。 LSK25与南极南奥克尼群岛Signy站隔离。菌株LSK25脂肪酶已在大肠杆菌系统中成功克隆，测序并过表达。序列分析表明假单胞菌属的脂肪酶基因。 LSK25由1432 bp组成，缺少N端信号肽，并编码由476个氨基酸组成的成熟蛋白。重组的LSK25脂肪酶通过使用Ni-Sepharose亲和色谱的一步纯化来纯化，并且分子量约为65kDa。最终回收率和纯化倍数分别为44％和1.3。 LSK25脂肪酶在30°C和pH 6时具有最佳活性。据报道，在5–30°C和pH 6–8之间，脂解活性稳定。在Ca 2 + 离子，米糠油和椰子油的有机脂质，合成的C12酯以及多种与水不混溶的有机溶剂的存在下，脂解活性显着增强。总体而言，脂肪酶菌株LSK25由于在低温，在一定pH值范围内和在有机溶剂中的稳定性而成为生物技术应用的潜在理想候选者。

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