Laboratory of Biochemistry and Enzymatic Engineering of Lipases, Engineering National School of Sfax (ENIS), University of Sfax, Sfax, Tunisia.
Laboratoire MMS Mer Molécules Santé (EA2160), Université du Maine, IUT de Laval Génie Biologique, Laval cedex 09, France.
Prep Biochem Biotechnol. 2024 Jul;54(6):736-748. doi: 10.1080/10826068.2023.2279111. Epub 2023 Nov 8.
The study illustrated here aims on an organic solvent tolerant lipase from (SCL). The gene part, encoding the mature lipase, was cloned and sequenced. The concluded polypeptide sequence, equivalent to the protein, consist of 388 amino acid residues with a molecular mass of about 45 kDa. A structure-based alignment of the SCL amino acid sequence shows high identities with those many staphylococcal lipases. From this alignment of sequences, the catalytic triad (Ser 117, Asp 308 and His 347) of SCL could be identified. The mature part of the SCL was expressed in and the recombinant lipase (r-SCL) was purified to homogeneity. The purified r-SCL presented a quite interesting stability at low temperatures (< 30 °C) and the enzyme was found to be highly stable in polar organic solvent and at a pH ranging from 3 to 12. After that, we have demonstrated that the recombinant enzyme may be implicated in the biodegradability of oily wastewater from effluents of fast-food restaurants; the maximum conversion yield into fatty acids obtained at 30 °C, was 65%.
本研究旨在研究一种来自 （SCL）的耐有机溶剂脂肪酶。克隆并测序了编码成熟脂肪酶的基因片段。得出的多肽序列与蛋白质相当，由 388 个氨基酸残基组成，分子量约为 45 kDa。基于结构的 SCL 氨基酸序列比对显示与许多葡萄球菌脂肪酶具有高度的同一性。从这个序列比对中，可以鉴定出 SCL 的催化三联体（Ser117、Asp308 和 His347）。SCL 的成熟部分在 中表达，重组脂肪酶（r-SCL）被纯化至均一性。纯化的 r-SCL 在低温（<30°C）下表现出相当有趣的稳定性，并且该酶在极性有机溶剂中和 pH 值为 3 到 12 的范围内非常稳定。之后，我们证明了重组酶可能参与快餐店废水的含油废水的生物降解；在 30°C 下获得的最大脂肪酸转化率为 65%。
