Ben Bacha Abir, Al-Assaf Alaa, Moubayed Nadine M S, Abid Islem
Biochemistry Department, Science College, King Saud University, P.O Box 22452, Riyadh 11495, Saudi Arabia.
Laboratory of Plant Biotechnology Applied to Crop Improvement, Faculty of Science of Sfax, University of Sfax, Sfax 3038, Tunisia.
Saudi J Biol Sci. 2018 Mar;25(3):409-417. doi: 10.1016/j.sjbs.2016.10.006. Epub 2016 Oct 14.
An extracellular lipase of a newly isolated strain ALA1 (SAL4) was purified from the optimized culture medium. The SAL4 specific activity determined at 60 °C and pH 12 by using olive oil emulsion or TC4, reached 7215 U/mg and 2484 U/mg, respectively. The 38 NH-terminal amino acid sequence of the purified enzyme starting with two extra amino acid residues (LK) was similar to known staphylococcal lipase sequences. This novel lipase maintained almost 100% and 75% of its full activity in a pH range of 4.0-12 after a 24 h incubation or after 0.5 h treatment at 70 °C, respectively. Interestingly, SAL4 displayed appreciable stability toward oxidizing agents, anionic and non-ionic surfactants in addition to its compatibility with several commercial detergents. Overall, these interesting characteristics make this new lipase promising for its application in detergent industry.
从优化培养基中纯化出一株新分离菌株ALA1（SAL4）的胞外脂肪酶。使用橄榄油乳液或TC4在60°C和pH 12条件下测定的SAL4比活性分别达到7215 U/mg和2484 U/mg。纯化酶的38个N端氨基酸序列从两个额外的氨基酸残基（LK）开始，与已知的葡萄球菌脂肪酶序列相似。这种新型脂肪酶在4.0 - 12的pH范围内，分别经过24小时孵育或在70°C处理0.5小时后，仍保持近100%和75%的全活性。有趣的是，SAL4除了与几种商用洗涤剂具有兼容性外，还对氧化剂、阴离子和非离子表面活性剂表现出明显的稳定性。总体而言，这些有趣的特性使这种新型脂肪酶在洗涤剂工业中的应用前景广阔。
