Adelpour Tina, Shahverdi Ahmad Reza, Amini Mohsen, Faramarzi Mohammad Ali, Mojtabavi Somayeh
Department of Pharmaceutical Biotechnology, Faculty of Pharmacy & Biotechnology Research Center, Tehran University of Medical Sciences, P.O. Box 14155-6451, Tehran 1417614411, Iran.
Department of Medicinal Chemistry, Faculty of Pharmacy, Tehran University of Medical Sciences, P.O. Box 14155-6451, Tehran 1417614411, Iran.
Int J Biol Macromol. 2025 Aug;319(Pt 2):145172. doi: 10.1016/j.ijbiomac.2025.145172. Epub 2025 Jun 26.
This study presents the successful one-step purification and characterization of a novel laccase derived from Halomonas elongata, an extremophilic bacterium with promising applications in industrial biocatalysis. The enzyme was purified using a Cu@FeO-NH@GA hybrid affinity support, exhibiting a specific activity of 377.8 U mg and a molecular weight of ~75 kDa. Characterized by halophilic properties, the laccase exhibited maximum activity at pH 9 and in the presence of 1.5 mM NaCl, demonstrating remarkable stability in organic solvents and against various inhibitors. The enzyme was successfully applied to the green synthesis of salicylic acid from its alcohol precursor, achieving an 89.9 % yield under optimized conditions: 325.9 U mL laccase, 15.8 mM TEMPO, 36 % solvent-to-buffer ratio, and 38.7 °C. These findings demonstrate the potential of this newly identified laccase as a promising biocatalyst for industrial applications, particularly in eco-friendly organic synthesis.
本研究展示了从嗜盐栖热菌中成功一步纯化和鉴定一种新型漆酶的过程，嗜盐栖热菌是一种在工业生物催化领域具有广阔应用前景的嗜极端微生物。该酶通过Cu@FeO-NH@GA混合亲和载体进行纯化，其比活性为377.8 U mg，分子量约为75 kDa。该漆酶具有嗜盐特性，在pH 9和1.5 mM NaCl存在的条件下表现出最大活性，在有机溶剂中以及面对各种抑制剂时表现出显著的稳定性。该酶成功应用于由其醇前体绿色合成水杨酸，在优化条件下（325.9 U mL漆酶、15.8 mM TEMPO、36%的溶剂与缓冲液比例以及38.7°C）产率达到89.9%。这些发现表明这种新鉴定的漆酶作为一种有前途的生物催化剂在工业应用中，特别是在环保有机合成方面具有潜力。
