Lima Natália Sarmanho Monteiro, Gomes-Pepe Elisângela Soares, Campanharo João Carlos, de Macedo Lemos Eliana Gertrudes
Department of Agricultural and Environmental Biotechnology, São Paulo State University, Jaboticabal Campus, Jaboticabal, São Paulo State, 14884-900, Brazil.
Molecular Biology Laboratory, Institute for Research in Bioenergy (IPBEN), Jaboticabal, São Paulo State, 14884-900, Brazil.
AMB Express. 2022 Mar 23;12(1):38. doi: 10.1186/s13568-022-01375-0.
Laccases are multicopper oxidases that act on various phenolic and non-phenolic compounds, enabling numerous applications including xenobiotic bioremediation, biofuel production, drug development, and cosmetic production, and they can be used as additives in the textile and food industries. This wide range of uses makes these enzymes extremely attractive for novel biotechnology applications. Here, we undertook the kinetic characterization of LacMeta, a predicted as homotrimeric (~ 107,93 kDa) small laccase, and demonstrated that this enzyme performs best at an acidic pH (pH 3-5) towards ABTS as substrate and has a broad thermal spectrum (10-60 °C), which can promote high plastic action potential through dynamic environmental temperature fluctuations. This enzyme showed following kinetic parameters: k = 6.377 s ± 0.303, K = 4.219 mM, and V = 24.43 µM/min (against ABTS as substrate). LacMeta almost completely degraded malachite green (50 mg/mL) in only 2 h. Moreover, the enzyme was able to degrade seven dyes from four distinct classes and it respectively achieved 85% and 83% decolorization of methylene blue and trypan blue with ABTS as the mediator. In addition, LacMeta showed potential for the degradation of two thirds of an agricultural fungicide: fentin hydroxide, thus demonstrating its biotechnological aptitude for bioremediation. The results of this study suggest that LacMeta has potential in textile wastewater treatment and that it could help in the bioremediation of other human/environmental toxins such as pesticides and antibiotic compounds belonging to the same chemical classes as the degraded dyes.
漆酶是一种多铜氧化酶，作用于各种酚类和非酚类化合物，具有多种应用，包括外源生物修复、生物燃料生产、药物开发和化妆品生产，还可作为纺织和食品工业中的添加剂。这种广泛的用途使这些酶在新型生物技术应用中极具吸引力。在此，我们对预测为同三聚体（约107,93 kDa）的小型漆酶LacMeta进行了动力学表征，结果表明该酶以ABTS为底物时在酸性pH（pH 3 - 5）下表现最佳，并且具有较宽的热谱范围（10 - 60°C），通过动态环境温度波动可促进高塑性作用潜力。该酶表现出以下动力学参数：k = 6.377 s ± 0.303，K = 4.219 mM，V = 24.43 μM/min（以ABTS为底物）。LacMeta仅在2小时内就几乎完全降解了孔雀石绿（50 mg/mL）。此外，该酶能够降解来自四个不同类别的七种染料，以ABTS为介质时分别实现了亚甲基蓝和台盼蓝85%和83%的脱色。此外，LacMeta对三分之二的农业杀菌剂：氢氧化三苯锡具有降解潜力，从而证明了其在生物修复方面的生物技术适用性。本研究结果表明，LacMeta在纺织废水处理方面具有潜力，并且有助于对其他人类/环境毒素进行生物修复，例如与降解染料属于同一化学类别的农药和抗生素化合物。
