Radveikienė Ingrida, Vidžiūnaitė Regina, Meškys Rolandas, Časaitė Vida
Life Sciences Center, Institute of Biochemistry, Vilnius University, Sauletekio Av. 7, 10257 Vilnius, Lithuania.
J Fungi (Basel). 2024 Aug 8;10(8):559. doi: 10.3390/jof10080559.
Laccases are important and valuable enzymes with a great potential for biotechnological applications. In this study, two novel laccases, LacHU1 and LacHU2, from sp. HU have been purified and characterized. The molecular mass of each isoenzyme was ~66 kDa. LacHU1 laccases was yellow and had no typical blue oxidase spectra and LacHU2 had a blue color and characteristic absorption spectra. The catalytic efficiency of LacHU1 for most substrates was higher than that of LacHU2 laccase. Both isoenzymes effectively oxidize flavonoids. sp. laccases were successfully immobilized on magnetic nanoparticles. The thermostability of immobilized laccases increased and optimal pH shifted to more alkaline compared to the free laccases. Potential applications of laccases from sp. HU are in the oxidation of flavonoids in cotton or in water treatment processes.
漆酶是重要且有价值的酶，在生物技术应用方面具有巨大潜力。在本研究中，已从HU菌株中纯化并表征了两种新型漆酶LacHU1和LacHU2。每种同工酶的分子量约为66 kDa。LacHU1漆酶呈黄色，没有典型的蓝色氧化酶光谱，而LacHU2呈蓝色并有特征吸收光谱。LacHU1对大多数底物的催化效率高于LacHU2漆酶。两种同工酶均能有效氧化类黄酮。HU菌株的漆酶成功固定在磁性纳米颗粒上。与游离漆酶相比，固定化漆酶的热稳定性提高，最佳pH值向更碱性方向移动。HU菌株漆酶的潜在应用在于棉花中类黄酮的氧化或水处理过程。
