InduBioCat Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 5 Iroon Polytechniou Str., Zografou Campus, 15780 Athens, Greece.
Biochemical and Chemical Process Engineering, Division of Sustainable Process Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, SE-97187 Luleå, Sweden.
Molecules. 2020 May 8;25(9):2221. doi: 10.3390/molecules25092221.
The enzymatic factory of ligninolytic fungi has proven to be a powerful tool in applications regarding the degradation of various types of pollutants. The degradative potential of fungi is mainly due to the production of different types of oxidases, of which laccases is one of the most prominent enzymatic activities. In the present work, crude laccases from the supernatant of cultures grown in olive oil mill wastewater (OOMW) were immobilized in crosslinked enzyme aggregates (CLEAs), aiming at the development of biocatalysts suitable for the enzymatic treatment of OOMW. The preparation of laccase CLEAs was optimized, resulting in a maximum of 72% residual activity. The resulting CLEAs were shown to be more stable in the presence of solvents and at elevated temperatures compared to the soluble laccase preparation. The removal of the phenolic component of OOMW catalyzed by laccase-CLEAs exceeded 35%, while they were found to retain their activity for at least three cycles of repetitive use. The described CLEAs can be applied for the pretreatment of OOMW, prior to its use for valorization processes, and thus, facilitate its complete biodegradation towards a consolidated process in the context of circular economy.
木质素降解真菌的酶工厂已被证明是一种强大的工具,可用于降解各种类型的污染物。真菌的降解能力主要归因于不同类型氧化酶的产生,其中漆酶是最突出的酶活性之一。在本工作中,从橄榄油厂废水(OOMW)培养物的上清液中提取的粗漆酶被固定在交联酶聚集体(CLEAs)中,旨在开发适用于 OOMW 酶处理的生物催化剂。优化了漆酶 CLEAs 的制备,使其残余活性最高可达 72%。与可溶性漆酶制剂相比,所得 CLEAs 在溶剂存在下和高温下更稳定。漆酶-CLEAs 催化的 OOMW 中酚类成分的去除率超过 35%,同时发现它们在至少三个重复使用周期中保持其活性。所描述的 CLEAs 可用于 OOMW 的预处理,然后再将其用于增值过程,从而促进其完全生物降解,以实现循环经济背景下的综合处理。