Expanding the application of lignin peroxidases from Irpex Lacteus in Lignin degradation by exploring the effects of small molecules on enzyme activity

Abstract

Lignin peroxidase can degrade lignin in a relatively high efficiency, the highly efficient application of lignin peroxidase for environmental prevention and governance was promoted by exploring the effects of small molecule substances on lignin peroxidase activities. In this study, the lignin peroxidase (LiP) gene from Irpex Lacteus was heterologous expressed in Escherichia coli. The activity of the recombinant LiP was 11.2 U/mg, the optimum temperature was 37℃, and the optimum pH was 3.5. In the range of 20-45℃ and pH 2.0-4.0, the relative enzyme activity remained above 50%, showing good acid resistance, Zn2+, malonic acid, glycerol and other substances can promote the activity of LiP enzyme, among which Zn2+ can increase the activity of LiP enzyme to 256%, and when the glycerol supplemental level is 3%, the activity of LiP enzyme can increase to 186%. This study for the first time verified the promoting effect of glycerol on LiP enzyme activity, serving as a reference for LiP in studies on lignin breakdown and paper wastewater treatment.