Heterologous production and secretion of active-form plant peroxidase in Brevibacillus choshinensis and their monolignol polymerization abilities analysis

Abstract Plant peroxidases are important for several processes, such as defense against pathogens, and auxin metabolism. In this study, we report the active production secretion of plant peroxidase mutated enzymes in bacterium Brevibacillus choshinensis first time world. We introduced mutations into prxA3a , an anionic gene hybrid aspen, Populus × kitakamiensis to substitute amino acid residues at surface protein analyzed their modified substrate specificities. have also reported heterologous expression PrxA3a yeast. Enzymes secreted culture medium by B . chosinensis were purified Ni affinity chromatography, anion-exchange size-exclusion chromatography. The ability polymerize sinapyl alcohol, a monolignol, was higher than that wild-type enzyme. particular, FYAW-mutated enzyme produced showed polymerization activity, similar