earticle

영어

Expressed as insoluble forms in E. coli, native CWPO_C (cell wall peroxidase from poplar tree) and mutated variants were successfully reactivated throughout refolding experiments and used for elucidating the previously presumed existence of electron transfer pathway in CWPO_C structure. Their catalytic properties were fully characterized through analysis such as steady state kinetics, direct oxidation of lignin macromolecules respectively accompanying with their stabilities during polymerization reactions, which proved strongly that the 74th residue on the CWPO_C structure plays the important role in catalyzing the macromolecules throughout electron transfer mechanism. This study also contributed deeper understanding about role of aromatic amino acids in electron transfer mechanism usually manipulated by peroxidase/H2O2 catalyst system. Furthermore, we also successfully synthesize the highly bioactive poly(catechin) by applying radical robust CWPO_C mutant in extension of poly(catechin). Anti-oxidation activity of synthesized poly(catechin) was confirmed by xanthine oxidase assay. The elucidation of uniquely catalytic mechanism in CWPO_C may improve applicability of peroxidase/H2O2 catalyst in conducting green polymer chemistry.