Role of surface tryptophan for peroxidase oxidation of nonphenolic lignin.

ABSTRACT:

Background

Despite claims as key enzymes in enzymatic delignification, very scarce information on the reaction rates between the ligninolytic versatile peroxidase (VP) and lignin peroxidase (LiP) and the lignin polymer is available, due to methodological difficulties related to lignin heterogeneity and low solubility.

Results

Two water-soluble sulfonated lignins (from Picea abies and Eucalyptus grandis) were chemically characterized and used to estimate single electron-transfer rates to the H₂O₂-activated Pleurotus eryngii VP (native enzyme and mutated variant) transient states (compounds I and II bearing two- and one-electron deficiencies, respectively). When the rate-limiting reduction of compound II was quantified by stopped-flow

SUBMITTER: Saez-Jimenez V 

PROVIDER: S-EPMC5467052 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature