Abstract
The kinetics of the laccase-catalyzed oxidation of model lignin components by oxygen has been studied. It has been shown that in natural lignis the fragments containing guaiacyl groups are enzymatically oxidized without cleavage of the ether bond in the methoxy group. The enzyme has been immobilized by entrapping in polyacrylamide gel and also by covalent attachment to the surface of alkylamine glass. Immobilized laccase was used for the construction of sensors with the Clark oxygen electrode; such sensors can be employed for the determination of the content of lignin-like and phenolic compounds in waste waters.
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