INVESTIGATION INTO THE KINETIC-PROPERTIES OF IMMOBILIZED LIGNIN PEROXIDASES

Mixtures of lignin peroxidase isozymes were immobilized onto controlle d pore glass (CPG) beads through three different functional groups (fr ee amino groups, free carboxylate groups, or the aldehyde groups of th e metaperiodate-oxidized carbohydrate portions of the proteins) and ca talytic properties of the immobilized proteins were determined. Some l oss of activity occurred in all immobilized samples, but relatively hi gh activities were maintained with enzymes immobilized via the modifie d carbohydrate moieties. The effectiveness of using the immobilized en zymes to treat anthracene and pulp mill bleach plant effluent was test ed. Bleach plant effluent precipitated onto the aminopropyl-CPG beads inactivating the enzymes, probably due to reactions with free amino gr oups. In contrast, anthracene was rapidly and completely degraded by t he immobilized lignin peroxidases.