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Investigation into the kinetic properties of immobilized lignin peroxidases

Journal of Biotechnology 35(1): 77-85
Investigation into the kinetic properties of immobilized lignin peroxidases
Mixtures of lignin peroxidase isozymes were immobilized onto controlled-pore glass (CPG) beads through three different functional groups (free amino groups, free carboxylate groups, or the aldehyde groups of the metaperiodate-oxidized carbohydrate portions of the proteins) and catalytic properties of the immobilized proteins were determined. Some loss of activity occurred in all immobilized samples, but relatively high activities were maintained with enzymes immobilized via the modified carbohydrate moieties. The effectiveness of using the immobilized enzymes to treat anthracene and pulp mill bleach plant effluent was tested. Bleach plant effluent precipitated onto the aminopropyl-CPG beads inactivating the enzymes, probably due to reactions with free amino groups. In contrast, anthracene was rapidly and completely degraded by the immobilized lignin peroxidases.

Accession: 002416720

DOI: 10.1016/0168-1656(94)90191-0

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