Applied Biochemistry and Biotechnology

, Volume 49, Issue 3, pp 257–280

Laccase

Properties, catalytic mechanism, and applicability

Authors

  • A. I. Yaropolov
    • Laboratory of Kinetics of Biochemical Processes, A. N. Bach Institute of BiochemistryRussian Academy of Sciences
  • O. V. Skorobogat’ko
    • Laboratory of Kinetics of Biochemical Processes, A. N. Bach Institute of BiochemistryRussian Academy of Sciences
  • S. S. Vartanov
    • Laboratory of Kinetics of Biochemical Processes, A. N. Bach Institute of BiochemistryRussian Academy of Sciences
  • S. D. Varfolomeyev
    • The Lomonosov Moscow University
Article

DOI: 10.1007/BF02783061

Cite this article as:
Yaropolov, A.I., Skorobogat’ko, O.V., Vartanov, S.S. et al. Appl Biochem Biotechnol (1994) 49: 257. doi:10.1007/BF02783061

Abstract

The present review was dedicated to laccase—the enzyme, belonging to the group of multinuclear copper, containing so called “blue” oxidases. The molecular structure, metals content, substrate specificity, and other physicochemical properties were described in this article. The authors considered the mechanism of enzymatic action and electrocatalytic oxygen reduction catalyzed by laccase in details. The data of laccase application in organic synthesis, biosensors, and immunoenzyme assay were presented.

Index Entries

Laccasecatalytic mechanismelectron-transferbioelectrocatalysisimmunoenzyme assaybiosensorsenzymatic synthesis
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Copyright information

© Humana Press Inc 1994