Improved activity and stability of an immobilized recombinant laccase in organic solvents

Annia I. Ruiz, Adriel J. Malavé, Claus Felby, Kai Griebenow

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

Laccase (E.C. 1.10.3.2) from Trametes versicolor was immobilized (adsorbed) by drying on various supports (glass, glass powder, silica gel, and Nylon 66 membrane). The enzyme activity and stability were determined in diethyl ether, ethyl acetate, and methylene chloride. The initial rate for the oxidation of syringaldazine varied up to 245-fold depending on the solvent and support, the best results being obtained with Nylon 66 membrane. No inactivation of immobilized laccase over 72 h was observed in diethyl ether and ethyl acetate, while exposure to methylene chloride resulted in significant activity decreases regardless of the support material.

Original languageEnglish (US)
Pages (from-to)229-233
Number of pages5
JournalBiotechnology Letters
Volume22
Issue number3
DOIs
StatePublished - Jan 1 2000
Externally publishedYes

Keywords

  • Dioxygenase
  • Enzyme activation
  • Enzyme immobilization
  • Non-aqueous enzymology

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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