Format

Send to

Choose Destination
See comment in PubMed Commons below
Appl Biochem Biotechnol. 1999 Feb;76(2):115-27.

Laccase of Coriolus zonatus: isolation, purification, and some physicochemical properties.

Author information

1
Laboratory of Kinetics of Biochemical Processes, A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow 117071, Russia. inbio@pop.glas.apc.org

Abstract

Laccase is one of the lignolytic enzymes found in liquid cultures of the fungus Coriolus zonatus in defined medium. The enzyme was isolated from culture liquid and characterized. Laccase from C. zonatus is a single-chain protein with a molecular mass of 60 kDa. Carbohydrate moiety of enzyme consisted of mannose, galactose and N-acetyl-glucosamine in a ratio of 6:2:0.6, respectively, and comprised 10% of the entire molecule. Isoelectric point was detected at pH 4.6. Laccase was found to have a pH optimum of 4.9 and temperature optimum of 55 degrees C. Substrate specificity studies were conducted with catechol, K-ferrocyanide, hydroquinone, and sinapinic acid as substrates. The highest efficiency of catalysis was observed with sinapic acid as the substrate. The kinetic constants kcat and Km of this reaction were 624 s-1 and 7 microM, respectively.

PMID:
15304730
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Loading ...
    Support Center