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

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.

authors

Koroljova OV,Stepanova EV,Gavrilova VP,Biniukov VI,Jaropolov AI,Varfolomeyev SD,Scheller F,Makower A,Otto A

doi

10.1385/abab:76:2:115

subject

Has Abstract

pub_date

1999-02-01 00:00:00

pages

115-27

issue

2

eissn

0273-2289

issn

1559-0291

pii

ABAB:76:2:115

journal_volume

76

pub_type

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