Laccase of Coriolus zonatus |
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| Authors: | O. V. Koroljova E. V. Stepanova V. P. Gavrilova V. I. Biniukov A. I. Jaropolov S. D. Varfolomeyev F. Scheller A. Makower A. Otto |
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| Affiliation: | (1) Laboratory of Kinetics of Biochemical Processes, A.N. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 117071 Moscow, Russia;(2) V. L. Komarova Institute of Botany, Russian Academy of Sciences, Prof. Popov St. 2, 197376 St. Petersuburg, Russia;(3) The Lomonosov Moscow University, 119809 Moscow, Rusia;(4) Institute for Biochemistry and Molecular Physiology, University of Potsdam, D-14943 Luckenwalde, Germany;(5) c/o Max-Delbruck-Centrum for Molecular Medicine, Robert-Rossle St. 10, 0-1115 Berlin, Germany |
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| 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 entiremolecule lsoelectric point was detected at pH 4.6. Laccase was found to have a pH optimum of 4.9 and temperature optimum of 55°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 k cat and K28 of this reaction were 624 s−1 and 7 μM, respectively. |
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| Keywords: | Laccase enzyme purification Coriolus zonatus substrate specificity thermostability pH stability |
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