Laccase production by a monokaryotic strain of Pycnoporus cinnabarinus derived from a dikaryotic strain

• Published in: World journal of microbiology & biotechnology Vol. 15; no. 4; pp. 481 - 484
• Main Authors: Sigoillot, J.C, Herpoel, I, Frasse, P, Moukha, S, Lesage-Meessen, L, Marcel, A
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer 01.08.1999; Springer Nature B.V
• Subjects: Biological and medical sciences; biological production; Biotechnology; Enzyme engineering; Enzymes; Fermentation; ferulic acid; Fundamental and applied biological sciences. Psychology; Methods. Procedures. Technologies; Production of selected enzymes; Pycnoporus cinnabarinus; Studies; Trametes versicolor; Fungi; Purification; Enzymatic activity; Enzyme; Production; N terminal-Sequence; Microorganism culture; Homology; Oxidoreductases; Aminoacid sequence; Thallophyta; Laccase
• ISSN: 0959-3993; 1573-0972
• DOI: 10.1023/A:1008986809395

Monokaryotic Pycnoporus cinnabarinus strains were obtained from the dikaryotic strain I-938. One of these, designated MK18, consistently produced high laccase activity. In cultures of MK18 and I-938 where ferulic acid was added as laccase inducer, laccase activity was enhanced about 2.5-fold reaching 3400 U/l for the MK18 strain. Laccase was purified to homogeneity and under the selected growth conditions, only one isoform of the enzyme was produced. The N-terminal sequence was similar to the amino terminal sequence of laccase II from Trametes versicolor. The enzyme was stable at 60 ^sup ^C for more than 1 h.[PUBLICATION ABSTRACT]