title: Characterization of alkaliphilic laccase activity in the culture supernatant of Myrothecium verrucaria 24G-4 in comparison with bilirubin oxidase.
abstract: An enzyme showing alkaliphilic laccase activity was purified from the culture supernatant of Myrothecium verrucaria 24G-4. The enzyme was highly stable under alkaline conditions, showed an optimum reaction pH of 9.0 for 4-aminoantipyrine/phenol coupling, and decolorized synthetic dyes under alkaline conditions. It showed structural and catalytic similarities with bilirubin oxidase, but preferably oxidized phenolic compounds. The enzyme catalyzed veratryl alcohol oxidation at pH 9.0 with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a mediator, suggesting that the laccase mediator system functioned well under alkaline conditions.
authors.affiliation: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-oiwakecho, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: Woro Triarsi
authors.initials: WT
authors.lastname: Sulistyaningdyah
authors.forename: Jun
authors.initials: J
authors.lastname: Ogawa
authors.forename: Hiromi
authors.initials: H
authors.lastname: Tanaka
authors.forename: Chiharu
authors.initials: C
authors.lastname: Maeda
authors.forename: Sakayu
authors.initials: S
authors.lastname: Shimizu
mesh_terms: D000595:Amino Acid Sequence; D001203:Ascomycota / Q000201:enzymology* / Q000254:growth & development*; D017077:Culture Media, Conditioned; D006863:Hydrogen-Ion Concentration; D042845:Laccase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000378:metabolism*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D017077:Culture Media, Conditioned; D042845:Laccase; D044925:Oxidoreductases Acting on CH-CH Group Donors; C042401:bilirubin oxidase