Characterization of alkaliphilic laccase activity in the culture supernatant of Myrothecium verrucaria 24G-4 in comparison with bilirubin oxidase.
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.
Sulistyaningdyah
Woro Triarsi
WT
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-oiwakecho, Sakyo-ku, Kyoto 606-8502, Japan.
Ogawa
Jun
J
Tanaka
Hiromi
H
Maeda
Chiharu
C
Shimizu
Sakayu
S
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
D017077:Culture Media, Conditioned; D042845:Laccase; D044925:Oxidoreductases Acting on CH-CH Group Donors; C042401:bilirubin oxidase