Reaction of substituted phenols with thermostable laccase bound to Bacillus subtilis spores.
A strain of B. subtilis produced 1.8 times more laccase on sporulation medium than on non-sporulation medium. Spores oxidized mono- and di-methoxyphenols (0.1 mM) at 50 degrees C. The half-life of laccase bound to spores was about 2 d and the substrate was repeatedly removed by spores recovered from the reaction mixture.
Department of Applied Chemistry, Faculty of Engineering, Miyazaki University, Miyazaki 889-2192, Japan. jhirose@cc.miyazaki-u.ac.jp
Jun
J
Hirose
Masako
M
Nasu
Haruhiko
H
Yokoi
D001412:Bacillus subtilis / Q000737:chemistry* / Q000145:classification / Q000201:enzymology* / Q000502:physiology; D001673:Biodegradation, Environmental; D042845:Laccase / Q000737:chemistry* / Q000378:metabolism*; D010636:Phenols / Q000378:metabolism*; D011485:Protein Binding; D013045:Species Specificity; D013171:Spores, Bacterial / Q000737:chemistry* / Q000145:classification / Q000201:enzymology*; D013696:Temperature
D010636:Phenols; D042845:Laccase