Degradation of triphenylmethane dyes using a temperature and pH stable spore laccase from a novel strain of Bacillus vallismortis.
The characterization of a spore laccase from Bacillus vallismortis fmb-103, isolated from textile industry disposal sites, is described. The activity was 6.5 U/g of dry spore with ABTS as the substrate. The enzyme was quite stable at high temperature. It retained more than 90% of its initial activity after 10h at 70 °C. The enzyme demonstrated broad pH stability in both acidic and alkaline conditions. There was almost no activity loss at pH 3 over an extended period of time, and the relative activity remained at 82% and 38% at pH 7 and pH 9 after 10 days. NaN(3), SDS, L-cysterine, Dithiothreitol, EDTA and NaCl inhibit the enzyme activity. Triphenylmethane dyes, including malachite green, brilliant green and aniline blue were efficiently degraded by the enzyme after 24h in combination with a mediator with efficiencies of 76.84%, 96.56% and 81.17%, respectively. The reusability of spore laccase for decolorization dyes was also examined.
Laboratory of Enzyme Engineering, College of Food Science and Technology, Nanjing Agriculture University, Nanjing 210095, PR China.
Chong
C
Zhang
Hanwen
H
Diao
Fengxia
F
Lu
Xiaomei
X
Bie
Yufeng
Y
Wang
Zhaoxin
Z
Lu
D001407:Bacillus / Q000187:drug effects / Q000201:enzymology*; D001673:Biodegradation, Environmental / Q000187:drug effects; D003116:Color; D004396:Coloring Agents / Q000302:isolation & purification*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability / Q000187:drug effects; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D042845:Laccase / Q000378:metabolism*; D008969:Molecular Sequence Data; D010802:Phylogeny; D013171:Spores, Bacterial / Q000187:drug effects / Q000201:enzymology; D013696:Temperature; D014320:Triphenylmethyl Compounds / Q000302:isolation & purification*
D004396:Coloring Agents; D004791:Enzyme Inhibitors; D014320:Triphenylmethyl Compounds; C046945:triphenylmethane; D042845:Laccase