Back to Search
Start Over
Purification, characterization of laccase from Pleurotus ostreatus HK35, and optimization for congo red biodecolorization using Box–Behnken design.
- Source :
-
3 Biotech . 2/14/2024, Vol. 14 Issue 3, p1-17. 17p. - Publication Year :
- 2024
-
Abstract
- This study is the first report on purification, characterization, and application of laccase derived from the white-rot fungus, Pleurotus ostreatus HK35 (Hungary strain), in Congo Red decolorization. The purification process involved ammonium sulfate precipitation, dialysis, anion exchange chromatography, and ultrafiltration, yielding a specific laccase activity of 15.26 U/mg and a 30.21% recovery rate. The purified enzyme, with a molecular weight of approximately 34 kilodaltons, displayed optimal activity at a temperature of 60 °C and pH 4.0 when using 2,2′-azino-bis (3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) as a substrate. The enzyme maintained over 82.02 ± 1.01% of its activity at temperatures up to 50 °C after 180 min but displayed less than 5% of its activity at 60 and 70 °C. Notably, the enzyme's activity was significantly enhanced by Pb(NO3)2, whereas β-mercaptoethanol completely inhibited the activity. Utilizing the Box–Behnken design, we optimized Congo Red decolorization efficiency to 91.05 ± 0.82% at 100 mg/L Congo Red, 1.5 mM mediator concentration, and 1.6 U/mL laccase activity. Analysis of Variance (ANOVA) suggested the model was significant, and all variables significantly influenced decolorization efficiency. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 2190572X
- Volume :
- 14
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- 3 Biotech
- Publication Type :
- Academic Journal
- Accession number :
- 175455071
- Full Text :
- https://doi.org/10.1007/s13205-024-03926-7