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Enzymatic Cascade Reactions for the Synthesis of Chiral Amino Alcohols from L-lysine
Published on: February 16, 2018
Purification, characterization of laccase from Pleurotus ostreatus HK35, and optimization for congo red
Jantiya Isanapong1, Kittikarn Suwannoi1, Surangkana Lertlattanapong1
1Faculty of Applied Science, Department of Agro-Industrial, Food and Environmental Technology, King Mongkut's University of Technology North Bangkok, 1518 Pracharat 1, Wongsawang, Bangsue, Bangkok, 10800 Thailand.
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.
Supplementary Information:
The online version contains supplementary material available at 10.1007/s13205-024-03926-7.
