Green production of a yellow laccase by Coriolopsis gallica for phenolic pollutants removal

Abstract

As a group of green biocatalysts, fungal laccases have aroused great interest in diverse biotechnological fields. Therein, yellow laccase has advantages over blue laccase in catalytic performance, but it is not common in the reported fungal laccases. Here, we report a yellow laccase from white-rot fungus Coriolopsis gallica NCULAC F1 about its production, purification, characterization, and application. Laccase production in the co-fermentation of pomelo peel and wheat bran reached the enzyme activity by 10,690 U/L after 5 days with a 13.58-time increase. After three steps of purification, laccase increased the specific activity from 30.78 to 188.79 U/mg protein with an activity recovery of 45.64%. The purified C. gallica laccase (CGLac) showed a molecular mass of about 57 kDa. CGLac had a yellow color and no absorption peaks at 610 nm and 330 nm, suggesting that it’s a yellow laccase. CGLac exhibited stability towards temperature (40–60 °C) and neutral pH (6.0–8.0). Fe3+ and Mn2+ strongly stimulated CGLac activity by 162.56% and 226.05%, respectively. CGLac remained high activities when exposed to organic reagents and putative inhibitors. Additionally, CGLac contributed to 90.78%, 93.26%, and 99.66% removal of phenol, p-chlorophenol and bisphenol A after 120 min, respectively. In conclusion, a green efficient production strategy was introduced for fungal laccase, and the obtained CGLac presented great enzymatic properties and catalytic potential in the removal of phenolic pollutants.

Immobilization of partially purified laccase on polyhydroxyalkanoate (PHA) microbeads and its application in biodegradation of catechol

“…However, utilizing lignocellulosic biorefinery wastewater in presence of an inducer such as copper sulfate, the same organism produced laccase with specific activity of 30 U g −1 34 . In another study, laccase produced by Coriolopsis gallica , grown in a mix of wheat bran and pomelo peel, reached activity of 10.69 U mL −1 after 5 days 35 . Ammonium sulfate (70–80%) precipitated enzyme showed specific activity of 41.62 U mg −1 .…”

“…34 In another study, laccase produced by Coriolopsis gallica, grown in a mix of wheat bran and pomelo peel, reached activity of 10.69 U mL −1 after 5 days. 35 Ammonium sulfate (70-80%) precipitated enzyme showed specific activity of 41.62 U mg −1 . Of numbered 40 fractions (2.0 mL each) of partially purified enzyme, the highest activity was seen in fractions 4 to 10.…”

Efficient Decolorization of the Poly-Azo Dye Sirius Grey by Coriolopsis gallica Laccase-Mediator System: Process Optimization and Toxicity Assessment

“…This fungus is known for its capacity to grow on several woods to produce ligninolytic enzymes [ 7 , 28 ]. Based on this fact, C. gallica was also shown to degrade many pollutants, including dyes [ 7 , 21 ], hydrocarbons [ 29 ], phenols, and bisphenol A [ 30 ]. Recently, C. gallica was shown to be able to degrade antibiotics [ 31 ].…”

The Role of Microbial Diversity in Lignocellulosic Biomass Degradation: A Biotechnological Perspective

“…Outline examples of bacteria and fungi that produce lignocellulolytic enzymes, along with their respective optimal temperature and pH conditions. Coriolopsis gallica 40-60 6.8 [114] Trametes versicolor 40-50 4.5 [115] Trametes polyzona 55 4.5 [116] Consequently, researchers are extensively investigating microbial genes to address these issues in a sustainable manner [119]. Microbes exhibit remarkable adaptability, thrive in diverse and extreme environments, and are omnipresent throughout the planet.…”