Cottonseed meal (CSM) is the major by-product of the cottonseed oil extraction process with high protein content. However, the presence of free gossypol (FG) in CSM severely restricts its utilization in the food and animal feed industries. The development of a biological strategy for the effective removal of FG in CSM has become an urgent need. In this study, three bacterial laccases including CotA from , CueO from , and LcLac from were heterologously expressed and investigated for their FG degradation ability. The results showed that CotA laccase displayed the highest FG-degrading capacity among the three laccases, achieving 100% FG degradation at 37 °C and pH 7.0 in 1 h without the addition of a redox mediator. Moreover, in vitro and in vivo studies confirmed that the hepatotoxicity of FG was effectively eliminated after oxidative degradation by CotA laccase. Furthermore, the addition of CotA laccase could achieve 87% to 98% FG degradation in defatted CSM within 2 h. In conclusion, CotA laccase can be developed as an effective biocatalyst for the detoxification of FG in CSM.
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http://dx.doi.org/10.3390/foods13040566 | DOI Listing |
Chemosphere
January 2025
Department of Life Science and Biochemical Engineering, Graduate School, SunMoon University, Asan, 31460, Republic of Korea; Genome-based Bio-IT Convergence Institute, Asan, 31460, Republic of Korea; Bio Big Data-based Chungnam Smart Clean Research Leader Training Program, SunMoon University, Asan, 31460, Republic of Korea; Department of Pharmaceutical Engineering and Biotechnology, SunMoon University, Asan, 31460, Republic of Korea. Electronic address:
Laccases are of particular interest in addressing environmental challenges, such as the degradation of triphenylmethane (TPM) dyes, including crystal violet (CV) and Coomassie Brilliant Blue (CBB), which are commonly used in SDS-PAGE for protein visualization. However, these dyes present significant environmental concerns due to their resistance to degradation, which makes their removal from industrial wastewater a major challenge. To address this, the current study investigates the potential of a novel CotA laccase derived from Bacillus sp.
View Article and Find Full Text PDFJ Hazard Mater
December 2024
School of Resources and Environment, Northeast Agricultural University, Harbin, Heilongjiang 150030, PR China. Electronic address:
Facing the combined pollution of antibiotics and heavy metals caused by livestock excrement and industrial effluents, how to use microbial technology to remove these pollutants simultaneously is an important research topic in environmental remediation. In addition, quick separation of the bacteria-water after remediation is also an urgent problem. In this study, we gradually developed a dual-bacteria microbial treatment technology capable of removing Pb(Ⅱ), Cd(Ⅱ) and common antibiotics, as well as self-settling after treatment.
View Article and Find Full Text PDFFront Microbiol
November 2024
Department of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Cairo, Egypt.
Introduction: Laccases are blue-multicopper containing enzymes that are known to play a role in the bioconversion of recalcitrant compounds. Their role in free radical polymerization of aromatic compounds for their valorization remains underexplored. In this study, we used a pBAD plasmid containing a previously characterized CotA laccase gene (abbreviated as -Lacc) from strain ATCC 9945a to express this enzyme and explore its biotransformation/polymerization potential on β-naphthol.
View Article and Find Full Text PDFFoods
November 2024
College of Animal Science and Technology, China Agricultural University, Beijing 100193, China.
Aflatoxin M (AFM) in milk poses a significant threat to human health. This study examined the capacity of CotA laccase to oxidize AFM. The optimal conditions for the CotA laccase-catalyzed AFM oxidation were observed at pH 8.
View Article and Find Full Text PDFChembiochem
December 2024
Key Laboratory of Environmental and Applied Microbiology, Chengdu Institute of Biology, Chinese Academy of Sciences, Chengdu, P. R. China.
CotA is a bacterial multicopper oxidase, capable of oxidizing lots of substrates. In previous work, small size lignin phenol derivates were found to lie only in the partially covered part of pocket. However, big size substate would occupy the whole pocket to react.
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