Optimization and kinetic modeling of <i>Trametes maxima</i> IIPLC-32 laccase and application in recalcitrant dye decolorization

Suman, Sunil Kumar; Malhotra, Manisha; Khichi, Shailendra Singh; Ghosh, Sanjoy; Jain, Suman L.

doi:10.1039/d0nj05179a

Cited by 7 publications

(1 citation statement)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Various supports, including chitosan, sepiolite, silica, and magnetic NPs, were previously used for laccase immobilization [ 28 - 31 ]. Compared to other systems, the Cu metals-based encapsulation of laccases via metal-protein hybrids is beneficial to retain better residual activity due to the presence of Cu as an active center in laccase [ 16 , 23 , 32 ]. In addition, Cu-based hybrids also exhibit laccase-mimicking properties and are helpful in the degradation of phenolics [ 33 , 34 ].…”

Section: Introductionmentioning

confidence: 99%

Laccase Immobilization on Copper-Magnetic Nanoparticles for Efficient Bisphenol Degradation

Patel

Kalia

Lee

2022

J. Microbiol. Biotechnol.

View full text Add to dashboard Cite

Laccase activity is influenced by copper (Cu) as an inducer. In this study, laccase was immobilized on Cu and Cu-magnetic (Cu/Fe 2 O 4 ) nanoparticles (NPs) to improve enzyme stability and potential applications. The Cu/Fe 2 O 4 NPs functionally activated by 3-aminopropyltriethoxysilane and glutaraldehyde exhibited an immobilization yield and relative activity (RA) of 93.1 and 140%, respectively. Under optimized conditions, Cu/Fe 2 O 4 NPs showed high loading of laccase up to 285 mg/g of support and maximum RA of 140% at a pH 5.0 after 24 h of incubation (4°C). Immobilized laccase, as Cu/Fe 2 O 4 -laccase, had a higher optimum pH (4.0) and temperature (45°C) than those of a free enzyme. The pH and temperature profiles were significantly improved through immobilization. Cu/Fe 2 O 4 -laccase exhibited 25-fold higher thermal stability at 65°C and retained residual activity of 91.8% after 10 cycles of reuse. The degradation of bisphenols was 3.9-fold higher with Cu/Fe 2 O 4 -laccase than that with the free enzyme. To the best of our knowledge, Rhus vernicifera laccase immobilization on Cu or Cu/Fe 2 O 4 NPs has not yet been reported. This investigation revealed that laccase immobilization on Cu/Fe 2 O 4 NPs is desirable for efficient enzyme loading and high relative activity, with remarkable bisphenol A degradation potential.

show abstract

Section: Introductionmentioning

confidence: 99%

Laccase Immobilization on Copper-Magnetic Nanoparticles for Efficient Bisphenol Degradation

Patel

Kalia

Lee

2022

J. Microbiol. Biotechnol.

View full text Add to dashboard Cite

show abstract

Enhanced laccase production by mutagenized Myrothecium verrucaria using corn stover as a carbon source and its potential in the degradation of 2-chlorophen

Gou

Lü

Cui

et al. 2022

Bioprocess Biosyst Eng

View full text Add to dashboard Cite

Production, Purification, and Characterization of Recombinant Bhargavaea beijingensis Laccase for Potential Lignin Degradation and Dyes Decolorization

et al. 2023

View full text Add to dashboard Cite

Optimization and kinetic modeling of Trametes maxima IIPLC-32 laccase and application in recalcitrant dye decolorization

Abstract: Enhanced laccase production by the Trametes maxima fungus and its use for decolorization of the textile dye RBBR.

Cited by 7 publications

References 38 publications

Laccase Immobilization on Copper-Magnetic Nanoparticles for Efficient Bisphenol Degradation

Laccase Immobilization on Copper-Magnetic Nanoparticles for Efficient Bisphenol Degradation

Enhanced laccase production by mutagenized Myrothecium verrucaria using corn stover as a carbon source and its potential in the degradation of 2-chlorophen

Production, Purification, and Characterization of Recombinant Bhargavaea beijingensis Laccase for Potential Lignin Degradation and Dyes Decolorization

Contact Info

Product

Resources

About