An oxidoreductase enzyme, fungal laccase immobilized on zeolitic imidazolate frameworks for the biocatalytic degradation of an endocrine-disrupting chemical, dimethyl phthalate

Dlamini, Mbongiseni Lungelo; Lesaoana, Mahadi; Kotzé, Izak A.; Richards, Heidi

doi:10.1016/j.jece.2023.109810

Cited by 4 publications

(2 citation statements)

References 87 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Though the de novo method of encapsulating the enzyme in MOFs could increase its activity and stability, it might result in a slower rate of enzyme reaction due to less opportunity for the substrate to bind to the enzyme's active sites. [35].…”

Section: The De Novo Methodsmentioning

confidence: 99%

Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives

Yang,

Zhang

et al. 2023

Materials

View full text Add to dashboard Cite

Oxidoreductases are a wide class of enzymes that can catalyze biological oxidation and reduction reactions. Nowadays, oxidoreductases play a vital part in most bioenergetic metabolic pathways, which have important applications in biodegradation, bioremediation, environmental applications, as well as biosensors. However, free oxidoreductases are not stable and hard to be recycled. In addition, cofactors are needed in most oxidoreductases catalyze reactions, which are so expensive and unstable that it hinders their industrial applications. Enzyme immobilization is a feasible strategy that can overcome these problems. Recently, metal–organic frameworks (MOFs) have shown great potential as support materials for immobilizing enzymes due to their unique properties, such as high surface-area-to-volume ratio, chemical stability, functional designability, and tunable pore size. This review discussed the application of MOFs and their composites as immobilized carriers of oxidoreductase, as well as the application of MOFs as catalysts and immobilized carriers in redox reactions in the perspective of the function of MOFs materials. The paper also focuses on the potential of MOF carrier-based oxidoreductase immobilization for designing an enzyme cascade reaction system.

show abstract

Section: The De Novo Methodsmentioning

confidence: 99%

Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives

Yang,

Zhang

et al. 2023

Materials

View full text Add to dashboard Cite

show abstract

“…Laccase has broad application in the efficient degradation of various organic pollutants in the environment due to its outstanding characteristics, such as a broad substrate spectrum, molecular oxygen as the terminal electron acceptor, unique oxidation mechanism without the need for cofactors or peroxides, mild reaction conditions, and environmental friendliness [4,5]. Extensive research has shown that laccase can effectively degrade a variety of recalcitrant environmental pollutants, including industrial synthetic dyes [6,7], olefins [8,9], chlorophenols [10,11], polycyclic aromatic hydrocarbons [12,13], pesticides [14,15], and endocrine disruptors [16,17]. As a result, the ability of laccase to degrade various environmental pollutants has received increasing attention.…”

Section: Introductionmentioning

confidence: 99%

Effective Decolorization and Detoxification of Single and Mixed Dyes with Crude Laccase Preparation from a White-Rot Fungus Strain Pleurotus eryngii

Ge,

Deng,

Wang

et al. 2024

Molecules

View full text Add to dashboard Cite

To fully harness the potential of laccase in the efficient decolorization and detoxification of single and mixed dyes with diverse chemical structures, we carried out a systematic study on the decolorization and detoxification of single and mixed dyes using a crude laccase preparation obtained from a white-rot fungus strain, Pleurotus eryngii. The crude laccase preparation showed efficient decolorization of azo, anthraquinone, triphenylmethane, and indigo dyes, and the reaction rate constants followed the order Remazol Brilliant Blue R > Bromophenol blue > Indigo carmine > New Coccine > Reactive Blue 4 > Reactive Black 5 > Acid Orange 7 > Methyl green. This laccase preparation exhibited notable tolerance to SO42− salts such as MnSO4, MgSO4, ZnSO4, Na2SO4, K2SO4, and CdSO4 during the decolorization of various types of dyes, but was significantly inhibited by Cl− salts. Additionally, this laccase preparation demonstrated strong tolerance to some organic solvents such as glycerol, ethylene glycol, propanediol, and butanediol. The crude laccase preparation demonstrated the efficient decolorization of dye mixtures, including azo + azo, azo + anthraquinone, azo + triphenylmethane, anthraquinone + indigo, anthraquinone + triphenylmethane, and indigo + triphenylmethane dyes. The decolorization kinetics of mixed dyes provided preliminary insight into the interactions between dyes in the decolorization process of mixed dyes, and the underlying reasons and mechanisms were discussed. Importantly, the crude laccase from Pleurotus eryngii showed efficient repeated-batch decolorization of single-, two-, and four-dye mixtures. This crude laccase demonstrated high stability and reusability in repeated-batch decolorization. Furthermore, this crude laccase was efficient in the detoxification of different types of single dyes and mixed dyes containing different types of dyes, and the phytotoxicity of decolorized dyes (single and mixed dyes) was significantly reduced. The crude laccase efficiently eliminated phytotoxicity associated with single and mixed dyes. Consequently, the crude laccase from Pleurotus eryngii offers significant potential for practical applications in the efficient decolorization and management of single and mixed dye pollutants with different chemical structures.

show abstract

Enhanced removal of dimethyl phthalate using heterogeneous UVC/VUV-Fenton amendment with Fe3O4@CM-β-CD/rGO catalyst: Efficiency, degradation mechanism and toxicity

Dong,

Li,

Rene

et al. 2024

Chemosphere

View full text Add to dashboard Cite

An oxidoreductase enzyme, fungal laccase immobilized on zeolitic imidazolate frameworks for the biocatalytic degradation of an endocrine-disrupting chemical, dimethyl phthalate

Cited by 4 publications

References 87 publications

Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives

Metal–Organic Framework for the Immobilization of Oxidoreductase Enzymes: Scopes and Perspectives

Effective Decolorization and Detoxification of Single and Mixed Dyes with Crude Laccase Preparation from a White-Rot Fungus Strain Pleurotus eryngii

Enhanced removal of dimethyl phthalate using heterogeneous UVC/VUV-Fenton amendment with Fe3O4@CM-β-CD/rGO catalyst: Efficiency, degradation mechanism and toxicity

Contact Info

Product

Resources

About