Removal of Selected Azo Dyes and Phenolic Compounds via Tyrosinase Immobilized Magnetic Iron Oxide Silver Nanoparticles

Yavaşer, Rukiye; Uygun, Deniz Aktaş; Karagözler, Arife Alev

doi:10.1007/s10562-022-04087-z

Cited by 6 publications

(2 citation statements)

References 41 publications

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“…However, free enzyme-mediated degradation is not appropriate for industrial usage due to poor stability, recycling difficulty, high cost, and so on. [1][2][3][4] To some extent, these restrictions may be solved by the immobilization of enzymes on a solid support. 5,6 Immobilization of enzymes often decreases the complexity of the manufacturing process, enabling continuous operation and allowing for the use of more costly but more efficient enzymes due to reusability.…”

Section: Introductionmentioning

confidence: 99%

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Metal ion‐mediated immobilization of catalase on poly(ε‐caprolactone)/polyethyleneimine electrospun nanofibers

Çetin

2023

J of Applied Polymer Sci

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A common industrial byproduct known as hydrogen peroxide, which is an essential intermediate, is associated with oxidative damage to brain cells and a number of neurodegenerative disorders. Although catalases are enzymes capable of decomposing hydrogen peroxide into water and oxygen, the low stability of free enzymes limits their industrial use. In the current study, poly(ε‐caprolactone)/polyethyleneimine nanofibers were fabricated using the electrospinning process and catalase was subsequently immobilized via coordination of Cu2+ ions. The characterization of the catalase‐immobilized nanofibers and their catalytic activity for hydrogen peroxide decomposition was evaluated by comparing the free catalase. The studies conducted in the pH range of 5.0–8.5 revealed that the catalase‐immobilized nanofibers had their highest levels of enzyme activity at pH 7.0. When compared to free catalase, it was shown that the thermal stability and storage stability of catalase‐immobilized nanofibers were significantly improved. Catalase‐immobilized nanofibers showed significant reusability, where activity was maintained by around 60% after five repeating cycles. The findings showed that catalase‐immobilized PCL/PEI‐Cu2+ nanofibers had a high potential for various industrial applications as a substitute for the existing techniques.

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Section: Introductionmentioning

confidence: 99%

“…Enzymes are highly efficient, and environmentally friendly catalysts. However, free enzyme‐mediated degradation is not appropriate for industrial usage due to poor stability, recycling difficulty, high cost, and so on 1–4 . To some extent, these restrictions may be solved by the immobilization of enzymes on a solid support 5,6 .…”

Section: Introductionmentioning

confidence: 99%

Metal ion‐mediated immobilization of catalase on poly(ε‐caprolactone)/polyethyleneimine electrospun nanofibers

Çetin

2023

J of Applied Polymer Sci

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Biogenic Nanomaterials: Synthesis, Characterization and Its Potential in Dye Remediation

Kumar,

Mathur,

Singh

2023

Environmental Science and Engineering

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Tyrosinase enzyme purification and immobilization from Pseudomonas sp. EG22 using cellulose coated magnetic nanoparticles: characterization and application in melanin production

El-Aziz,

Faraag,

Ibrahim

et al. 2023

World J Microbiol Biotechnol

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Melanin is a brown-black pigment with significant roles in various biological processes. The tyrosinase enzyme catalyzes the conversion of tyrosine to melanin and has promising uses in the pharmaceutical and biotechnology sectors. This research aims to purify and immobilize the tyrosinase enzyme from Pseudomonas sp.EG22 using cellulose-coated magnetic nanoparticles. Various techniques were utilized to examine the synthesized nanoparticles, which exhibited a spherical shape with an average diameter of 12 nm and a negative surface potential of − 55.7 mV with a polydispersity index (PDI) of 0.260. Comparing the immobilized magnetic tyrosinase enzyme with the free enzyme, the study’s findings showed that the immobilized tyrosinase enzyme had optimal activity at a pH of 6 and a temperature of 35 °C, and its activity increased as the concentration of tyrosine increased. The study investigated the antibacterial and anticancer bioactivity of the enzyme’s melanin product and found that it exhibited potential antibacterial activity against a multi-drug resistant strain including S. aureus and E. coli. The produced melanin also demonstrated the potential to decrease cell survival and induce apoptosis in initiation cells.

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Removal of Selected Azo Dyes and Phenolic Compounds via Tyrosinase Immobilized Magnetic Iron Oxide Silver Nanoparticles

Cited by 6 publications

References 41 publications

Metal ion‐mediated immobilization of catalase on poly(ε‐caprolactone)/polyethyleneimine electrospun nanofibers

Metal ion‐mediated immobilization of catalase on poly(ε‐caprolactone)/polyethyleneimine electrospun nanofibers

Biogenic Nanomaterials: Synthesis, Characterization and Its Potential in Dye Remediation

Tyrosinase enzyme purification and immobilization from Pseudomonas sp. EG22 using cellulose coated magnetic nanoparticles: characterization and application in melanin production

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