Cibacron blue F3GA incorporated immobilized metal chelate affinity sorbent as a high efficient affinity immobilization materials for catalase enzyme

Esen, Elif; Öztürk, Simge; Uygun, Hilmiye Deniz Ertuğrul; Demir, M. Nalan

doi:10.1016/j.colsurfb.2021.111911

Cited by 3 publications

(2 citation statements)

References 39 publications

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“…[28][29][30] Since catalases have the ability to decompose H 2 O 2 into water and oxygen, they are often employed for the elimination of H 2 O 2 in widespread industries, such as food, bioremediation, textile, biomedical, pharmaceutical, agricultural, detergent, and biosensor technology. [31][32][33][34][35][36] Catalase is employed to remove H 2 O 2 which can inhibit bacterial cultures required in cheese production. 37 It is used with glucose oxidase to eliminate glucose from egg white before drying for use in the baking industry.…”

Section: Introductionmentioning

confidence: 99%

“…Catalases are heme‐containing metalloenzymes existing in plants and animal tissues, and each catalase protein having ferriporphyrin as a prosthetic group in each of its four subunits 28–30 . Since catalases have the ability to decompose H 2 O 2 into water and oxygen, they are often employed for the elimination of H 2 O 2 in widespread industries, such as food, bioremediation, textile, biomedical, pharmaceutical, agricultural, detergent, and biosensor technology 31–36 . Catalase is employed to remove H 2 O 2 which can inhibit bacterial cultures required in cheese production 37 .…”

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%

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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Biodegradation of environmental pollutants using catalase-based biocatalytic systems

Gan¹,

Ashraf

Bilal

et al. 2022

Environmental Research

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Development of New Affinity Material for Urease Purification: Synthesis and Characterization

Uygun,

Coşkun,

Öztürk

et al. 2024

Preprint

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Urease (urea amidohydrolase, E.C.3.5.1.5) is an enzyme that catalyzes the hydrolyzation of urea to form ammonium and carbon dioxide. This is an essential reaction in industrial and medical applications. Urease has a vital role in accelerating the hydrolysis of the urea in the agricultural gut, calculating the amount of urea in biological fluids, urine removal from artificial kidneys, and urea removal in wastewater and fruit juices. Purifying urease is also crucial for treating some diseases, such as gastrointestinal infection and hypertension. This research aimed at developing an environmentally friendly green biocomposite with high mechanical stability by suspension polymerization of chitosan (CTS), 2-hydroxyethyl methacrylate (HEMA), and N-methacryloyl- (L) -glutamic acid (MAGA) and to determine its optimum conditions for urease purification. The synthesized p (HEMA-MAGA) -CTS sorbent was investigated by FTIR, XPS, XRD, TGA, SEM, and particle size analysis. After the characterization, the parameters affecting the adsorption of urease, such as pH, sorbent amount, contact time, initial urease concentration, heat, and ionic strength, were optimized. In this study, equilibrium adsorption isotherms of urease on the synthesized affinity sorbent were examined and The Freundlich isotherm was found to provide a much better fit than the Langmuir and Dubinin-Radushkevich isotherms. The urease adsorbed on the p(HEMA-MAGA)-CTS affinity sorbent was desorbed in over 75% yield with 1.0 M NaSCN (pH 8.0) in 2 hours. The maximum adsorption capacity was found to be 9.47 mg mg-1 at pH 4.0 and 25°C. p(HEMA-MAGA)-CTS for urease purification was successfully developed.

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Cibacron blue F3GA incorporated immobilized metal chelate affinity sorbent as a high efficient affinity immobilization materials for catalase enzyme

Cited by 3 publications

References 39 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

Biodegradation of environmental pollutants using catalase-based biocatalytic systems

Development of New Affinity Material for Urease Purification: Synthesis and Characterization

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