Immobilization of horseradish peroxidase on Fe<sub>3</sub>O<sub>4</sub>/nanotubes composites for Biocatalysis-degradation of phenol

Zhang, Chuang; Cai, Xiulan

doi:10.1080/09276440.2018.1504265

Cited by 42 publications

(24 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This decreased activity was caused by the inactivation of the enzyme, which was induced by protein denaturation and high substrate concentrations [24]. Zhang and Cat [25] and Yu et al [26] demonstrated that the HRP immobilization on Fe3O4/nanotubes composites and amino-functionalized bacterial cellulose retained 65% and 70% of the original activity after 6 and 10 times, respectively.…”

Section: Resultsmentioning

confidence: 99%

Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

2020

View full text Add to dashboard Cite

Horseradish peroxidase (HRP) enzyme was effectively encapsulated onto an Fe3O4 nanoparticle–polymethyl methacrylate (PMMA) film via the casting method. The HRP was immobilized on the 0.5% Fe3O4Np–PMMA film and characterized by Fourier transform infrared spectroscopy and field emission scanning electron microscopy. Moreover, the reusability, thermal stability, optimum pH, optimum temperature, the influence of metal ions, and the effects of detergent and organic solvent were investigated. After optimizing the immobilization conditions, the highest efficiency of the immobilized enzyme was 88.4% using 0.5% Fe3O4Np–PMMA. The reusability of the immobilized HRP activity was 78.5% of its initial activity after being repeatedly used for 10 cycles. When comparing the free and immobilized forms of the HRP enzyme, changes in the optimum temperature and optimum pH from 30 to 40 °C and 7.0 to 7.5, respectively, were observed. The Km and Vmax for the immobilized HRP were estimated to be 41 mM, 0.89 U/mL for guaiacol and 5.84 mM, 0.66 U/mL for H2O2, respectively. The high stability of the immobilized HRP enzyme was obtained using metal ions, a high urea concentration, isopropanol, and Triton X-100. In conclusion, the applicability of immobilized HRP involves the removal of phenol in the presence of hydrogen peroxide, therefore, it could be a potential catalyst for the removal of wastewater aromatic pollutants.

show abstract

Section: Resultsmentioning

confidence: 99%

Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

2020

View full text Add to dashboard Cite

show abstract

“…After 6 consecutive reactions, the IHRP sustained 48% of initial activity. Previously, IHRPs on different supports showed above fifty percent of initial enzyme activity after five [41], six [4,5] or ten cycles [14]. The reuse number of immobilized enzymes was related with support material and the substrate of the enzyme.…”

Section: Reusabilitymentioning

confidence: 94%

“…Among them, TiO2 is quite special as a support because of its excellent resistance to pH and corrosion, superior mechanical strength, and outstanding antimicrobial performance [10,11]. Previously, HRP has been immobilized on colloidal Au modified ITO glass support [12], colloid/cysteamine-modified gold electrode [13], on Fe3O4/nanotubes composites by APTES [5], cubic mesoporous silicate (SBA-16) [14], modified acrylonitrile copolymer membrane [15], kaolin [16], mesoporous activated carbon [17], wool [18], chitosan crosslinked with cyanuric chloride [6], acrylic polymer activated by cyanuric chloride [19], bacterial cellulose [20], magnetic composite microsphere containing polyethylene glycol [21], multi-walled carbon nanotubes (MWCNTs) buckypaper/polyvinyl alcohol composite membrane [22].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Optimization of the Immobilization Conditions of Horseradish Peroxidase on TiO2-COOH nanoparticles by Box-Behnken Design

Şahin

2019

Süleyman Demirel Üniversitesi Fen Bilimleri Enstitüsü Dergisi

View full text Add to dashboard Cite

In this study, TiO2 nanoparticles were prepared and-COOH functionalized with 3-(3,4-dihydroxyphenyl) propionic acid. The characterization of nanoparticles was performed by FTIR, TEM, EDS and XRD. HRP was immobilized on those nanoparticles by EDC/NHS coupling reaction. The immobilization conditions of HRP including A: enzyme concentration (0.5-1.5 mg/mL), B: immobilization pH (4.0-8.0), C: immobilization temperature (4-50°C), D: immobilization time (1-20 h) were optimized by response surface methodology and Box-Behnken design. The optimized immobilization conditions were identified as 0.5 mg/mL HRP, at pH 5.5, 40 °C for 8 h for activity of immobilized HRP, 1.5 mg/mL HRP, at pH 4 and 18°C for 20 h for protein binding yield (%). At these optimum conditions, the experimental value for the activity of immobilized HRP was 80.39 U ± 1.06; protein binding yield was 94.25 ± 3.58%. Moreover, the optimum temperature and pH of free and immobilized enzyme were determined as 50°C and 4.0; 50°C and 3.5, respectively. The activity of the immobilized HRP sustained 52% of its initial activity after 10 days storage at 4°C. Furthermore, the immobilized HRP sustained 48% of its initial activity after 6 consecutive reactions.

show abstract

“…There have been several reviews on the role of immobilized enzymes in environmental applications, describing various types of biocatalytic systems based on oxidoreductases (laccase and peroxidase) and their use as catalysts in wastewater treatment. Some of them concern immobilized laccases [19, 20•, 21] and peroxidases [22][23][24] and their potential application to remediate pollutants. Others refer to methods of immobilization, the support matrices used, and the types of pollutants treated [8,[25][26][27].…”

Section: Introductionmentioning

confidence: 99%

Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment

Kołodziejczak-Radzimska

Nghiem

Jesionowski

2021

Curr Pollution Rep

View full text Add to dashboard Cite

Purpose of Review Untreated wastewater discharge can significantly and negatively impact the state of the environment. Rapid industrialization and economic development have directly contributed to land and water pollution resulting from the application of many chemicals such as organic dyes, pharmaceuticals, and industrial reagents. The removal of these chemicals before effluent discharge is crucial for environmental protection. This review aims to explore the importance of functionalized materials in the preparation of biocatalytic systems and consider their application in eliminating water pollutants. Recent Findings Wastewater treatment methods can be classified into three groups: (i) chemical (e.g., chemical oxidation and ozonation), (ii) physical (e.g., membrane separation and ion exchange), and (iii) biological processes. Biological treatment is the most widely used method due to its cost-effectiveness and eco-friendliness. In particular, the use of immobilized enzymes has recently become more attractive as a result of scientific progress in advanced material synthesis. The selection of an appropriate support plays an important role in the preparation of such biologically active systems. Recent studies have demonstrated the use of various materials for enzyme immobilization in the purification of water. Summary This review identifies and discusses different biocatalytic systems used in the enzymatic degradation of various water pollutants. Materials functionalized by specific groups can serve as good support matrices for enzyme immobilization, providing chemical and thermal stability to support catalytic reactions. Enzymatic biocatalysis converts the pollutants into simpler products, which are usually less toxic than their parents. Due to immobilization, the enzyme can be used over multiple cycles to reduce the cost of wastewater treatment. Future studies in this field should focus on developing new platforms for enzyme immobilization in order to improve degradation efficiency.

show abstract

Immobilization of horseradish peroxidase on Fe₃O₄/nanotubes composites for Biocatalysis-degradation of phenol

Cited by 42 publications

References 38 publications

Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

Optimization of the Immobilization Conditions of Horseradish Peroxidase on TiO2-COOH nanoparticles by Box-Behnken Design

Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment

Contact Info

Product

Resources

About

Immobilization of horseradish peroxidase on Fe3O4/nanotubes composites for Biocatalysis-degradation of phenol

Cited by 42 publications

References 38 publications

Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

Encapsulation of HRP Enzyme onto a Magnetic Fe3O4 Np–PMMA Film via Casting with Sustainable Biocatalytic Activity

Optimization of the Immobilization Conditions of Horseradish Peroxidase on TiO2-COOH nanoparticles by Box-Behnken Design

Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment

Contact Info

Product

Resources

About

Immobilization of horseradish peroxidase on Fe₃O₄/nanotubes composites for Biocatalysis-degradation of phenol