Horseradish peroxidase immobilized on the magnetic composite microspheres for high catalytic ability and operational stability

Xie, Xueqiao; Luo, Peng; Han, Juan; Chen, Tong; Wang, Yun; Cai, Yunfeng; Liu, Qian

doi:10.1016/j.enzmictec.2018.12.007

Cited by 30 publications

(17 citation statements)

References 48 publications

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“…According to literature the use of glutaraldehyde as a functionalizing agent of supports provides greater operational stability on immobilized biocatalysts [ 65 ]. The decreasing residual activity of the IBs in the subsequent cycles of reuse probably occurs due to the denaturation of the enzyme [ 66 ].…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

et al. 2020

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In the present work the radish (Raphanus sativus L.) was used as the low-cost alternative source of peroxidase. The enzyme was immobilized in different supports: coconut fiber (CF), calcium alginate microspheres (CAMs) and silica SBA-15/albumin hybrid (HB). Physical adsorption (PA) and covalent binding (CB) as immobilization techniques were evaluated. Immobilized biocatalysts (IBs) obtained were physicochemical and morphologically characterized by SEM, FTIR and TGA. Also, optimum pH/temperature and operational stability were determined. For all supports, the immobilization by covalent binding provided the higher immobilization efficiencies—immobilization yield (IY%) of 89.99 ± 0.38% and 77.74 ± 0.42% for HB and CF, respectively. For CAMs the activity recovery (AR) was of 11.83 ± 0.68%. All IBs showed optimum pH at 6.0. Regarding optimum temperature of the biocatalysts, HB-CB and CAM-CB maintained the original optimum temperature of the free enzyme (40 °C). HB-CB showed higher operational stability, maintaining around 65% of the initial activity after four consecutive cycles. SEM, FTIR and TGA results suggest the enzyme presence on the IBs. Radish peroxidase immobilized on HB support by covalent binding is promising in future biotechnological applications.

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Section: Resultsmentioning

confidence: 99%

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

et al. 2020

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“…30 Despite the progress on SF/Fe 3 O 4 magnetic materials, their application in enzyme immobilization and development of an efficient method to achieve high performances has a substantial demand. 31…”

Section: Introductionmentioning

confidence: 99%

Self-Assembled Regenerated Silk Fibroin Microsphere-Embedded Fe₃O₄ Magnetic Nanoparticles for Immobilization of Zymolyase

Xiao

2019

ACS Omega

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Cytoplasm of Saccharomyces cerevisiae yeast cells contains a significant amount of desired intracellular products for both industrial utility and academic research. To recover intracellular compounds, it is necessary to break the yeast cells with high efficiency, which, under certain circumstances, requires the use of the lytic enzyme zymolyase to completely digest the cell walls. A promising strategy for zymolyase immobilization on silk fibroin (SF) was developed. SF/Fe3O4 magnetic microspheres (MMs) were constructed by solvent (ethanol)-induced self-assembly of SF surrounding Fe3O4 magnetic nanoparticles (MNs), which were synthesized by a coprecipitation method. Zymolyase was covalently bonded on the surface of the SF/Fe3O4 MMs by a photochemical cross-linking method to produce robust biocatalysts of zymolyase/SF/Fe3O4. The chemical, magnetic, and morphological properties of the MM supports and the immobilized zymolyase were investigated. Enzymolysis results demonstrated that the immobilized zymolyase showed good activity and stability for digesting yeast cell walls, and the biocatalyst can be readily recycled through convenient magnetic separation for reuse. At the optimum pH = 7.5, the immobilized zymolyase maintained 84% of the activity of the free zymolyase and retained 41% of its initial activity after four times of reuse. At unfavorable acidic pH = 4, the immobilized zymolyase retained 81% of its initial activity, while the free zymolyase showed no significant activity. Consequently, the SF/Fe3O4 MMs exhibit superior performance in terms of immobilizing enzymes, which have a good prospect in the biological application.

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“…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%

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

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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.

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Horseradish peroxidase immobilized on the magnetic composite microspheres for high catalytic ability and operational stability

Cited by 30 publications

References 48 publications

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

Self-Assembled Regenerated Silk Fibroin Microsphere-Embedded Fe₃O₄ Magnetic Nanoparticles for Immobilization of Zymolyase

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

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Horseradish peroxidase immobilized on the magnetic composite microspheres for high catalytic ability and operational stability

Cited by 30 publications

References 48 publications

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

Self-Assembled Regenerated Silk Fibroin Microsphere-Embedded Fe3O4 Magnetic Nanoparticles for Immobilization of Zymolyase

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

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Self-Assembled Regenerated Silk Fibroin Microsphere-Embedded Fe₃O₄ Magnetic Nanoparticles for Immobilization of Zymolyase