Using concanavalinA as a spacer for immobilization of E. coli onto magnetic nanoparticles

Zhuang, Meng-Yao; Xu, Ming; Ling, Xiao-Min; Shen, Jiajia; Zhang, Ye-Wang

doi:10.1016/j.ijbiomac.2017.05.150

Cited by 25 publications

(13 citation statements)

References 46 publications

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“…The protons bind to the lone pair electrons on the amino N atom under acidic conditions. Whereas under pH 8, the hydrogen bonds on support will be broken in alkalinity conditions 4 , 5 . Based on the information, the optimal pH for immobilization was determined to be 7.0.…”

Section: Resultsmentioning

confidence: 99%

“…It is highly preferable that the carrier matrix that binds the enzyme can be produced reproducibly and does not disrupt the enzyme activity, because it has a great importance for technological performance and commercial success 1 – 3 . However, those materials also have some disadvantages (low mechanical strength and limited thermal stability) which can be improved using appropriate modification process 4 , 5 .…”

Section: Introductionmentioning

confidence: 99%

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Evaluation of MxOy/fucoidan hybrid system and their application in lipase immobilization process

Kołodziejczak-Radzimska

Bielejewski

Biadasz

et al. 2022

Sci Rep

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In this work, new MxOy/fucoidan hybrid systems were fabricated and applied in lipase immobilization. Magnesium (MgO) and zirconium (ZrO2) oxides were used as MxOy inorganic matrices. In the first step, the proposed oxides were functionalized with fucoidan from Fucus vesiculosus (Fuc). The obtained MgO/Fuc and ZrO2/Fuc hybrids were characterized by means of spectroscopic analyses, including Fourier transform infrared spectroscopy, X-ray photoelectron spectroscopy, and nuclear magnetic resonance. Additionally, thermogravimetric analysis was performed to determine the thermal stability of the hybrids. Based on the results, the mechanism of interaction between the oxide supports and fucoidan was also determined. Furthermore, the fabricated MxOy/fucoidan hybrid materials were used as supports for the immobilization of lipase from Aspergillus niger, and a model reaction (transformation of p-nitrophenyl palmitate to p-nitrophenol) was performed to determine the catalytic activity of the proposed biocatalytic system. In that reaction, the immobilized lipase exhibited high apparent and specific activity (145.5 U/gcatalyst and 1.58 U/mgenzyme for lipase immobilized on MgO/Fuc; 144.0 U/gcatalyst and 2.03 U/mgenzyme for lipase immobilized on ZrO2/Fuc). The immobilization efficiency was also confirmed using spectroscopic analyses (FTIR and XPS) and confocal microscopy.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Evaluation of MxOy/fucoidan hybrid system and their application in lipase immobilization process

Kołodziejczak-Radzimska

Bielejewski

Biadasz

et al. 2022

Sci Rep

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“…The properties of the carrier play an important role and normally the carrier should have large surface area [13][14][15]. Graphene with a lamellar structure has many industrial applications due to its unique physical and electronic properties [16].…”

Section: Introductionmentioning

confidence: 99%

Rapid Immobilization of Cellulase onto Graphene Oxide with a Hydrophobic Spacer

Gao

Wang

et al. 2018

Catalysts

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A rapid immobilization method for cellulase was developed. Functional graphene oxide was synthesized and grafted with hydrophobic spacer P-β-sulfuric acid ester ethyl sulfone aniline (SESA) though etherification and diazotization. The functionalized graphene oxide was characterized by Fourier-transform infrared spectroscopy and was used as the carrier for the immobilization of cellulase via covalent binding. The immobilization of cellulase was finished in a very short time (10 min) and very high immobilization yield and efficiency of above 90% were achieved after optimization. When compared with the free cellulase, thermal and operational stabilities of the immobilized cellulase were improved significantly. At 50 °C, the half-life of the immobilized cellulase (533 min) was six-fold higher than that of the free cellulase (89 min). Additionally, the affinity between immobilized cellulase (Km = 2.19 g L −1 ) and substrate was more favorable than that of free cellulase (Km = 3.84 g L −1 ), suggesting the immobilized cellulase has higher catalytic efficiency. The possible immobilization mechanism was proposed. The results strongly indicate that the immobilization is highly efficient and has great potential for the immobilization of other enzymes.

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“…The FT-IR spectra (Fig. 2a) indicated strong absorbance at 1653 and 1526 cm -1 , which is characteristic of the amide groups of the protein and was absent in the case of the free CuFe 2 O 4 hollow NPs [18,19] The presence of the amide group on the support confirmed the binding of the enzyme to the NPs. Further, the N-H bending vibration and stretching in the amide group in lipase appeared at 3297 cm -1 for both the free and immobilized lipase [20].…”

mentioning

confidence: 87%

Copper Ferrite Magnetic Nanoparticles for the Immobilization of Enzyme

et al. 2018

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In this study, novel, hollow superparamagnetic copper ferrite (CuFe 2 O 4 ) nanoparticles (NPs) were synthesized by a low-temperature hydrothermal method. The hollow magnetic spheres were characterized by field emission scanning electron microscopy and high resolution transmission electron microscopy to confirm their morphology and size. The hollow NPs were demonstrated as the support for biological materials by the immobilization of Thermomyces lanuginosus lipase on the inner and outer surfaces of the hollow spheres. The immobilization of the enzyme was confirmed by Fourier Transform Infra-red spectroscopy and confocal laser scanning microscopy. The immobilized enzyme was shown to have an immobilization efficiency of 84.5%, with approximately 176 mg g -1 of enzyme loading, for the hollow-NPs support. The immobilized enzyme exhibited high storage and temperature stability. The reusability of the immobilized lipase was more than 80% after 10 cycles of repeated use.

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Using concanavalinA as a spacer for immobilization of E. coli onto magnetic nanoparticles

Cited by 25 publications

References 46 publications

Evaluation of MxOy/fucoidan hybrid system and their application in lipase immobilization process

Evaluation of MxOy/fucoidan hybrid system and their application in lipase immobilization process

Rapid Immobilization of Cellulase onto Graphene Oxide with a Hydrophobic Spacer

Copper Ferrite Magnetic Nanoparticles for the Immobilization of Enzyme

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