Rational surface silane modification for immobilizing glucose oxidase

Tian, Feibao; Guo, Yi; Zhang, Yumei; Yuan, Qipeng; Liang, Hao

doi:10.1016/j.ijbiomac.2016.02.055

Cited by 9 publications

(11 citation statements)

References 24 publications

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“…Nanostructured carriers have high specific surface area [ 18 ], excellent dispersibility, and low mass transfer resistance, being considered as ideal materials for immobilizing enzymes [ 19 , 20 , 21 ]. To enhance enzymatic stability and activity, many nanomaterials have been used for immobilizing enzymes [ 22 ]. Compared with micro-scale carriers, nonporous nanoparticles are more flexible for reactors and rigid enough to withstand high pressure during their application, but they are quite fragile and can be frayed and hardened by dehydration or an intense crosslinking [ 23 ].…”

Section: Introductionmentioning

confidence: 99%

Co-Immobilization of Enzymes and Magnetic Nanoparticles by Metal-Nucleotide Hydrogelnanofibers for Improving Stability and Recycling

Li¹,

Jiang

Zhao

et al. 2017

Molecules

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In this paper we report a facile method for preparing co-immobilized enzyme and magnetic nanoparticles (MNPs) using metal coordinated hydrogel nanofibers. Candida rugosa lipase (CRL) was selected as guest protein. For good aqueous dispersity, low price and other unique properties, citric acid-modified magnetic iron oxide nanoparticles (CA-Fe3O4 NPs) have been widely used for immobilizing enzymes. As a result, the relative activity of CA-Fe3O4@Zn/AMP nanofiber-immobilized CRL increased by 8-fold at pH 10.0 and nearly 1-fold in a 50 °C water bath after 30 min, compared to free CRL. Moreover, the immobilized CRL had excellent long-term storage stability (nearly 80% releative activity after storage for 13 days). This work indicated that metal-nucleotide nanofibers could efficiently co-immobilize enzymes and MNPs simultaneously, and improve the stability of biocatalysts.

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Section: Introductionmentioning

confidence: 99%

Co-Immobilization of Enzymes and Magnetic Nanoparticles by Metal-Nucleotide Hydrogelnanofibers for Improving Stability and Recycling

Li¹,

Jiang

Zhao

et al. 2017

Molecules

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“…The bioactivity of enzymes would be mostly maintained because the modification by the EDC/NHS method was usually in a mild condition [10]. However, a molecular CRL could be modified by several molecules of silanes when adding different amounts of APTES into the reaction system.…”

Section: Resultsmentioning

confidence: 99%

“…Recently, much research has focused on using nanostructured materials for immobilisation [11]. The nanostructured materials are very special, which are ideal carriers for the enzyme, that can offer many advantages, such as large surface‐to‐volume ratio, high surface activity, and strong adsorption ability [10, 17]. Silica nanoparticles are typical representatives of nanostructured materials, and it can provide reactive groups on the surface after surface modification [18].…”

Section: Introductionmentioning

confidence: 99%

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Facile one‐pot synthesis of silica‐based lipase nanocatalysts for improving stability

Zhou

Sun

Jiang

et al. 2018

Micro & Nano Letters

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The inactivation of lipases caused by organic solvents, high temperature, extremely acidic and alkaline requires a high stability. In this work, a novel one-pot synthesis for the lipase immobilisation on silica nanoparticles was reported. The optimal amounts of (3-ammonia propyl) triethoxysilane (APTES) and ammonia were studied. The apparent K m value of the immobilised Candida rugosa lipase (CRL) was lower than that of free enzyme, showing affinity of the immobilised CRL to its substrate had increased. The results of stability test showed that the immobilised lipase was more stable than free enzyme at different temperatures and pH values. In particular, the immobilised CRL kept 96% activity at 90°C, while the free enzyme only remained 75% activity. Immobilised lipase had high catalytic efficiency, enhanced stability and recyclable usability compared to free enzymes, because of the cross-linking between the protein and the rigid carrier. Therefore, the immobilised method would be beneficial to improving the activity and stability of enzyme universally.

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“…Furthermore, the secondary structure of the lipase was more integrated into the cationic polymer. Therefore, surface modification with a cationic polymer would be beneficial to improving the activity and stability of the immobilized enzyme as well as increasing the loading amount (Cowan and Fernandez-Lafuente, 2011;Tian et al, 2016).…”

Section: Thermal Stabilitymentioning

confidence: 99%

Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method

Moreira

Oliveira

Júnior

et al. 2020

Front. Bioeng. Biotechnol.

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In this communication, it was evaluated the production of fatty acid ethyl ester (FAAE) from the free fatty acids of babassu oil catalyzed by lipase from Rhizomucor miehei (RML) immobilized on magnetic nanoparticles (MNP) coated with 3-aminopropyltriethoxysilane (APTES), Fe 3 O 4 @APTES-RML or RML-MNP for short. MNPs were prepared by co-precipitation coated with 3-aminopropyltriethoxysilane and used as a support to immobilize RML (immobilization yield: 94.7 ± 1.0%; biocatalyst activity: 341.3 ± 1.2 U p−NPB /g), which were also activated with glutaraldehyde and then used to immobilize RML (immobilization yield: 91.9 ± 0.2%; biocatalyst activity: 199.6 ± 3.5 U p−NPB /g). RML-MNP was characterized by X-Ray Powder Diffraction (XRPD), Fourier Transform-Infrared (FTIR) spectroscopy and Scanning Electron Microscope (SEM), proving the incorporation and immobilization of RML on the APTES matrix. In addition, the immobilized biocatalyst presented at 60 • C a half-life 16-19 times greater than that of the soluble lipase in the pH range 5-10. RML and RML-MNP showed higher activity at pH 7; the immobilized enzyme was more active than the free enzyme in the pH range (5-10) analyzed. For the production of fatty acid ethyl ester, under optimal conditions [40 • C, 6 h, 1:1 (FFAs/alcohol)] determined by the Taguchi method, it was possible to obtain conversion of 81.7 ± 0.7% using 5% of RML-MNP.

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Rational surface silane modification for immobilizing glucose oxidase

Cited by 9 publications

References 24 publications

Co-Immobilization of Enzymes and Magnetic Nanoparticles by Metal-Nucleotide Hydrogelnanofibers for Improving Stability and Recycling

Co-Immobilization of Enzymes and Magnetic Nanoparticles by Metal-Nucleotide Hydrogelnanofibers for Improving Stability and Recycling

Facile one‐pot synthesis of silica‐based lipase nanocatalysts for improving stability

Lipase From Rhizomucor miehei Immobilized on Magnetic Nanoparticles: Performance in Fatty Acid Ethyl Ester (FAEE) Optimized Production by the Taguchi Method

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