Enzyme Immobilized on Nanoporous Carbon Derived from Metal–Organic Framework: A New Support for Biodiesel Synthesis

Liu, Li Hao; Shih, Yung Han; Liu, Wan Ling; Lin, Chia Her; Huang, Hsi Ya

doi:10.1002/cssc.201700142

Cited by 41 publications

(11 citation statements)

References 57 publications

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“…This weak binding (compared to covalent binding) between enzymes and carrier made it inevitable for enzymes dropping off. However, the reusability results were relatively higher than the reported data (Table ), which was possibly attributed that there were some exposed oxygen active sites on MHNiO to strengthen the binding between enzyme and carrier through hydrogen binding.…”

Section: Resultscontrasting

confidence: 71%

“…However, to date, there are few reports on the use of MOF-derived oxide/carbon composites for enzyme immobilization. [29][30][31] In such study, no pore size control was conducted to match the size of enzyme to enhance its activity, and no interaction of the enzyme with substrate in the enzymatic reactor was investigated.…”

Section: Introductionmentioning

confidence: 99%

“…So, MOF‐derived oxide/carbon composites is considered as ideal candidates for enzyme immobilization owing to their unique properties, including large surface area, controllable porosity, and tunable composition and morphology. However, to date, there are few reports on the use of MOF‐derived oxide/carbon composites for enzyme immobilization . In such study, no pore size control was conducted to match the size of enzyme to enhance its activity, and no interaction of the enzyme with substrate in the enzymatic reactor was investigated.…”

Section: Introductionmentioning

confidence: 99%

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Enzyme Immobilization in MOF‐derived Porous NiO with Hierarchical Structure: An Efficient and Stable Enzymatic Reactor

et al. 2019

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MOF‐derived porous NiO with hierarchical structure (MHNiO) was prepared based on thermolysis of Ni metal organic framework (Ni‐MOF), which was used as carrier for the immobilization of horseradish peroxidase (HRP) and cytochrome C (Cyt c). The pore size of MHNiO was tuned as 11.8 nm to match the size of free enzyme so as to depress the aggregation of the enzymes in the pore. Meanwhile, the hierarchical structure allowed the substrates concentrated in the vicinity of the enzymes. The obtained enzymatic reactors exhibited better thermal stability, storage stability and reusability. For example, over 83 % of its original activity after 1 h incubation at 70 °C could be remained compared to 18.1 % or 38.4 % remained activity of free HRP and Cyt c, respectively; After 12 cycles of use, over 53 % of original catalytic activity of both the enzymatic reactor could be maintain. The enzymatic kinetic data (Km, Vmax, kcat) and thermodynamic data (Ka, ΔH, ΔS and ΔG) indicated that the improved catalytic performance was attributed to the affinity, selectivity and binding of enzyme to substrate. The two enzymatic reactors could be applied in the fast degradation of 2,4‐dichlorophenol and rifaximin in artificial wastewater, a complete degradation of 2 mg ⋅ mL−1 of 2,4‐dichlorophenol or 20 μg ⋅ mL−1 of rifaximin was achieved in only 20 min.

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Section: Resultscontrasting

confidence: 71%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Enzyme Immobilization in MOF‐derived Porous NiO with Hierarchical Structure: An Efficient and Stable Enzymatic Reactor

et al. 2019

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“…Burkholderia cepacia lipase (LBC) is of microbial origin and is widely used in several biotransformations due to its high selectivity and stability and tolerance to solvents frequently used in the reaction medium [ 4 ]. Transesterification using LBC has been reported by several studies and with different oils: soybean [ 5 ], palm [ 6 ], cotton seed [ 7 ], jatropha [ 8 ], sunflowers [ 9 ], and colza [ 10 ].…”

Section: Introductionmentioning

confidence: 99%

Lipase Immobilization on Silica Xerogel Treated with Protic Ionic Liquid and its Application in Biodiesel Production from Different Oils

Carvalho

Vidal

Barbosa

et al. 2018

IJMS

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Treated silica xerogel with protic ionic liquid (PIL) and bifunctional agents (glutaraldehyde and epichlorohydrin) is a novel support strategy used in the effective immobilization of lipase from Burkholderia cepacia (LBC) by covalent binding. As biocatalysts with the highest activity recovery yields, LBC immobilized by covalent binding with epichlorohydrin without (203%) and with PIL (250%), was assessed by the following the hydrolysis reaction of olive oil and characterized biochemically (Michaelis–Menten constant, optimum pH and temperature, and operational stability). Further, the potential transesterification activity for three substrates: sunflower, soybean, and colza oils, was also determined, achieving a conversion of ethyl esters between 70 and 98%. The supports and the immobilized lipase systems were characterized using Fourier transform infrared spectra (FTIR), scanning electron microscopy (SEM), elemental analysis, and thermogravimetric (TG) analysis.

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“…For instance, binding force is too weak to release enzyme from carriers, and the activity was always decreased by conformational changes or accidently cross-linking the active sites of enzyme (Jesionowski et al, 2014). Recently, some novel strategies for enzymatic immobilization were developed based on new immobilized supporters such as nanomaterials, magnetic materials, and chemical modified supporters (Yang et al, 2016;Zucca et al, 2016;Liu et al, 2017). Among them, a facile and rapid preparation of protein-inorganic hybrid nanoflowers was first accidently discovered by Ge et al (2012).…”

mentioning

confidence: 99%

Improving the Catalytic Performance of Pectate Lyase Through Pectate Lyase/Cu3(PO4)2 Hybrid Nanoflowers as an Immobilized Enzyme

Luo

et al. 2020

Front. Bioeng. Biotechnol.

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Pectate lyases (Pels) can be used in the textile industrial process for cotton scouring and ramie degumming, and its hydrolyzed products oligo galacturonic acid, are high-value added agricultural and health products. In our previous studies, an alkaline pectate lyase PEL168 mutant, PEL3, was obtained with improved specific activity and thermostability. Here, a facile and rapid method for preparing an immobilized PEL3-inorganic hybrid nanoflower was developed, as it could improve its biocatalytic performance. With 0.02 mg/mL (112.2 U/mL) PEL3 in PBS buffer, five different divalent ions, including Mn 2+ , Ca 2+ , Co 2+ , Zn 2+ , and Cu 2+ , were used as inorganic component. The results showed that PEL3/Cu 3 (PO 4) 2 hybrid nanoflowers presented the highest relative activity with 2.5-fold increase, compared to the free PEL3. X-ray diffraction analysis confirmed that the composition of PEL3/Cu 3 (PO 4) 2 hybrid nanoflowers were pectate lyase PEL3 and Cu 3 (PO 4) 2 •5H 2 O. The optimum temperature and pH of PEL3/Cu 3 (PO 4) 2 hybrid nanoflowers were ascertained to be 55 • C and pH 9.0, respectively, exhibiting subtle difference from the free PEL3. However, the PEL3/Cu 3 (PO 4) 2 hybrid nanoflowers maintained 33% residual activity after 24 h incubation at 55 • C, while the free PEL3 completely lost its activity after 18 h incubation at 55 • C. Furthermore, over 50% residual activity of the PEL3/Cu 3 (PO 4) 2 hybrid nanoflowers was remained, even after four times of repetitive utilization, demonstrating its promising stability for practical application.

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Enzyme Immobilized on Nanoporous Carbon Derived from Metal–Organic Framework: A New Support for Biodiesel Synthesis

Cited by 41 publications

References 57 publications

Enzyme Immobilization in MOF‐derived Porous NiO with Hierarchical Structure: An Efficient and Stable Enzymatic Reactor

Enzyme Immobilization in MOF‐derived Porous NiO with Hierarchical Structure: An Efficient and Stable Enzymatic Reactor

Lipase Immobilization on Silica Xerogel Treated with Protic Ionic Liquid and its Application in Biodiesel Production from Different Oils

Improving the Catalytic Performance of Pectate Lyase Through Pectate Lyase/Cu3(PO4)2 Hybrid Nanoflowers as an Immobilized Enzyme

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