Immobilization of His-tagged proteins on NiO foams for recyclable enzymatic reactors

Rosado, Pedro C.; Meyrelles, Ricardo; Macatrão, M.; Justino, Marta C.; Gomes, G. G.; Montemor, M.F.; Alves, Marta M.; Justino, Gonçalo C.; Ribeiro, Ana P. C.; Shimizu, Karina

doi:10.1016/j.apsusc.2020.147848

Cited by 5 publications

(3 citation statements)

References 51 publications

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“…In recent decades, many efforts have been performed to develop affinity immobilization, especially metal affinity immobilization through coordination interaction between polyhistidine tags and metal ions that has attracted increasing interest. This strategy presents several advantages as follows: (1) the protection of the enzyme activity and conformation in the immobilization process, (2) coupling the immobilization and purification of the enzyme in one step, (3) high enzyme loading due to strong affinity linkage, and (4) the possibility of reuse of the supports. − Metal ions that are routinely used for affinity immobilization include Cu 2+ , Ni 2+ , Co 2+ , Zn 2+ , Mn 2+ , Fe 3+ , and Al 3+ , which are chelated by some functional groups from the support, e.g. , amines and carboxyl groups, and are then connected to the enzyme .…”

Section: Introductionmentioning

confidence: 99%

Metal Affinity Immobilization of the Processive Endoglucanase EG5C-1 from Bacillus subtilis on a Recyclable pH-Responsive Polymer

Pedroso

et al. 2021

ACS Sustainable Chem. Eng.

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Establishing a suitable immobilization strategy to improve the accessibility of immobilized cellulase for insoluble cellulose and subsequently recover the enzyme from the remaining substrate is crucial to promote the industrialization of biofuels. Here, using iminodiacetic acid (IDA) and Ni2+ ions, a novel metal-chelated copolymer of methacrylic acid and methyl methacrylate was prepared for the immobilization of His-tagged processive endoglucanase EG5C-1 via affinity interaction between polyhistidine tag and Ni2+. The optimum loading capacity of the functionalized polymer (Eud-IDA-Ni2+) for EG5C-1 was about 280 mg/g, where more than 80% of the activity was recovered. Immobilized EG5C-1 exhibited improved thermal and pH stability and better reusability than the free one, and after five cycles of usage, the hydrolysis productivity remained above 70% of the initial value. The Eud-IDA-Ni2+/EG5C-1 biocomposite displayed reversibly soluble–insoluble characteristics with pH change, which was in the soluble state during the enzyme reaction process but could be recovered in an insoluble form by lowering the pH after the reaction. Thus, the yield obtained from the hydrolysis of an insoluble phosphoric acid-swollen cellulose substrate was similar for the free and immobilized form of EG5C-1. Our combined results suggested that a metal-ion-chelated, pH-responsive polymer had the potential for His-tagged cellulase immobilization to improve both the operational efficiency and economic benefit of the cellulosic biorefinery industry.

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Section: Introductionmentioning

confidence: 99%

Metal Affinity Immobilization of the Processive Endoglucanase EG5C-1 from Bacillus subtilis on a Recyclable pH-Responsive Polymer

Pedroso

et al. 2021

ACS Sustainable Chem. Eng.

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“…prepared magnetic nanoparticles coated by carboxymethylated polyethyleneimine (CMPEI)‐Ni 2+ , which could selectively capture His‐tagged recombinant retinoid X receptor protein from cell lysate. Rosado et al [28] . used NiO foams as carrier for His‐tagged overexpressed proteins.…”

Section: Introductionmentioning

confidence: 99%

Selective Immobilization of His‐Tagged Phosphomannose Isomerase on Ni Chelated Nanoparticles with Good Reusability and Activity

et al. 2022

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Self‐stable precipitation polymerization was used to prepare an enzyme‐immobilized microsphere composite. Phosphomannose isomerase (PMI) with His‐tag was successfully immobilized on Ni2+ charged pyridine‐derived particles. The maximum amount of PMI immobilized on such particles was ∼184 mg/g. Compared with free enzyme, the activity of the immobilized enzymes was significantly improved. In addition, the immobilized enzymes showed a much better thermostability than free enzymes. At the same time, the immobilized enzymes can be reused for multiple reaction cycles. We observed that the enzyme activity did not decrease significantly after six cycles. We conclude that the pyridine‐derived particles can be used to selectively immobilize His‐tagged enzymes, which can couple the enzyme purification and catalysis steps and improve the efficiency of enzyme‐catalyzed industrial processes.

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“…Nickel oxide (NiO) is considered the prototype p-type oxide semiconductor [1,2] and combined with the reported values of its energy band gap in the range of 3.6-4.0 eV it is the most widely used p-type transparent conductive oxide. Due to its chemical stability and non-toxicity, NiO has found numerous applications in photo-bio-catalysis [3][4][5], sensing [6,7], microbatteries [8] and transparent optoelectronics such as smart windows [9], ultra-violet (UV) photodetectors [10] and photovoltaics (PVs). In the case of PVs, NiO has been used in conventional PVs and ultra-violet UV-PVs, in addition to perovskite PVs, in which it is used as a hole transport layer [11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Transparent All-Oxide Hybrid NiO:N/TiO2 Heterostructure for Optoelectronic Applications

et al. 2021

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Nickel oxide (NiO) is a p-type oxide and nitrogen is one of the dopants used for modifying its properties. Until now, nitrogen-doped NiO has shown inferior optical and electrical properties than those of pure NiO. In this work, we present nitrogen-doped NiO (NiO:N) thin films with enhanced properties compared to those of the undoped NiO thin film. The NiO:N films were grown at room temperature by sputtering using a plasma containing 50% Ar and 50% (O2 + N2) gases. The undoped NiO film was oxygen-rich, single-phase cubic NiO, having a transmittance of less than 20%. Upon doping with nitrogen, the films became more transparent (around 65%), had a wide direct band gap (up to 3.67 eV) and showed clear evidence of indirect band gap, 2.50–2.72 eV, depending on %(O2-N2) in plasma. The changes in the properties of the films such as structural disorder, energy band gap, Urbach states and resistivity were correlated with the incorporation of nitrogen in their structure. The optimum NiO:N film was used to form a diode with spin-coated, mesoporous on top of a compact, TiO2 film. The hybrid NiO:N/TiO2 heterojunction was transparent showing good output characteristics, as deduced using both I-V and Cheung’s methods, which were further improved upon thermal treatment. Transparent NiO:N films can be realized for all-oxide flexible optoelectronic devices.

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Immobilization of His-tagged proteins on NiO foams for recyclable enzymatic reactors

Cited by 5 publications

References 51 publications

Metal Affinity Immobilization of the Processive Endoglucanase EG5C-1 from Bacillus subtilis on a Recyclable pH-Responsive Polymer

Metal Affinity Immobilization of the Processive Endoglucanase EG5C-1 from Bacillus subtilis on a Recyclable pH-Responsive Polymer

Selective Immobilization of His‐Tagged Phosphomannose Isomerase on Ni Chelated Nanoparticles with Good Reusability and Activity

Transparent All-Oxide Hybrid NiO:N/TiO2 Heterostructure for Optoelectronic Applications

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