Surface functionalized natural inorganic nanorod for highly efficient cellulase immobilization

Yang, Chao; Mo, Haodao; Zang, Limin; Chen, Jian; Wang, Zhenqiang; Qiu, Jianhui

doi:10.1039/c6ra15659b

Cited by 20 publications

(11 citation statements)

References 38 publications

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“…Free cellulase produced 90.3 mg glucose/g wheat straw, whereas two immobilized cellulase systems provided 76.6 and 11.9 mg glucose/g wheat straw. 55 In a comparable study by Sańchez-Rami ́rez et al, the hydrolysis of microcrystalline cellulose by commercial cellulase in the free form or immobilized on chitosan-coated magnetic nanoparticles resulted in substrate conversions of about 68 and 45%, respectively. 56 In the present study, the Eud-IDA-Ni 2+ /EG5C-1 biocomposite could exist in a soluble state during the reaction process, thus providing high accessibility to the substrate, and achieving efficient hydrolysis of PASC (Figure S2).…”

Section: ■ Results and Discussionmentioning

confidence: 71%

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: ■ Results and Discussionmentioning

confidence: 71%

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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“…Therefore, for a practical use of cellulase, its stability and reusability should be enhanced. A practical way to the improvement of enzyme stability and reusability is immobilization of enzymes onto solid supports. − Among the various supports for immobilization of enzymes, − magnetic supports are more interesting because their magnetic properties allow us to separate them by using an external magnet. − This advantage of magnetic supports is highly desirable in large-scale applications where the separation of large amounts of immobilized enzyme does not need a troublesome filtration or centrifugation. ,, There are two conventional methods for enzyme immobilization: physical adsorption − and covalent binding. − The physical adsorption of enzyme onto the solid support provides an easy way for immobilization which rarely changes the structure of enzyme and therefore decreases the activity loss. , However, the physical linkage is not firm and the enzyme will easily detach from the support surface, so in this case the reusability of supported enzyme is poor. , In the second method, enzyme is attached to the surface of support by a covalent bond. The covalent binding of enzyme onto the support surface increases the stability and reusability of the enzyme; however, it may reduce the activity. ,,, Despite the loss of enzyme activity resulting from covalent binding, this method is still more suitable for industrial applications than physical immobilization, since the expensive cellulase must be reused several times. , …”

Section: Introductionmentioning

confidence: 99%

Covalent Immobilization of Cellulase Using Magnetic Poly(ionic liquid) Support: Improvement of the Enzyme Activity and Stability

Hosseini

Zohreh

Yaghoubi

et al. 2018

J. Agric. Food Chem.

110

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A magnetic nanocomposite was prepared by entrapment of FeO nanoparticles into the cross-linked ionic liquid/epoxy type polymer. The resulting support was used for covalent immobilization of cellulase through the reaction with epoxy groups. The ionic surface of the support improved the adsorption of enzyme, and a large amount of enzyme (106.1 mg/g) was loaded onto the support surface. The effect of the presence of ionic monomer and covalent binding of enzyme was also investigated. The structure of support was characterized by various instruments such as FT-IR, TGA, VSM, XRD, TEM, SEM, and DLS. The activity and stability of immobilized cellulase were investigated in the prepared support. The results showed that the ionic surface and covalent binding of enzyme onto the support improved the activity, thermal stability, and reusability of cellulase compared to free cellulase.

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“…Immobilization on a solid support can improve an enzyme’s stability and makes it easier to recover said enzyme from the medium and soluble substrate, as previously proven [ 10 , 11 ]. For a solid substrate, immobilization can also provide a way to improve the stability and reusability of enzymes.…”

Section: Introductionmentioning

confidence: 99%

Preparation of Chitosan/Magnetic Porous Biochar as Support for Cellulase Immobilization by Using Glutaraldehyde

Qiu

2020

Polymers

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In this work, porous biochar was obtained from sugarcane bagasse by alkali activation and pyrolysis and then magnetized with γ-Fe2O3 by calcination. After functionalization with chitosan and activation with glutaraldehyde, the as-prepared chitosan/magnetic porous biochar served as a support to immobilize cellulase by covalent bonds. The immobilization amount of cellulase was 80.5 mg cellulase/g support at pH 5 and 25 °C for 12 h of immobilization. To determine the enzymatic properties, 1% carboxymethyl cellulose sodium (CMC) (dissolved in 0.1 M buffer) was considered as a substrate for hydrolysis at different pH values (3–7) and temperatures (30–70 °C) for 30 min. The results showed that the optimum pH and temperature of the free and immobilized cellulase did not change, which were pH 4 and 60 °C, respectively. The immobilized cellulase had a relatively high activity recovery of 73.0%. However, it also exhibited a higher Michaelis–Menten constant (Km) value and a slower maximum reaction velocity (Vmax) value compared to the free enzyme. In the reusability assay, the immobilized cellulase showed initial glucose productivity of 330.9 mg glucose/g CMC and remained at 86.0% after 10 uses. In conclusion, the chitosan/magnetic porous biochar has great potential applications as a support for enzyme immobilization.

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Surface functionalized natural inorganic nanorod for highly efficient cellulase immobilization

Abstract: Immobilization of cellulase on attapulgite@chitosan nanocomposite support.

Cited by 20 publications

References 38 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

Covalent Immobilization of Cellulase Using Magnetic Poly(ionic liquid) Support: Improvement of the Enzyme Activity and Stability

Preparation of Chitosan/Magnetic Porous Biochar as Support for Cellulase Immobilization by Using Glutaraldehyde

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