Ultra-Thin 2D CuO Nanosheet for HRP Immobilization Supported by Encapsulation in a Polymer Matrix: Characterization and Dye Degradation

Aldhahri, Musab; Almulaiky, Yaaser Q.; El‐Shishtawy, Reda M.; Al-Shawafi, Waleed M.; Salah, Numan; Alshahrie, Ahmed; Alzahrani, Hassan A. H.

doi:10.1007/s10562-020-03289-7

Cited by 43 publications

(20 citation statements)

References 58 publications

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“…Recently, various immobilization strategies were developed to enhance enzyme stability and reuse for continuous operations. − Among them, nanoparticle-supported enzymes, especially those synthesized in a molecularly oriented manner, have shown great promise. − Through controlling the orientation of enzymes on supports, site-specific immobilization could minimize adverse enzyme–carrier interactions and maximize active-site accessibility . Consequently, without compromising the activity, the performance of immobilized enzymes can be improved, such as their activity, enzyme stability, and resistance to chemicals or inhibitors. − This further promoted the wide use of enzymes in industries. − More significantly, site-specific immobilization may become more desired when complicated reaction conditions are involved. The lipase-catalyzed transesterification reaction such as biodiesel production is a typical example. , The reaction involves two substrates and a non-aqueous/biphasic reaction medium; improper orientation may hinder the opening of the lid and partially block the active sites.…”

Section: Introductionmentioning

confidence: 99%

Site-Specific and Covalent Immobilization of Lipase on Natural Polyphenol-Modified Magnetic Nanoparticles for Effective Biodiesel Production

Tang

Zhang

et al. 2022

ACS Sustainable Chem. Eng.

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Site-specific and covalent attachment is the most desirable immobilization strategy, but classic methods typically require genetic engineering or complicated material fabrication, resulting in operational complexity and difficulty. Herein, a novel site-specific and covalent immobilization strategy based on accurately selected immobilization sites on lipase was developed. Specifically, computer-aided structural analysis of functional groups on lipase revealed that lysine residues with free amino groups were far away from the catalytic pocket and lid, which were suitable to be chosen as the best immobilization sites to effectively reduce the loss in its activity. Meanwhile, natural polyphenol-modified magnetic nanoparticles could increase the active immobilization sites, and lipase can be immobilized on them directly via a covalent reaction. This site-specific immobilization system exhibited significant enhancement in activity recovery (71.3%) compared to random immobilization (42.5 and 55.9%). As expected, experimental and computational analyses revealed that tailor-made site-specific immobilization carriers were beneficial to maintain the native catalytic pocket conformation and enhance the rigidity of the immobilized lipase, which exhibited a higher biodiesel yield (92.1%) than free and randomly immobilized lipases. Besides, the site-specifically immobilized lipase could maintain as high as 75.3% biodiesel yield after eight cycles, making it an ideal nanocatalyst for efficient production of biodiesel. Overall, the site-specific enzyme immobilization technology can provide stable catalytic activity advantages over the randomly covalent immobilization strategy, which can significantly promote green manufacturing and sustainable production.

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Section: Introductionmentioning

confidence: 99%

Site-Specific and Covalent Immobilization of Lipase on Natural Polyphenol-Modified Magnetic Nanoparticles for Effective Biodiesel Production

Tang

Zhang

et al. 2022

ACS Sustainable Chem. Eng.

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“…Therefore, immobilization provides multiple advantages over free enzymes under identical reaction conditions, enhancing catalytic efficiency and enzyme recycling [20,21]. Catalase (EC 1.11.1.6) is a heme-containing metalloenzyme and is regarded as one of the most common enzymes in plant and animal tissues.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Catalase on Chitosan/ZnO and Chitosan/ZnO/Fe2O3 Nanocomposites: A Comparative Study

2021

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The strong catalytic performance, eco-friendly reaction systems, and selectivity of enzyme-based biocatalysts are extremely interesting. Immobilization has been shown to be a good way to improve enzyme stability and recyclability. Chitosan-incorporated metal oxides, among other support matrices, are an intriguing class of support matrices for the immobilization of various enzymes. Herein, the cross-linked chitosan/zinc oxide nanocomposite (CS/ZnO) was synthesized and further improved by adding iron oxide (Fe2O3) nanoparticles. The final cross-linked CS/ZnO/Fe2O3 nanocomposite was used as an immobilized support for catalase and is characterized by SEM, EDS, and FTIR. The nanocomposite CS/ZnO/Fe2O3 enhanced the biocompatibility and immobilized system properties. CS/ZnO/Fe2O3 achieved a higher immobilization yield (84.32%) than CS/ZnO (37%). After 10 repeated cycles, the remaining immobilized catalase activity of CS/ZnO and CS/ZnO/Fe2O3 was 14% and 45%, respectively. After 60 days of storage at 4 °C, the remaining activity of immobilized enzyme onto CS/ZnO and CS/ZnO/Fe2O3 was found to be 32% and 47% of its initial activity. The optimum temperature was noticed to be broad at 25–30 °C for the immobilized enzyme and 25 °C for the free enzyme. Compared with the free enzyme optimum pH (7.0), the optimum pH for the immobilized enzyme was 7.5. The Km and Vmax values for the free and immobilized enzyme on CS/ZnO, and the immobilized enzyme on CS/ZnO/Fe2O3, were found to be 91.28, 225.17, and 221.59 mM, and 10.45, 15.87, and 19.92 µmole ml−1, respectively. Catalase immobilization on CS/ZnO and CS/ZnO/Fe2O3 offers better stability than free catalase due to the enzyme’s half-life. The half-life of immobilized catalase on CS/ZnO/Fe2O3 was between 31.5 and 693.2 min.

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“…12 Aldhahri and co-workers reported immobilization of horseradish peroxidase (HRP) on a copper oxide nanosheet (CuONS), and the recovered HRP enzymatic activity was 72.8%. 13 Thus, the treated enzyme, with a higher catalytic activity than the free enzyme, remains extremely attractive for many researchers. Moreover, engineering rational structuration could boost the catalytic activity of natural enzymes and also strengthen their resistance to temperature, acid, and alkali.…”

Section: Introductionmentioning

confidence: 99%

“…For instance, Li and co-workers immobilized laccase on the surface of Fe 3 O 4 @C-Cu 2+ nanoparticles for biodegradation of dyes; however, 82.3% of the laccase enzymatic activity was reserved . Aldhahri and co-workers reported immobilization of horseradish peroxidase (HRP) on a copper oxide nanosheet (CuONS), and the recovered HRP enzymatic activity was 72.8% . Thus, the treated enzyme, with a higher catalytic activity than the free enzyme, remains extremely attractive for many researchers.…”

Section: Introductionmentioning

confidence: 99%

Photoenzymatic Activity of Artificial–Natural Bienzyme Applied in Biodegradation of Methylene Blue and Accelerating Polymerization of Dopamine

Zheng

Cui

Zhou

et al. 2021

ACS Appl. Mater. Interfaces

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Enzymes as biocatalysts have attracted extensive attention. In addition to immobilizing or encapsulating various enzymes for combating the easy loss of enzymatic activity, strengthening the enzymatic activity upon light irradiation is a challenge. To the best of our knowledge, the work of spatiotemporally modulating the catalytic activity of artificialnatural bienzymes with a near-infrared light irradiation has not been reported. Inspired by immobilized enzymes and nanozymes, herein a platinum nanozyme was synthesized; subsequently, the platinum nanozyme was grafted on the body of laccase, thus successfully obtaining the artificial-natural bienzyme. The threedimensional structure of the artificial-natural bienzyme was greatly different from that of the immobilized enzyme or the encapsulated enzyme. The platinum nanozyme possessed excellent laccase-like activity, which was 3.7 times higher than that of laccase. Meanwhile, the coordination between the platinum nanozyme and laccase was proved. Besides, the cascaded catalysis of artificialnatural bienzyme was verified with hydrogen peroxide as a mediator. The enzymatic activities of artificial-natural bienzyme with and without near-infrared light irradiation were, respectively, 46.2 and 29.5% higher than that of free laccase. Moreover, the reversible catalytic activity of the coupled enzyme could be manipulated with and without a near-infrared light at 808 nm. As a result, the degradation rates of methylene blue catalyzed by the coupled enzyme and the platinum nanozyme were higher than that of laccase. Furthermore, accelerating polymerization of the dopamine was also demonstrated. Briefly, this facile strategy may provide a universal approach to control the catalytic activity of other natural enzymes.

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Ultra-Thin 2D CuO Nanosheet for HRP Immobilization Supported by Encapsulation in a Polymer Matrix: Characterization and Dye Degradation

Cited by 43 publications

References 58 publications

Site-Specific and Covalent Immobilization of Lipase on Natural Polyphenol-Modified Magnetic Nanoparticles for Effective Biodiesel Production

Site-Specific and Covalent Immobilization of Lipase on Natural Polyphenol-Modified Magnetic Nanoparticles for Effective Biodiesel Production

Immobilization of Catalase on Chitosan/ZnO and Chitosan/ZnO/Fe2O3 Nanocomposites: A Comparative Study

Photoenzymatic Activity of Artificial–Natural Bienzyme Applied in Biodegradation of Methylene Blue and Accelerating Polymerization of Dopamine

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