Covalent organic frameworks as emerging host platforms for enzyme immobilization and robust biocatalysis – A review

Gan, JianSong; Bagheri, Ahmad Reza; Aramesh, Nahal; Gul, Ijaz; Franco, Marcelo; Almulaiky, Yaaser Q.; Bilal, Muhammad

doi:10.1016/j.ijbiomac.2020.12.002

Cited by 131 publications

(66 citation statements)

References 86 publications

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“…However, care should be taken with solubility of MOFs in the presence of various compounds such as amino acids, some organic acids or buffers that present high affinity for the MOF-metal, inducing leaching of the enzyme via MOF dissolution [156,157]. Covalent organic frameworks, only composed of light elements (H, C, B, N, and O) and covalent bonds, with higher stability than MOFs, can be alternatives as efficient matrices for enzymes [158].…”

Section: Metal-based Porous Matrixmentioning

confidence: 99%

From Enzyme Stability to Enzymatic Bioelectrode Stabilization Processes

et al. 2021

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Bioelectrocatalysis using redox enzymes appears as a sustainable way for biosensing, electricity production, or biosynthesis of fine products. Despite advances in the knowledge of parameters that drive the efficiency of enzymatic electrocatalysis, the weak stability of bioelectrodes prevents large scale development of bioelectrocatalysis. In this review, starting from the understanding of the parameters that drive protein instability, we will discuss the main strategies available to improve all enzyme stability, including use of chemicals, protein engineering and immobilization. Considering in a second step the additional requirements for use of redox enzymes, we will evaluate how far these general strategies can be applied to bioelectrocatalysis.

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Section: Metal-based Porous Matrixmentioning

confidence: 99%

From Enzyme Stability to Enzymatic Bioelectrode Stabilization Processes

et al. 2021

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“…The properties include biodegradability, biocompatibility, renewability, enhanced mechanical properties, and non-toxicity. Hence, these nanocomposite materials are of considerable attention [1][2][3][4][5]. Chitosan is an amino polysaccharide formed by chitin deacetylation and consists of randomly distributed units of (1,4)-linked-glucosamine and N-acetyl-d-glucosamine [6].…”

Section: Introductionmentioning

confidence: 99%

“…Hence, these nanocomposite materials are of considerable attention [1][2][3][4][5]. Chitosan is an amino polysaccharide formed by chitin deacetylation and consists of randomly distributed units of (1,4)-linked-glucosamine and N-acetyl-d-glucosamine [6]. At present, chitosan is a versatile, easily processable cationic biomaterial that can be widely used in medical, antibacterial dressings, tissue engineering and enzyme immobilization applications [7][8][9].…”

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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“…In addition, the performance of the immobilized multiple enzymes had not changed significantly after being reused five times. Therefore, the co-immobilization of multi-enzymes with cascade reaction had good application potential [ 22 , 23 , 24 ].…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, they should have a reasonable diffusion rate for substrates and products. Enzyme immobilization materials should also have good structural stability, and be able to maintain the original structure after repeated experiments to avoid leakage of the enzyme [ 22 ].…”

Section: Introductionmentioning

confidence: 99%

Preparation of ZIF@ADH/NAD-MSN/LDH Core Shell Nanocomposites for the Enhancement of Coenzyme Catalyzed Double Enzyme Cascade

et al. 2021

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The field of enzyme cascades in limited microscale or nanoscale environments has undergone a quick growth and attracted increasing interests in the field of rapid development of systems chemistry. In this study, alcohol dehydrogenase (ADH), lactate dehydrogenase (LDH), and mesoporous silica nanoparticles (MSN) immobilized nicotinamide adenine dinucleotide (NAD+) were successfully immobilized on the zeolitic imidazolate frameworks (ZIFs). This immobilized product was named ZIF@ADH/NAD-MSN/LDH, and the effect of the multi-enzyme cascade was studied by measuring the catalytic synthesis of lactic acid. The loading efficiency of the enzyme in the in-situ co-immobilization method reached 92.65%. The synthesis rate of lactic acid was increased to 70.10%, which was about 2.82 times that of the free enzyme under the optimal conditions (40 °C, pH = 8). Additionally, ZIF@ADH/NAD-MSN/LDH had experimental stability (71.67% relative activity after four experiments) and storage stability (93.45% relative activity after three weeks of storage at 4 °C; 76.89% relative activity after incubation in acetonitrile-aqueous solution for 1 h; 27.42% relative activity after incubation in 15% N, N-Dimethylformamide (DMF) solution for 1 h). In summary, in this paper, the cyclic regeneration of coenzymes was achieved, and the reaction efficiency of the multi-enzyme biocatalytic cascade was improved due to the reduction of substrate diffusion.

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Covalent organic frameworks as emerging host platforms for enzyme immobilization and robust biocatalysis – A review

Cited by 131 publications

References 86 publications

From Enzyme Stability to Enzymatic Bioelectrode Stabilization Processes

From Enzyme Stability to Enzymatic Bioelectrode Stabilization Processes

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

Preparation of ZIF@ADH/NAD-MSN/LDH Core Shell Nanocomposites for the Enhancement of Coenzyme Catalyzed Double Enzyme Cascade

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