Facile Immobilization of Enzyme via Co-Electrospinning: A Simple Method for Enhancing Enzyme Reusability and Monitoring an Activity-Based Organic Semiconductor

Aldhahri, Musab; Almulaiky, Yaaser Q.; El‐Shishtawy, Reda M.; Al-Shawafi, Waleed M.; Alngadh, Ahmed; Maghrabi, Rayan

doi:10.1021/acsomega.8b00366

Cited by 20 publications

(13 citation statements)

References 36 publications

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Section: Electrospinningmentioning

confidence: 99%

“…Immobilization techniques have become a rational project subject due to the nature of enzymes and the functionality of immobilization [216][217][218]. The improvement and innovation in enzyme immobilization techniques made it possible to overcome some common limitations [216][217][218][219][220]. Electrospinning is a practical, simple, and highly efficient technological tool for synthesizing ultrafine fibers with diameters in the range of nanometers [216,219,221,222].…”

Section: Electrospinningmentioning

confidence: 99%

“…The improvement and innovation in enzyme immobilization techniques made it possible to overcome some common limitations [216][217][218][219][220]. Electrospinning is a practical, simple, and highly efficient technological tool for synthesizing ultrafine fibers with diameters in the range of nanometers [216,219,221,222]. The fundamental principle of this technology is based on the electrostatic forces for the production of nanofibers.…”

Section: Electrospinningmentioning

confidence: 99%

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Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization

Cavalcante

Sousa

et al. 2021

Catalysts

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The market for industrial enzymes has witnessed constant growth, which is currently around 7% a year, projected to reach $10.5 billion in 2024. Lipases are hydrolase enzymes naturally responsible for triglyceride hydrolysis. They are the most expansively used industrial biocatalysts, with wide application in a broad range of industries. However, these biocatalytic processes are usually limited by the low stability of the enzyme, the half-life time, and the processes required to solve these problems are complex and lack application feasibility at the industrial scale. Emerging technologies create new materials for enzyme carriers and sophisticate the well-known immobilization principles to produce more robust, eco-friendlier, and cheaper biocatalysts. Therefore, this review discusses the trending studies and industrial applications of the materials and protocols for lipase immobilization, analyzing their advantages and disadvantages. Finally, it summarizes the current challenges and potential alternatives for lipases at the industrial level.

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Section: Electrospinningmentioning

confidence: 99%

Section: Electrospinningmentioning

confidence: 99%

Section: Electrospinningmentioning

confidence: 99%

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Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization

Cavalcante

Sousa

et al. 2021

Catalysts

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“…A utilização da eletrofiação para produção de enzimas imobilizadas em mantas vem sendo estudada. Aldhahri et al Reportou que enzima α-amilase e substrato Alq3 foram eletrofiados juntamente com o polímero de carbotano em etanol por meio da técnica de co-electrosppining utilizando as seguintes condições: 19,5 kV de tensão, 15 cm de distância e fluxo de 0,9 mL.h -1 (ALDHAHRI et al, 2018). Após 10 ciclos a enzima apresentou 30% da atividade inicial.…”

Section: Amostraunclassified

“…A partir do exposto, faz-se necessária uma investigação mais aprofundada para examinar a influência da voltagem na atividade enzimática nas condições de eletrofiação, tendo em vista os relatos de sucesso usando voltagens inferiores à usada no presente estudo HSIEH, 2008;ALDHAHRI et al, 2018), assim como aplicação do mat contendo a enzima livre de suporte, para aumentar a superfície exposta ao substrato.…”

Section: Amostraunclassified

Ésteres de celulose: síntese, propriedades e preparação de mantas e esferas visando aplicações em imobilização de lipase

Polez¹

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The aim of the present study was the esterification of cotton linter cellulose in homogeneous medium, using as solvent system lithium chloride/N,N-dimethylacetamide (LiCl/DMAc), and hexanoic anhydride or benzoyl chloride as esterifying agents. Cotton linter cellulose was used because it is a fast-growing source and is considered the highest purity cellulose isolated from plant sources. The synthesis of cellulose esters (hexanoate, benzoate as well as mixed esters, cellulose hexanoate-benzoate) aimed to obtain different average degrees of substitution (DS = 1, 2 and 3) by adjusting the Molesterifying agent/ MolOH of AGU ratio. The obtained cellulose esters (characterized by FTIR, 1 H NMR, and TGA) were used as starting materials in the preparation of mats and spheres, which corresponded to a second goal of the study. Cellulose hexanoate mats were obtained by electrospinning technique from tetrahydrofuran/N,N-dimethylacetamide (THF/DMAc) solutions, and cellulose benzoate and hexanoate benzoate mats were prepared from trifluoroacetic acid (TFA) solutions. Electrospinning resulted in ultrathin fiber networks (> 100 nm) over a wide diameter range by varying the experimental conditions such as polymeric solution flow rate (5.5, 15.5 and 45.5 μL.min-1), distance (5, 10, 15 and 25 cm), applied voltage between needle and collector (10, 15, 20 and 25 kV) and polymeric solution concentration (7, 9, 11, 13 and 15%). When evaluating SEM micrographs, it was observed that a smaller injection flow favored the formation of ultrathin fibers up to 150 nm. The spheres were prepared by dripping a solution of cellulose ester and acetone in non-solvent (water or methanol). The spheres obtained in water had slightly larger diameters and less rough surface when compared to spheres obtained in methanol. Mats and spheres of cellulose esters, selected from the results of the respective characterizations, were used as supports for immobilization of Pseudomonas fluorescens lipases (PFL) by encapsulation and subsequently applied to the enzymatic kinetic resolution of racemic hydrochlorins by reaction with vinyl acetate catalyzed by immobilized lipase, this step is the third goal of this study. The kinetic resolution was analyzed by Gas Chromatography coupled to a flame ionization detector (GC-FID) to determine the reaction parameters. The nonimmobilized reference lipase showed moderate conversion (c = 34%), excellent enantiomeric purity (eep = 98%) and excellent enantiomeric ratio (E = 212). Lipase immobilized in mats did not show catalytic activity, probably due to the voltage applied during electroporation, which may have inactivated the enzymes, and/or the application of the blankets on support, which may have impaired enzyme access. For Hex 12 beads (15% LPF) obtained using water as a counter solvent, the results were promising, superior conversion after 120h reaction (c = 40%) and 94% enantiomeric purity. By reusing the spheres in a second cycle, a 24% reduction in the reaction conversion rate was observed.

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

et al. 2020

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Facile Immobilization of Enzyme via Co-Electrospinning: A Simple Method for Enhancing Enzyme Reusability and Monitoring an Activity-Based Organic Semiconductor

Cited by 20 publications

References 36 publications

Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization

Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization

Ésteres de celulose: síntese, propriedades e preparação de mantas e esferas visando aplicações em imobilização de lipase

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

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