Editorial for Special Issue: Enzyme Immobilization and Its Applications

Fernández-Lafuente, Roberto

doi:10.3390/molecules24244619

Cited by 15 publications

(14 citation statements)

References 40 publications

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“…Immobilized enzymes may display enhanced biocatalytic properties [ 3 ]. Hence, after immobilization, it is important to assess the biocatalytic properties of the immobilized enzyme.…”

Section: Resultsmentioning

confidence: 99%

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Chitosan-Grafted Halloysite Nanotubes-Fe3O4 Composite for Laccase-Immobilization and Sulfamethoxazole-Degradation

et al. 2020

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A surface-engineered nano-support for enzyme laccase-immobilization was designed by grafting the surface of halloysite nanotubes (HNTs) with Fe3O4 nanoparticles and chitosan. Herein, HNTs were magnetized (HNTs-M) by a cost-effective reduction-precipitation method. The synthesized HNTs-M were grafted with 0.25%, 0.5%, 1%, and 2% chitosan (HNTs-M-chitosan), respectively. Synthesized HNTs-M-chitosan (0.25%), HNTs-M-chitosan (0.5%), HNTs-M-chitosan (1%) and HNTs-M-chitosan (2%) were linked with glutaraldehyde (GTA) for laccase immobilization. Among these formulations, HNTs-M-chitosan (1%) exhibited the highest laccase immobilization with 95.13% activity recovery and 100.12 mg/g of laccase loading. The optimized material was characterized thoroughly by scanning electron microscopy (SEM), high-resolution transmission electron microscopy (HR-TEM), X-ray powder diffraction (XRD), thermal gravimetric analysis (TGA), and vibrating sample magnetometer (VSM) analysis. The immobilized laccase (HNTs-M-chitosan (1%)-GTA-Laccase) exhibited higher pH, temperature, and storage stabilities. The HNTs-M-chitosan (1%)-GTA-Laccase possesses excellent reusability capabilities. At the end of 10 cycles of the reusability experiment, HNTs-M-chitosan (1%)-GTA-Laccase retained 59.88% of its initial activity. The immobilized laccase was utilized for redox-mediated degradation of sulfamethoxazole (SMX), resulting in 41%, 59%, and 62% degradation of SMX in the presence of 2,2′-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS), guaiacol (GUA), and syringaldehyde (SA), respectively. Repeated SMX degradation (57.10% after the sixth cycle) confirmed the potential of HNTs-M-chitosan (1%)-GTA-Laccase for environmental pollutant degradation. Thus, we successfully designed chitosan-based, rapidly separable super-magnetic nanotubes for efficacious enhancement of laccase biocatalysis, which can be applied as nano-supports for other enzymes.

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“…Immobilized enzymes may display enhanced biocatalytic properties [ 3 ]. Hence, after immobilization, it is important to assess the biocatalytic properties of the immobilized enzyme.…”

Section: Resultsmentioning

confidence: 99%

“…Biocatalyst enzymes have long been explored, due to their high specificity, catalytic power, and stereo-selectivity [ 2 ]. Enzyme immobilization processes gave us bio-based catalysts with enhanced properties for diverse applications [ 3 , 4 ]. Laccase is a capable biocatalyst for micro-pollutant removal [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Chitosan-Grafted Halloysite Nanotubes-Fe3O4 Composite for Laccase-Immobilization and Sulfamethoxazole-Degradation

et al. 2020

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“…In recent decades, great advances in the field of enzyme immobilization have made immobilized enzymes very promising catalysts in modern industry. However, enzyme immobilization (especially chemical immobilization) is still facing many challenges if analyzed in a global way, such as the overall cost of the supports, the ease of the immobilization protocols and protein conformation sensitivity [ 15 , 16 ]. Developing novel immobilization approaches to improve enzyme performance has been a permanent pursuit.…”

Section: Discussionmentioning

confidence: 99%

Constructing an Efficient Bacillus subtilis Spore Display by Using Cohesin−Dockerin Interactions

Wang

Jiang²,

Qian³

et al. 2021

Molecules

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Bacillus subtilis spore display has become a field of increasing interest in the past two decades. To improve the efficiency of B. subtilis spore display, its directed modification was performed based on the cellulosome architecture by introducing onto them divergent cohesin (Coh) modules that can specifically bind to the target enzyme bearing the matching dockerins (Doc). In this study, five different pairs of cohesins and dockerins, selected from four cellulolytic microbes, were examined for their capabilities in displaying a tetrameric enzyme β-galactosidase from Bacillus stearothermophilus IAM11001 on the surface of B. subtilis WB600 spores. Immunofluorescence microscopy, western blotting, dot blotting, and enzyme assay was applied to confirm its surface expression. All the resultant five Coh–Doc based spore display can hydrolyze o-nitrophenyl-β-D-galactopyranoside. Further, the optimized Coh–Doc based spore display exhibited the highest display efficiency. Overall, the results of current study may open new perspectives on the use of Coh–Doc interaction, which will find application in improving the efficiency of B. subtilis spore display.

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“…Enzyme immobilization, that was initialized as a way to solve the problem of enzyme solubility, is also an extremely useful methodology for modulating enzymatic features such as activity, selectivity, stability, etc. [9,32,[58][59][60][61][62][63][64][65][66][67][68][69][70]. As lipases are one of the most (if not the most) frequently used biocatalysts [71][72][73][74][75][76], it is not surprising to find a plethora of immobilization protocols described for these enzymes [77][78][79][80][81][82].…”

Section: Enzymatic Biocatalysismentioning

confidence: 99%

“…That is, even if the costs of the enzyme loss may be economically acceptable, the advantages of a proper enzyme immobilization may be too relevant to discard this powerful tool to improve the enzyme. This great potential of enzyme immobilization has promoted the continuous growth in the number of scientific publications in this apparently old-fashioned topic [64,358]. Immobilization may also alter lipase selectivity or specificity or produce enzyme purification [60][61][62][63][352][353][354][355][356] (Figures 17 and 18).…”

Section: Use Of Individually Immobilized Lipasesmentioning

confidence: 99%

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

et al. 2020

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Lipases are among the most utilized enzymes in biocatalysis. In many instances, the main reason for their use is their high specificity or selectivity. However, when full modification of a multifunctional and heterogeneous substrate is pursued, enzyme selectivity and specificity become a problem. This is the case of hydrolysis of oils and fats to produce free fatty acids or their alcoholysis to produce biodiesel, which can be considered cascade reactions. In these cases, to the original heterogeneity of the substrate, the presence of intermediate products, such as diglycerides or monoglycerides, can be an additional drawback. Using these heterogeneous substrates, enzyme specificity can promote that some substrates (initial substrates or intermediate products) may not be recognized as such (in the worst case scenario they may be acting as inhibitors) by the enzyme, causing yields and reaction rates to drop. To solve this situation, a mixture of lipases with different specificity, selectivity and differently affected by the reaction conditions can offer much better results than the use of a single lipase exhibiting a very high initial activity or even the best global reaction course. This mixture of lipases from different sources has been called “combilipases” and is becoming increasingly popular. They include the use of liquid lipase formulations or immobilized lipases. In some instances, the lipases have been coimmobilized. Some discussion is offered regarding the problems that this coimmobilization may give rise to, and some strategies to solve some of these problems are proposed. The use of combilipases in the future may be extended to other processes and enzymes.

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Editorial for Special Issue: Enzyme Immobilization and Its Applications

Abstract: Modern chemistry demands cleaner processes, for which more efficient catalysts are required [...]

Cited by 15 publications

References 40 publications

Chitosan-Grafted Halloysite Nanotubes-Fe3O4 Composite for Laccase-Immobilization and Sulfamethoxazole-Degradation

Chitosan-Grafted Halloysite Nanotubes-Fe3O4 Composite for Laccase-Immobilization and Sulfamethoxazole-Degradation

Constructing an Efficient Bacillus subtilis Spore Display by Using Cohesin−Dockerin Interactions

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

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