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Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering

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A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Organic Chemistry".

Deadline for manuscript submissions: closed (31 March 2023) | Viewed by 18355

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Special Issue Editors

Prof. Dr. Yi Hu

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Guest Editor

State Key Laboratory of Materials-Oriented Chemical Engineering, School of Pharmaceutical Sciences, Nanjing Tech University, Nanjing 210009, China
Interests: industrial biocatalysis; green organic synthesis; enzyme engineering; synergistic catalysis of metal-enzyme
Special Issues, Collections and Topics in MDPI journals

Dr. Gang Xu

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Guest Editor

College of Chemical and Biological Engineering, Zhejiang University, Hangzhou 310027, China
Interests: biocatalysis; biotrans; chiral synthesis; enzymatic-cat; chemo-enzymatic cat
Special Issues, Collections and Topics in MDPI journals

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Dear Colleagues,

With the depletion of non-renewable resources and the increase in environmental pollution, organic reactions, which produce a lot of organic solvent consumption, are considered to be environmentally unfriendly. As a practical and sustainable alternative to traditional organic reactions, biocatalysis exhibits its extremely advantages in selectivity and efficiency. Many classic C-C and C-X bond formation reactions could be efficiently catalyzed by biocatalysts, and which have been widely used in the synthesis of fine chemicals such as pharmaceuticals and their intermediates, nutritional additives, cosmetics, etc. Various solvents have been developed and used as the medium of enzymatic reactions, and various immobilization materials and methods have been developed to improve the stability of enzymes. Moreover, the increasing demands for efficient and versatile synthetic methods, combined with powerful new discoveries and engineering tools, have prompted innovations in biocatalysis, especially the development of new enzymes for precise transformations or "molecular editing". As a result, the past decade has witnessed an impressive expansion of biocatalysis.

This Special Issue on "Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering"aims to be an open forum where researchers share their achievements on enzyme engineering and its applications in organic synthesis. Contributions to this issue, in the form of both original research and review articles, may cover the enhancement of catalytic performance of enzymes including immobilization, chemical modification, rational design and directed evolution, applications of biocatalysts in organic synthesis, biocatalytic promiscuity, development and utilizations of green solvents for enzymatic reactions, enzymatic-chemical methods for the synthesis fine chmicals, multi-enzyme synergistic catalysis, photo-enzyme synergistic catalysis, and others.

Prof. Dr. Yi Hu
Dr. Gang Xu
Guest Editors

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Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

enzyme engineering
biocatalytic promiscuity
enzyme immobilization
directed evolution
biocatalysis
enzymatic reactions

Related Special Issue

Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering–2nd Edition in Molecules (2 articles)

Published Papers (12 papers)

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Research

14 pages, 3880 KiB

Open AccessArticle

Semi-Rational Design of L-Isoleucine Dioxygenase Generated Its Activity for Aromatic Amino Acid Hydroxylation

by Jianhong An, Jiaojiao Guan and Yao Nie

Molecules 2023, 28(9), 3750; https://doi.org/10.3390/molecules28093750 - 27 Apr 2023

Cited by 1 | Viewed by 1314

Abstract

Fe (II)-and 2-ketoglutarate-dependent dioxygenases (Fe (II)/α-KG DOs) have been applied to catalyze hydroxylation of amino acids. However, the Fe (II)/α-KG DOs that have been developed and characterized are not sufficient. L-isoleucine dioxygenase (IDO) is an Fe (II)/α-KG DO that specifically catalyzes the formation of 4-hydroxyisoleucine (4-HIL) from L-isoleucine (L-Ile) and exhibits a substrate specificity toward L-aliphatic amino acids. To expand the substrate spectrum of IDO toward aromatic amino acids, in this study, we analyzed the regularity of the substrate spectrum of IDO using molecular dynamics (MD) simulation and found that the distance between Fe²⁺, C2 of α-KG and amino acid chain’s C4 may be critical for regulating the substrate specificity of the enzyme. The mutation sites (Y143, S153 and R227) were also subjected to single point saturation mutations based on polarity pockets and residue free energy contributions. It was found that Y143D, Y143I and S153A mutants exhibited catalytic L-phenylalanine activity, while Y143I, S153A, S153Q and S153Y exhibited catalytic L-homophenylalanine activity. Consequently, this study extended the substrate spectrum of IDO with aromatic amino acids and enhanced its application property. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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14 pages, 5179 KiB

Open AccessFeature PaperArticle

R97 at “Handlebar” Binding Mode in Active Pocket Plays an Important Role in Fe(II)/α-Ketoglutaric Acid-Dependent Dioxygenase cis-P3H-Mediated Selective Synthesis of (2S,3R)-3-Hydroxypipecolic Acid

by Jiaojiao Guan, Yilei Lu, Zixuan Dai, Songyin Zhao, Yan Xu and Yao Nie

Molecules 2023, 28(4), 1854; https://doi.org/10.3390/molecules28041854 - 15 Feb 2023

Cited by 1 | Viewed by 1345

Abstract

Pipecolic acid (Pip) and its derivative hydroxypipecolic acids, such as (2S,3R)-3-hydroxypipecolic acid (cis-3-L-HyPip), are components of many natural and synthetic bioactive molecules. Fe(II)/α-ketoglutaric acid (Fe(II)/2-OG)-dependent dioxygenases can catalyze the hydroxylation of pipecolic acid. However, the available enzymes with desired activity and selectivity are limited. Herein, we compare the possible candidates in the Fe(II)/2-OG-dependent dioxygenase family, and cis-P3H is selected for potentially catalyzing selective hydroxylation of L-Pip. cis-P3H was further engineered to increase its catalytic efficiency toward L-Pip. By analyzing the structural confirmation and residue composition in substrate-binding pocket, a “handlebar” mode of molecular interactions is proposed. Using molecular docking, virtual mutation analysis, and dynamic simulations, R97, E112, L57, and G282 were identified as the key residues for subsequent site-directed saturation mutagenesis of cis-P3H. Consequently, the variant R97M showed an increased catalytic efficiency toward L-Pip. In this study, the k_cat/K_m value of the positive mutant R97M was about 1.83-fold that of the wild type. The mutation R97M would break the salt bridge between R97 and L-Pip and weaken the positive-positive interaction between R97 and R95. Therefore, the force on the amino and carboxyl groups of L-Pip was lightly balanced, allowing the molecule to be stabilized in the active pocket. These results provide a potential way of improving cis-P3H catalytic activity through rational protein engineering. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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19 pages, 3155 KiB

Open AccessArticle

Improved Bioproduction of the Nylon 12 Monomer by Combining the Directed Evolution of P450 and Enhancing Heme Synthesis

by Jiaming Yu, Jiawei Ge, Hongwei Yu and Lidan Ye

Molecules 2023, 28(4), 1758; https://doi.org/10.3390/molecules28041758 - 13 Feb 2023

Viewed by 1932

Abstract

The nylon 12 (PA12) monomer ω-aminododecanoic acid (ω-AmDDA) could be synthesized from lauric acid (DDA) through multi-enzyme cascade transformation using engineered E. coli, with the P450 catalyzing terminal hydroxylation of DDA as a rate-limiting enzyme. Its activity is jointly determined by the heme domain and the reductase domain. To obtain a P450 mutant with higher activity, directed evolution was conducted using a colorimetric high-throughput screening (HTS) system with DDA as the real substrate. After two rounds of directed evolution, a positive double-site mutant (R14R/D629G) with 90.3% higher activity was obtained. Molecular docking analysis, kinetic parameter determination and protein electrophoresis suggested the improved soluble expression of P450 resulting from the synonymous mutation near the N-terminus and the shortened distance of the electron transfer between FMN and FAD caused by D629G mutation as the major reasons for activity improvement. The significantly increased k_cat and unchanged K_m provided further evidence for the increase in electron transfer efficiency. Considering the important role of heme in P450, its supply was strengthened by the metabolic engineering of the heme synthesis pathway. By combining P450-directed evolution and enhancing heme synthesis, 2.02 ± 0.03 g/L of ω-AmDDA was produced from 10 mM DDA, with a yield of 93.6%. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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12 pages, 1443 KiB

Open AccessArticle

Genetically Engineering Escherichia coli to Produce Xylitol from Corncob Hydrolysate without Lime Detoxification

by Xinsong Yuan, Jiyun Cao, Rui Wang, Yu Han, Jinmiao Zhu, Jianping Lin, Lirong Yang and Mianbin Wu

Molecules 2023, 28(4), 1550; https://doi.org/10.3390/molecules28041550 - 06 Feb 2023

Cited by 3 | Viewed by 1447

Abstract

Before fermentation with hemicellulosic hydrolysate as a substrate, it is generally necessary to detoxify the toxic substances that are harmful to microorganism growth. Cyclic AMP receptor protein (CRP) is a global regulator, and mutation of its key sites may have an important impact on E. coli virulence tolerance. Using corncob hydrolysate without ion-exchange or lime detoxification as the substrate, shake flask fermentation experiments showed that CRP mutant IS5-dG (I112L, T127G, A144T) produced 18.4 g/L of xylitol within 34 h, and the OD₆₀₀ was 9.7 at 24 h; these values were 41.5% and 21.3% higher than those of the starting strain, IS5-d, respectively. This mutant produced 82 g/L of xylitol from corncob hydrolysate without ion-exchange or lime detoxification during fed-batch fermentation in a 15-L bioreactor, with a productivity of 1.04 g/L/h; these values were 173% and 174% higher than the starting strain, respectively. To our knowledge, this is the highest xylitol concentration and productivity produced by microbial fermentation using completely non-detoxified hemicellulosic hydrolysate as the substrate to date. This study also showed that alkali neutralization, high temperature sterilization, and fermentation of the hydrolysate had important effects on the xylose loss rate and xylitol production. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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14 pages, 9664 KiB

Open AccessArticle

New Anti-Prelog Stereospecific Whole-Cell Biocatalyst for Asymmetric Reduction of Prochiral Ketones

by Min-Yu Wang, Shun-Ju Cai, Jia-Chun Lin, Xiao-Jun Ji and Zhi-Gang Zhang

Molecules 2023, 28(3), 1422; https://doi.org/10.3390/molecules28031422 - 02 Feb 2023

Viewed by 1348

Abstract

The biocatalytic asymmetric reduction of prochiral ketones for the production of enantiopure alcohols is highly desirable due to its inherent advantages over chemical methods. In this study, a new bacterial strain capable of transforming ketones to corresponding alcohols with high activity and excellent enantioselectivity was discovered in a soil sample. The strain was subsequently identified as Bacillus cereus TQ-2 based on its physiological characteristics and 16S rDNA sequence analysis. Under optimized reaction conditions, the resting cells of B. cereus TQ-2 converted acetophenone to enantioenriched (R)-1-phenylethanol with 99% enantiometric excess following anti-Prelog’s rule, which is scarce in biocatalytic ketone reduction. The optimum temperature for the cells was 30 °C, and considerable catalytic activity was observed over a broad pH range from 5.0 to 9.0. The cells showed enhanced catalytic activity in the presence of 15% (v/v) glycerol as a co-substrate. The catalytic activity can also be substantially improved by adding Ca²⁺ or K⁺ ions. Moreover, the B. cereus TQ-2 cell was highly active in reducing several structurally diverse ketones and aldehydes to form corresponding alcohols with good to excellent conversion. Our study provides a versatile whole-cell biocatalyst that can be used in the asymmetric reduction of ketones for the production of chiral alcohol, thereby expanding the biocatalytic toolbox for potential practical applications. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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12 pages, 2967 KiB

Open AccessArticle

Dual-Enzyme Cascade Composed of Chitosan Coated FeS₂ Nanozyme and Glucose Oxidase for Sensitive Glucose Detection

by Bowen Shen, Molan Qing, Liying Zhu, Yuxian Wang and Ling Jiang

Molecules 2023, 28(3), 1357; https://doi.org/10.3390/molecules28031357 - 31 Jan 2023

Cited by 5 | Viewed by 1657

Abstract

Immobilizing enzymes with nanozymes to catalyze cascade reactions overcomes many of the shortcomings of biological enzymes in industrial manufacturing. In the study, glucose oxidases were covalently bound to FeS₂ nanozymes as immobilization carriers while chitosan encapsulation increased the activity and stability of the immobilized enzymes. The immobilized enzymes exhibited a 10% greater increase in catalytic efficiency than the free enzymes while also being more stable and catalytically active in environments with an alkaline pH of 9.0 and a high temperature of 100 °C. Additionally, the FeS₂ nanozyme-driven double-enzyme cascade reaction showed high glucose selectivity, even in the presence of lactose, dopamine, and uric acid, with a limit of detection (LOD) (S/N = 3) as low as 1.9 × 10⁻⁶ M. This research demonstrates that nanozymes may be employed as ideal carriers for biological enzymes and that the nanozymes can catalyze cascade reactions together with natural enzymes, offering new insights into interactions between natural and synthetic biosystems. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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13 pages, 5274 KiB

Open AccessArticle

Preparation of Coupling Catalyst HamZIF-90@Pd@CALB with Tunable Hollow Structure for Efficient Dynamic Kinetic Resolution of 1-Phenylethylamine

by Pengcheng Li, Jingjing Zhu, Hongyu Zhang, Lan Wang, Shulin Wang, Mengting Zhang, Jianping Wu, Lirong Yang and Gang Xu

Molecules 2023, 28(3), 922; https://doi.org/10.3390/molecules28030922 - 17 Jan 2023

Cited by 1 | Viewed by 1447

Abstract

Chiral amines are essential components for many pharmaceuticals and agrochemicals. However, the difficulty in obtaining enantiomerically pure amines limits their application. In this study, hollow amorphous ZIF-90 (HamZIF-90) materials were prepared by template engraving, and chemical–enzyme coupling catalysts (HamZIF-90@Pd@CALB) were constructed for the chiral resolution of 1-phenylethylamine. Different from conventional materials, HamZIF-90 had tunable hollow structures by altering its central node zinc ion concentrations, and the embedded hydrogel template gave it more pore structures, which facilitated the loading of enzyme molecules and Pd nanoparticles (NPs). The establishment of the coupling catalysts shortened the mass transfer distance of the reactant molecules between the metal nanoparticles and the enzyme catalyst in the dynamic kinetic resolution (DKR) reaction, resulting in 98% conversion of 1-phenylethylamine and 93% selectivity of Sel.R-amide. The proposal of this idea provided a good idea for future tailor-made MOFs loaded with chemical and enzyme coupled catalyst. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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13 pages, 3527 KiB

Open AccessArticle

Magnetic Polyethyleneimine Nanoparticles Fabricated via Ionic Liquid as Bridging Agents for Laccase Immobilization and Its Application in Phenolic Pollutants Removal

by Runtang Liu, Wei Zhang, Shushu Wang, Huajin Xu and Yi Hu

Molecules 2022, 27(23), 8522; https://doi.org/10.3390/molecules27238522 - 03 Dec 2022

Cited by 8 | Viewed by 1219

Abstract

In this study, polyethyleneimine was combined with magnetic Fe₃O₄ nanoparticles through the bridging of carboxyl-functionalized ionic liquid, and laccase was loaded onto the carrier by Cu²⁺ chelation to achieve laccase immobilization (MCIL–PEI–Cu–lac). The carrier was characterized by Fourier transform infrared spectroscopy, scanning electron microscope, thermogravimetric analysis, X-ray diffraction analysis, magnetic hysteresis loop and so on. MCIL–PEI–Cu–lac has good immobilization ability; its loading and activity retention could reach 52.19 mg/g and 91.65%, respectively. Compared with free laccase, its thermal stability and storage stability have been significantly improved, as well. After 6 h of storage at 60 °C, 51.45% of the laccase activity could still be retained, and 81.13% of the laccase activity remained after 1 month of storage at 3 °C. In the pollutants removal test, the removal rate of 2,4-dichlorophenol (10 mg/L) by MCIL–PEI–Cu–lac could reach 100% within 10 h, and the removal efficiency could still be maintained 60.21% after repeated use for 8 times. In addition, MCIL–PEI–Cu–lac also has a good removal effect on other phenolic pollutants (such as bisphenol A, phenol, 4-chlorophenol, etc.). Research results indicated that an efficient strategy for laccase immobilization to biodegrade phenolic pollutants was developed. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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13 pages, 2997 KiB

Open AccessArticle

Lipase-Catalyzed Phospha-Michael Addition Reactions under Mild Conditions

by Yuelin Xu, Fengxi Li, Jinglin Ma, Jiapeng Li, Hanqing Xie, Chunyu Wang, Peng Chen and Lei Wang

Molecules 2022, 27(22), 7798; https://doi.org/10.3390/molecules27227798 - 12 Nov 2022

Cited by 4 | Viewed by 1615

Abstract

Organophosphorus compounds are the core structure of many active natural products. The synthesis of these compounds is generally achieved by metal catalysis requiring specifically functionalized substrates or harsh conditions. Herein, we disclose the phospha-Michael addition reaction of biphenyphosphine oxide with various substituted β-nitrostyrenes or benzylidene malononitriles. This biocatalytic strategy provides a direct route for the synthesis of C-P bonds with good functional group compatibility and simple and practical operation. Under the optimal conditions (styrene (0.5 mmol), biphenyphosphine oxide (0.5 mmol), Novozym 435 (300 U), and EtOH (1 mL)), lipase leads to the formation of organophosphorus compounds in yields up to 94% at room temperature. Furthermore, we confirm the role of the catalytic triad of lipase in this phospha-Michael addition reaction. This new biocatalytic system will have broad applications in organic synthesis. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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17 pages, 1900 KiB

Open AccessArticle

Efficient Synthesis of Key Chiral Intermediate in Painkillers (R)-1-[3,5-Bis(trifluoromethyl)phenyl]ethanamine by Bienzyme Cascade System with R-ω-Transaminase and Alcohol Dehydrogenase Functions

by Yuan Lu, Jinmei Wang, Haobo Xu, Chuyue Zhang, Pengpeng Cheng, Lihua Du, Lan Tang, Jinghua Li and Zhimin Ou

Molecules 2022, 27(21), 7331; https://doi.org/10.3390/molecules27217331 - 28 Oct 2022

Cited by 1 | Viewed by 1403

Abstract

(R)-1-[3,5-bis(trifluoromethyl)phenyl]ethanamine, a key chiral intermediate of selective tetrodotoxin-sensitive blockers, was efficiently synthesized by a bienzyme cascade system formed by with R-ω-transaminase (ATA117) and an alcohol dehydrogenase (ADH) co-expression system. Herein, we report that the use of ATA117 as the biocatalyst for the amination of 3,5-bistrifluoromethylacetophenone led to the highest efficiency in product performance (enantiomeric excess > 99.9%). Moreover, to further improve the product yield, ADH was introduced into the reaction system to promote an equilibrium shift. Additionally, bienzyme cascade system was constructed by five different expression systems, including two tandem expression recombinant plasmids (pETDuet-ATA117-ADH and pACYCDuet-ATA117-ADH) and three co-expressed dual-plasmids (pETDuet-ATA117/pET28a-ADH, pACYCDuet-ATA117/pET28a-ADH, and pACYCDuet-ATA117/pETDuet-ADH), utilizing recombinant engineered bacteria. Subsequent studies revealed that as compared with ATA117 single enzyme, the substrate handling capacity of BL21(DE3)/pETDuet-ATA117-ADH (0.25 g wet weight) developed for bienzyme cascade system was increased by 1.50 folds under the condition of 40 °C, 180 rpm, 0.1 M pH9 Tris-HCl for 24 h. To the best of our knowledge, ours is the first report demonstrating the production of (R)-1-[3,5-bis(trifluoromethyl)phenyl]ethanamine using a bienzyme cascade system, thus providing valuable insights into the biosynthesis of chiral amines. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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12 pages, 1890 KiB

Open AccessArticle

Ultrasound Plus Vacuum-System-Assisted Biocatalytic Synthesis of Octyl Cinnamate and Response Surface Methodology Optimization

by Ming-Fang Tsai, Shang-Ming Huang, Hsin-Yi Huang, Shuo-Wen Tsai, Chia-Hung Kuo and Chwen-Jen Shieh

Molecules 2022, 27(21), 7148; https://doi.org/10.3390/molecules27217148 - 22 Oct 2022

Cited by 1 | Viewed by 1122

Abstract

Cinnamic acid is one of the phenolic compounds that is isolated from cinnamon, or other natural plants, and has a wide range of physiological activities. However, the application of cinnamic acid is limited due to its poor solubility and low oral bioavailability. In this study, the feasibility of producing octyl cinnamate by ultrasonic assistance, combined with a rotary evaporation under vacuum, was studied using methyl cinnamate and octanol as the starting materials. A Box–Behnken design (BBD) was employed to evaluate the effects of the operation parameters, including reaction temperature (55–75 °C), reaction time (4–12 h), and ultrasonic power (90–150 W) on the production of octyl cinnamate. Meanwhile, the synthesis process was further optimized by the modeling response surface methodology (RSM). The data indicated that octyl cinnamate was efficiently synthesized from methyl cinnamate and octanol using the ultrasound plus vacuum system; further, this system was superior to the conventional method. According to the RSM model for the actual experiments, a reaction temperature of 74.6 °C, a reaction time of 11.1 h, and an ultrasound power of 150 W were determined to be the best conditions for the maximum molar conversion of octyl cinnamate (93.8%). In conclusion, the highly efficient synthesis of octyl cinnamate by a rotary evaporator with an ultrasound plus vacuum system was achieved via RSM optimization. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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14 pages, 4904 KiB

Open AccessArticle

Preparation and Characterization of Magnetic Metal–Organic Frameworks Functionalized by Ionic Liquid as Supports for Immobilization of Pancreatic Lipase

by Moju Li, Xusheng Dai, Aifeng Li, Qi Qi, Wenhui Wang, Jia Cao, Zhenting Jiang, Renmin Liu, Hongbo Suo and Lili Xu

Molecules 2022, 27(20), 6800; https://doi.org/10.3390/molecules27206800 - 11 Oct 2022

Cited by 3 | Viewed by 1374

Abstract

Enzymes are difficult to recycle, which limits their large-scale industrial applications. In this work, an ionic liquid-modified magnetic metal–organic framework composite, IL-Fe₃O₄@UiO-66-NH₂, was prepared and used as a support for enzyme immobilization. The properties of the support were characterized with X-ray powder diffraction (XRD), Fourier-transform infrared (FTIR) spectra, transmission electron microscopy (TEM), scanning electronic microscopy (SEM), and so on. The catalytic performance of the immobilized enzyme was also investigated in the hydrolysis reaction of glyceryl triacetate. Compared with soluble porcine pancreatic lipase (PPL), immobilized lipase (PPL-IL-Fe₃O₄@UiO-66-NH₂) had greater catalytic activity under reaction conditions. It also showed better thermal stability and anti-denaturant properties. The specific activity of PPL-IL-Fe₃O₄@UiO-66-NH₂ was 2.3 times higher than that of soluble PPL. After 10 repeated catalytic cycles, the residual activity of PPL-IL-Fe₃O₄@UiO-66-NH₂ reached 74.4%, which was higher than that of PPL-Fe₃O₄@UiO-66-NH₂ (62.3%). In addition, kinetic parameter tests revealed that PPL-IL-Fe₃O₄@UiO-66-NH₂ had a stronger affinity to the substrate and, thus, exhibited higher catalytic efficiency. The results demonstrated that Fe₃O₄@UiO-66-NH₂ modified by ionic liquids has great potential for immobilized enzymes. Full article

(This article belongs to the Special Issue Modern Trends of Biocatalysis in Organic Chemistry and Enzyme Engineering)

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