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Keywords = biocatalytic reaction

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26 pages, 2278 KiB  
Review
Advances in Hydrodechlorination Technologies for Diclofenac Removal from Aqueous Systems
by Cristian Castillo, Jorge A. Mora and Maria H. Brijaldo
Molecules 2025, 30(16), 3332; https://doi.org/10.3390/molecules30163332 - 9 Aug 2025
Viewed by 485
Abstract
This review article describes the most recent studies carried out on the catalytic hydrodechlorination (HDC) of Diclofenac (DFC). In this context, the most commonly employed catalytic materials for the removal of DFC from aqueous matrices are reviewed, along with their main performance outcomes. [...] Read more.
This review article describes the most recent studies carried out on the catalytic hydrodechlorination (HDC) of Diclofenac (DFC). In this context, the most commonly employed catalytic materials for the removal of DFC from aqueous matrices are reviewed, along with their main performance outcomes. Various strategies for the HDC of DFC are discussed, including conventional approaches that rely on molecular hydrogen as the electron donor, as well as emerging alternatives based on biocatalytic and electrocatalytic processes. Additionally, the optimized reaction conditions for each catalytic system are discussed, along with relevant kinetic models and mechanistic insights that contribute to a deeper understanding of the HDC of DFC. Future perspectives on the use of catalysts with alternative properties for DFC removal via HDC are also discussed, aiming to highlight potential applications in wastewater treatment and the broader field of heterogeneous catalysis. Full article
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14 pages, 2022 KiB  
Article
Photo-Biocatalytic One-Pot Cascade Reaction for the Asymmetric Synthesis of Hydroxysulfone Compounds
by Xuebin Qiao, Qianqian Pei, Yihang Dai, Lei Wang and Zhi Wang
Catalysts 2025, 15(8), 733; https://doi.org/10.3390/catal15080733 - 1 Aug 2025
Viewed by 453
Abstract
Asymmetric synthesis of chiral hydroxysulfones, key pharmaceutical intermediates, is challenging. We report an efficient synthesis from readily available materials via a one-pot photo-biocatalytic cascade reaction in aqueous conditions, utilizing visible light as an energy source. This sustainable process achieves up to 84% yields [...] Read more.
Asymmetric synthesis of chiral hydroxysulfones, key pharmaceutical intermediates, is challenging. We report an efficient synthesis from readily available materials via a one-pot photo-biocatalytic cascade reaction in aqueous conditions, utilizing visible light as an energy source. This sustainable process achieves up to 84% yields and 99% ee. Engineered ketoreductase produces R-configured products with high conversion and enantioselectivity across diverse substrates. Molecular dynamics (MD) simulations explored enzyme–substrate interactions and their influence on reaction activity and stereoselectivity. Full article
(This article belongs to the Section Biocatalysis)
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25 pages, 6054 KiB  
Review
Recent Advances in Biocatalytic Dearomative Spirocyclization Reactions
by Xiaorui Chen, Changtong Zhu, Luyun Ji, Changmei Liu, Yan Zhang, Yijian Rao and Zhenbo Yuan
Catalysts 2025, 15(7), 673; https://doi.org/10.3390/catal15070673 - 10 Jul 2025
Viewed by 866
Abstract
Spirocyclic architectures, which feature two rings sharing a single atom, are common in natural products and exhibit beneficial biological and material properties. Due to the significance of these architectures, biocatalytic dearomative spirocyclization has recently emerged as a powerful approach for constructing three-dimensional spirocyclic [...] Read more.
Spirocyclic architectures, which feature two rings sharing a single atom, are common in natural products and exhibit beneficial biological and material properties. Due to the significance of these architectures, biocatalytic dearomative spirocyclization has recently emerged as a powerful approach for constructing three-dimensional spirocyclic frameworks under mild, sustainable conditions and with exquisite stereocontrol. This review surveys the latest advances in biocatalyzed spirocyclization of all-carbon arenes (phenols and benzenes), aza-aromatics (indoles and pyrroles), and oxa-aromatics (furans). We highlight cytochrome P450s, flavin-dependent monooxygenases, multicopper oxidases, and novel metalloenzyme platforms that effect regio- and stereoselective oxidative coupling, epoxidation/semi-pinacol rearrangement, and radical-mediated cyclization to produce diverse spirocycles. Mechanistic insights gleaned from structural, computational, and isotope-labeling studies are discussed where necessary to help the readers further understand the reported reactions. Collectively, these examples demonstrate the transformative potential of biocatalysis to streamline access to spirocyclic scaffolds that are challenging to prepare through traditional methods, underscoring biocatalysis as a transformative tool for synthesizing pharmaceutically relevant spiroscaffolds while adhering to green chemistry paradigms to ultimately contribute to a cleaner and more sustainable future. Full article
(This article belongs to the Section Biocatalysis)
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14 pages, 504 KiB  
Article
Biotransformations with Photobiocatalysts for Enantioselective Ester Hydrolysis
by Agnieszka Śliżewska, Paulina Majewska and Ewa Żymańczyk-Duda
Molecules 2025, 30(13), 2767; https://doi.org/10.3390/molecules30132767 - 27 Jun 2025
Viewed by 333
Abstract
This study investigates the efficient and enantioselective hydrolysis of ester bonds through a series of biotransformations employing various photobiocatalysts. A racemic mixture of 1-phenylethyl acetate served as the model substrate. The described research identified three strains exhibiting the highest biocatalytic activity: Nostoc cf-muscorum [...] Read more.
This study investigates the efficient and enantioselective hydrolysis of ester bonds through a series of biotransformations employing various photobiocatalysts. A racemic mixture of 1-phenylethyl acetate served as the model substrate. The described research identified three strains exhibiting the highest biocatalytic activity: Nostoc cf-muscorum (CCALA 129), Leptolyngbya foveolarum (CCALA 76), and Synechococcus bigranulatus (CCALA 187). Their application led to the complete hydrolysis of the starting reagent, yielding both the unreacted ester and its corresponding alcohol in an enantioselective manner. Notably, the selectivity, expressed as S, reached an impressive value of 283 in certain outcomes. The photobiotransformations were conducted under varying conditions, with particular focus on two essential parameters: the duration of the process, crucial for kinetically controlled reactions, and light exposure, critical for light-dependent organisms. The representative results highlight the efficacy of these biocatalysts. For instance, using Leptolyngbya foveolarum (CCALA 76), Nostoc cf-muscorum (CCALA 129), and Synechococcus bigranulatus (CCALA 187) facilitated the production of 1-(R)-phenylethanol with enantiomeric excesses (ee) of 89%, 88%, and 86%, respectively, at a conversion degree of approximately 50%. These processes also yielded an optically enriched mixture of the unreacted substrate, 1-(S)-phenylethyl acetate. Specifically, in the case of Leptolyngbya foveolarum (CCALA 76), the ee of the unreacted ester reached up to 98%. Light exposure emerged as a key factor influencing selectivity factor (S). Adjusting this parameter allowed us to achieve an E value of up to 283 for the formation of 1-(R)-phenylethanol with an ee > 99% when utilizing the Nostoc cf-muscorum (CCALA 129) strain. Furthermore, light intensity proved crucial for scaling up these processes. Significant results were obtained with Synechococcus bigranulatus, particularly at substrate concentrations ranging from 1 to 10 mM under limited exposure. Here, the conversion degree was 55%, the ee of the (R)-alcohol was 86%, and the selectivity factor (S) value was 21. Full article
(This article belongs to the Special Issue Biocatalytic Platforms Towards Synthesis and Degradation Processes)
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29 pages, 3527 KiB  
Review
Advanced Biocatalytic Processes for the Conversion of Renewable Feedstocks into High-Value Oleochemicals
by João H. C. Wancura, Eliane Pereira Cipolatti, Evelin Andrade Manoel, Febri Odel Nitbani, Angie Vanessa Caicedo-Paz, Cassamo Ussemane Mussagy, Tamer M. M. Abdellatief, Ahmad Mustafa and Luigi di Bitonto
Catalysts 2025, 15(6), 600; https://doi.org/10.3390/catal15060600 - 17 Jun 2025
Viewed by 919
Abstract
Oleochemicals, which are obtained from vegetable and animal fats and oils, have become indispensable in the food, cosmetics, pharmaceutical and biofuel industries. Traditionally, they are synthesized using chemical catalysts, a process that is often associated with high energy requirements and a considerable environmental [...] Read more.
Oleochemicals, which are obtained from vegetable and animal fats and oils, have become indispensable in the food, cosmetics, pharmaceutical and biofuel industries. Traditionally, they are synthesized using chemical catalysts, a process that is often associated with high energy requirements and a considerable environmental impact. Biocatalysis, using enzymes such as lipases, has emerged as a transformative alternative that offers high specificity, environmental friendliness and cost-efficiency. This review comprehensively examines the current state of biocatalysis for oleochemical synthesis, highlighting key reactions such as esterification and transesterification and their integration into industrial processes. A bibliometric analysis uncovers global trends and collaborations, while case studies illustrate cost efficiency and scalability. The article outlines recommendations and future research directions to advance biocatalytic processes. This review is intended to be an important resource for researchers and industries transitioning to sustainable oleochemical production. Full article
(This article belongs to the Special Issue Sustainable Enzymatic Processes for Fine Chemicals and Biodiesel)
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13 pages, 3678 KiB  
Communication
Ecotechnologies for Glucose Oxidase-GOx Immobilization on Nonconductive and Conductive Textiles for Heterogeneous Catalysis and Water Decontamination
by Nemeshwaree Behary, May Kahoush, Mohammad Neaz Morshed, Jinping Guan and Vincent Nierstrasz
Catalysts 2025, 15(5), 472; https://doi.org/10.3390/catal15050472 - 10 May 2025
Viewed by 663
Abstract
The need for sustainable and efficient water decontamination methods has led to the increasing use of redox enzymes such as glucose oxidase (GOx). GOx immobilization on textile supports provides a promising alternative for catalyzing pollutant degradation in bio-Fenton (BF) and bio-electro-Fenton (BEF) systems. [...] Read more.
The need for sustainable and efficient water decontamination methods has led to the increasing use of redox enzymes such as glucose oxidase (GOx). GOx immobilization on textile supports provides a promising alternative for catalyzing pollutant degradation in bio-Fenton (BF) and bio-electro-Fenton (BEF) systems. However, challenges related to enzyme stability, reusability, and environmental impact remain a concern. This communication paper outlines innovative strategies developed to address these challenges, notably the use of ecotechnologies to achieve efficient GOx immobilization while maintaining biocatalytic activity. Plasma ecoprocesses, amino-bearing biopolymer-chitosan, as well as a bio-crosslinker genipin have been used efficiently on conductive carbon and non-conductive polyester-PET nonwovens. In certain cases, immobilized GOx can retain high catalytic activity after multiple cycles, making them an effective biocatalyst for organic dye degradation (Crystal Violet and Remazol Blue) via bio-Fenton reactions, including total heterogeneous bio-Fention system. Moreover, the conductive carbon felt-based bioelectrodes successfully supported simultaneous pollutant degradation and energy generation in a BEF system. This work highlights the potential of textile-based enzyme immobilization for sustainable wastewater treatment, bio-electrochemical energy conversion, and also for bacterial deactivation. Future research will focus on optimizing enzyme stability and enhancing BEF efficiency for large-scale applications. Full article
(This article belongs to the Section Environmental Catalysis)
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13 pages, 2419 KiB  
Article
Enhancement of Enzyme Activity by Alternating Magnetic Field and Near-Infrared Irradiation
by Fang Wang, Yuchen Liu, Qikai Dong, Zihan Li, Senrong Liang, Tianyi Zhang, Liangtao Xu and Renjun Gao
Catalysts 2025, 15(4), 386; https://doi.org/10.3390/catal15040386 - 16 Apr 2025
Viewed by 631
Abstract
The enhancement of enzyme activity has garnered significant attention in biotransformation processes and applications. This enhancement is achieved through the use of specific nanomaterials (NMs) with unique physicochemical characteristics responsive to external stimuli. In this study, an enzyme–Fe3O4 nano-biocatalytic system [...] Read more.
The enhancement of enzyme activity has garnered significant attention in biotransformation processes and applications. This enhancement is achieved through the use of specific nanomaterials (NMs) with unique physicochemical characteristics responsive to external stimuli. In this study, an enzyme–Fe3O4 nano-biocatalytic system (NBS) was developed to enable real-time activation of enzymatic catalysis under alternating magnetic field (AMF) and near-infrared (NIR) irradiation using dual-functional Fe3O4 magnetic nanoparticles (MNPs). When exposed to an AMF, Fe3O4 MNPs generate molecular vibrations through mechanisms such as Néel or Brown relaxation while acting as a photothermal agent in response to NIR irradiation. The synergistic effect of AMF and NIR irradiation significantly enhanced energy transfer between the enzyme and Fe3O4 MNPs, resulting in a maximum 4.3-fold increase in enzyme activity. Furthermore, the system reduced aldol reaction time by 66% (from 4 h to 1.5 h) while achieving 90% product yield. Additionally, factors such as nanoparticle size and NIR power were found to play a critical role in the efficiency of this real-time regulation strategy. The results also demonstrate that the enzyme–Fe3O4 nanocomposites (NCs) significantly enhanced catalytic efficiency and reduced the reaction time for aldol reactions. This study demonstrates an efficient NBS controlled via the synergistic effects of AMF and NIR irradiation, enabling spatiotemporal control of biochemical reactions. This work also provides a breakthrough strategy for dynamic biocatalysis, with potential applications in industrial biomanufacturing, on-demand drug synthesis, and precision nanomedicine. Full article
(This article belongs to the Special Issue Enzyme Catalysis and Enzyme Engineering)
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17 pages, 4733 KiB  
Article
Distinguishing the Contribution of Extracellular Electron Transfer in the Desulfovibrio caledoniensis-Induced Total Corrosion of Q235 Carbon Steel
by Keliang Fan, Fang Guan, Xiaofan Zhai, Guanhua Jiao, Yugang Sang, Min Jing and Jizhou Duan
Materials 2025, 18(7), 1613; https://doi.org/10.3390/ma18071613 - 2 Apr 2025
Viewed by 525
Abstract
Microbially influenced corrosion (MIC) in anaerobic environments accounts for many severe failures and losses in different industries. Sulfate-reducing bacteria (SRB) represent a typical class of corrosive microorganisms capable of acquiring electrons from steel through extracellular electron transfer processes, thereby inducing severe electrical microbially [...] Read more.
Microbially influenced corrosion (MIC) in anaerobic environments accounts for many severe failures and losses in different industries. Sulfate-reducing bacteria (SRB) represent a typical class of corrosive microorganisms capable of acquiring electrons from steel through extracellular electron transfer processes, thereby inducing severe electrical microbially influenced corrosion (EMIC). Although prior research has underscored the significance of extracellular electron transfer, the contribution of EMIC to the whole MIC has not been comprehensively studied. In this study, Q235 steel coupons were employed in an H-shaped electrochemical cell to conduct electrochemical and coupon immersion experiments, aiming to determine the contribution of EMIC to the overall MIC. The experiments were conducted under two distinct carbon source conditions: 100% carbon source (CS) and 1% CS environments. It was observed that the biotic electrodes exhibited significantly higher cathodic currents, with the most pronounced biological cathodic activity detected in the 100% CS biotic medium. The voltammetric responses of the electrodes before and after changes in the medium confirmed the biocatalytic capability of the attached biofilm in stimulating the cathodic reaction. The proportion of EMIC in MIC was calculated using linear polarization resistance, revealing a trend over time. Additionally, weight loss tests indicated that the contribution of EMIC to the total MIC was approximately 27.69%. Furthermore, the results demonstrated that while the overall corrosion rate was lower in the 1% CS environment, the proportion of EMIC in MIC increased to approximately 37.68%. Full article
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15 pages, 4537 KiB  
Article
Construction of a Cofactor Self-Sufficient Enzyme Cascade System Coupled with Microenvironmental Engineering for Efficient Biosynthesis of Tetrahydrofolate and Its Derivative of L-5-Methyltetrahydrofolate
by Ziting Yan, Lisha Qin, Ruirui Qin, Xin Wang and Kequan Chen
Catalysts 2025, 15(3), 235; https://doi.org/10.3390/catal15030235 - 28 Feb 2025
Viewed by 1052
Abstract
Tetrahydrofolate (THF), the biologically active form of folate, serves as a crucial carrier of one-carbon units essential for synthesizing cellular components such as amino acids and purine nucleotides in vivo. It also acts as an important precursor for the production of pharmaceuticals, including [...] Read more.
Tetrahydrofolate (THF), the biologically active form of folate, serves as a crucial carrier of one-carbon units essential for synthesizing cellular components such as amino acids and purine nucleotides in vivo. It also acts as an important precursor for the production of pharmaceuticals, including folinate and L-5-methyltetrahydrofolate (L-5-MTHF). In this study, we developed an efficient enzyme cascade system for the production tetrahydrofolate from folate, incorporating NADPH recycling, and explored its application in the synthesis of L-5-MTHF, a derivative of tetrahydrofolate. To achieve this, we first screened dihydrofolate reductases (DHFRs) from various organisms, identifying SmDHFR from Serratia marcescens as the enzyme with the highest catalytic activity. We then conducted a comparative analysis of formate dehydrogenases (FDHs) from different sources, successfully establishing an NADPH recycling system. To further enhance biocatalytic efficiency, we optimized key reaction parameters, including temperature, pH, enzyme ratio, and substrate concentration. To address the challenge of pH mismatch in dual-enzyme reactions, we employed an enzymatic microenvironment regulation strategy. This involved covalently conjugating SmDHFR with a superfolder green fluorescent protein mutant carrying 30 surface negative charges (−30sfGFP), using the SpyCatcher/SpyTag system. This modification resulted in a 2.16-fold increase in tetrahydrofolate production, achieving a final yield of 4223.4 µM. Finally, we extended the application of this tetrahydrofolate synthesis system to establish an enzyme cascade for L-5-MTHF production with NADH recycling. By incorporating methylenetetrahydrofolate reductase (MTHFR), we successfully produced 389.8 μM of L-5-MTHF from folate and formaldehyde. This work provides a novel and efficient pathway for the biosynthesis of L-5-MTHF and highlights the potential of enzyme cascade systems in the production of tetrahydrofolate-derived compounds. Full article
(This article belongs to the Special Issue Enzyme Engineering—the Core of Biocatalysis)
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20 pages, 4626 KiB  
Article
Enzymatic Oxidation of Hydroxytyrosol in Deep Eutectic Solvents for Chitosan Functionalization and Preparation of Bioactive Nanogels
by Myrto G. Bellou, Anastasia Skonta, Alexandra V. Chatzikonstantinou, Angeliki C. Polydera, Petros Katapodis, Epaminondas Voutsas and Haralambos Stamatis
Catalysts 2025, 15(2), 180; https://doi.org/10.3390/catal15020180 - 14 Feb 2025
Cited by 1 | Viewed by 1030
Abstract
Biocatalytic processes for the formation of bioactive compounds and biopolymer preparations that can be applied in pharmaceuticals and cosmetics are gaining increasing interest due to their safety and sustainability, relying on environmentally friendly approaches and biocompatible compounds. In this work, we investigate the [...] Read more.
Biocatalytic processes for the formation of bioactive compounds and biopolymer preparations that can be applied in pharmaceuticals and cosmetics are gaining increasing interest due to their safety and sustainability, relying on environmentally friendly approaches and biocompatible compounds. In this work, we investigate the implementation of various Deep Eutectic Solvents (DES) in the laccase-catalyzed oxidation of hydroxytyrosol (HT), aiming to produce its oligomer derivatives such as HT dimer and trimer. The composition of the reaction mixture in which the oligomers’ yield was the highest was 70% v/v Bet:PG (1:4 molar ratio). The oligomers formed were subsequently used for the non-enzymatic grafting of chitosan (CS) and the development of bioactive chitosan-based nanogels (NG). Grafted chitosan nanogels were prepared by ionic gelation using sodium tripolyphosphate (TPP) as a cross-linking agent. The functionalized chitosan was characterized using Fourier-Transform Infrared (FTIR) and Nuclear Magnetic Resonance (NMR) spectroscopy, while Scanning Electron Microscopy (SEM) was employed for nanogel characterization. Compared to unmodified chitosan nanogels, grafted chitosan nanogels exhibited almost ten-fold higher antioxidant activity and approximately 20% greater antibacterial activity. Full article
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23 pages, 5174 KiB  
Article
Designed Reactive Natural Deep Eutectic Solvents for Lipase-Catalyzed Esterification
by Alina Ramona Buzatu, Anamaria Todea, Raluca Pop, Diana Maria Dreavă, Cristina Paul, Ioan Bîtcan, Marilena Motoc, Francisc Peter and Carmen Gabriela Boeriu
Molecules 2025, 30(4), 778; https://doi.org/10.3390/molecules30040778 - 7 Feb 2025
Cited by 4 | Viewed by 1435
Abstract
Natural deep eutectic solvents (NADESs) are a sustainable, green option for extraction and reaction media in biorefineries and various chemical and biotechnological applications. Particularly, enzymatic reactions profit from NADES applications, as these solvents help to maintain high substrate solubility while improving both enzyme [...] Read more.
Natural deep eutectic solvents (NADESs) are a sustainable, green option for extraction and reaction media in biorefineries and various chemical and biotechnological applications. Particularly, enzymatic reactions profit from NADES applications, as these solvents help to maintain high substrate solubility while improving both enzyme stability and efficiency. Recent studies confirmed that NADESs can perform multiple functions simultaneously, as reaction media for biocatalytic conversions, but also as substrates and catalysts for reactions, fulfilling the role of a reactive solvent. This study reports the beneficial effect of designed reactive natural deep eutectic solvents (R-NADESs) on the esterification activity and thermal stability of free and immobilized lipases in the synthesis of polyol- and carbohydrate-based biosurfactants. We manufactured and characterized 16 binary and ternary R-NADES systems with choline chloride (ChCl) as the hydrogen bond acceptor (HBA) and carbohydrate polyols; mono-, di-, and oligosaccharides; urea (U); N-methyl urea (MU); and water as the hydrogen bond donors (HBDs), in different combinations and molar ratios, most of which are reported for the first time in this paper. We determined their physicochemical, thermal, and molecular properties, including among others viscosity, polarizability, and the number of hydrogen bonds, and we showed that these properties are controlled by composition, molar ratio, molecular properties, temperature, and water content. Many lipases, both native and immobilized, showed high stability and remarkable catalytic performance in R-NADESs during esterification reactions. Full article
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19 pages, 2835 KiB  
Article
Production of Lipase from Streptomyces spp. AM9-01 by Solid-State Fermentation of Residual Babassu Mesocarp and Immobilization in Accurel® MP1000
by Aldo A. T. Junior, Tamires N. dos Anjos, Melissa L. E. Gutarra, Rodrigo P. do Nascimento and Ivaldo Itabaiana Jr.
Reactions 2025, 6(1), 11; https://doi.org/10.3390/reactions6010011 - 4 Feb 2025
Viewed by 1065
Abstract
A wide range of agro-industrial waste has been generated due to higher demands for food and energy. New protocols for its valorization are urgent strategies for sustainable development. In this work, residual babassu mesocarp, a native plant from the north of Brazil, was [...] Read more.
A wide range of agro-industrial waste has been generated due to higher demands for food and energy. New protocols for its valorization are urgent strategies for sustainable development. In this work, residual babassu mesocarp, a native plant from the north of Brazil, was used as a matrix for producing lipases through solid-state fermentation (SSF) by actinobacterial strains. Initially, 121 strains were screened by rhodamine B and tributyrin methods, where strain Streptomyces spp. AM9-01 was the most promising. It was submitted to the SSF at 30 °C, where 84.8 ± 1.5 U·mL−1 of hydrolytic activity (HA) was found in 48 h. Further studies at pH 7 increased lipase production, achieving 94.6 ± 1.6 U·mL−1 of HA in 12 h. The enzymatic extract was immobilized in Accurel® MP1000, where the biocatalyst Lip 10 showed 79.9 ± 1.5% immobilization efficiency, 4234 ± 24 U·g−1 of HA, and activity retention of 55.4%. Lip10 was used to synthesize ethyl oleate, showing conversions of over 97% in 6 h of reaction, while the commercial biocatalysts TLIM® and N435® showed conversions of over 95% in just 8 h. In addition, Lip10 showed operational stability for eight consecutive cycles. Therefore, it was demonstrated that babassu mesocarp is a viable alternative for obtaining competitive biocatalysts containing lipases for industrial applications from SSF by actinobacteria, which have few reports in the literature and could be potential biocatalytic agents. Full article
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11 pages, 3429 KiB  
Article
Study of Chiral Center Effect on CaLB-Catalyzed Hydrolysis of (±)-1-(Acetoxymethyl)-3, 4, 5-methylpyrrolidin-2-ones
by Luis G. Hernández-Vázquez, Grecia Katherine Sánchez-Muñoz and Jaime Escalante
Catalysts 2024, 14(12), 861; https://doi.org/10.3390/catal14120861 - 26 Nov 2024
Viewed by 962
Abstract
Several chemical and biocatalytic methods have been described for chiral γ-lactams syntheses. However, only one biocatalytic method has been reported for γ4-lactam resolution, while γ2- and γ3-lactams have not been reported. On the other hand, its resolution [...] Read more.
Several chemical and biocatalytic methods have been described for chiral γ-lactams syntheses. However, only one biocatalytic method has been reported for γ4-lactam resolution, while γ2- and γ3-lactams have not been reported. On the other hand, its resolution through biocatalysts is complicated since enzymes such as ENZA-1 (Rhodococcus equi NCIB 40213) and ENZA-20 (Pseudomonas solanacearum NCIB 40249) are difficult to obtain. Therefore, in this paper, the resolution of γ-lactams 7-9 was carried out through a hydrolysis reaction using the commercially available enzyme CaLB. Full article
(This article belongs to the Special Issue New Advances in Chemoenzymatic Synthesis, 2nd Edition)
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12 pages, 5223 KiB  
Article
Dynamics of Nanomotors Propelled by Enzyme Cascade Reactions
by Jia-Qi Hu, Rui Zhao, Ru-Fei Cui, Jian-Long Kou and Jiang-Xing Chen
Int. J. Mol. Sci. 2024, 25(23), 12586; https://doi.org/10.3390/ijms252312586 - 23 Nov 2024
Cited by 1 | Viewed by 1342 | Correction
Abstract
Enzyme-powered nanomotors have attracted significant attention in materials science and biomedicine for their biocompatibility, versatility, and the use of biofuels in biological environments. Here, we employ a hybrid mesoscale method combining molecular dynamics and multi-particle collision dynamics (MD–MPC) to study the dynamics of [...] Read more.
Enzyme-powered nanomotors have attracted significant attention in materials science and biomedicine for their biocompatibility, versatility, and the use of biofuels in biological environments. Here, we employ a hybrid mesoscale method combining molecular dynamics and multi-particle collision dynamics (MD–MPC) to study the dynamics of nanomotors powered by enzyme reactions. Two cascade enzymes are constructed to be layered on the same surface of a Janus colloid, providing a confined space that greatly enhances reaction efficiency. Simulations indicate that such a configuration significantly improves the utilization of intermediate products and, consequently, increases the self-propulsion of the Janus motor. By presenting the gradient fields of substrates and products, as well as the hydrodynamics surrounding the motor, we explore the underlying mechanism behind the enhanced autonomous velocity. Additionally, we discuss the improvements in environmental safety of the modified motor, which may shed light on the fabrication of biocatalytic nano-machines in experiments. Full article
(This article belongs to the Section Physical Chemistry and Chemical Physics)
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11 pages, 524 KiB  
Article
Novel Basidiomycetous Alcohol Oxidase from Cerrena unicolor—Characterisation, Kinetics, and Proteolytic Modifications
by Sylwia Stefanek, Rafał Typek, Michał Dybowski, Dorota Wianowska, Magdalena Jaszek and Grzegorz Janusz
Int. J. Mol. Sci. 2024, 25(22), 11890; https://doi.org/10.3390/ijms252211890 - 5 Nov 2024
Viewed by 872
Abstract
Intracellular alcohol oxidase (AOX) was isolated from the basidiomycetous white rot fungus Cerrena unicolor FCL139. The enzyme was semi-purified (13-fold) using two-step chromatography with 30% activity recovery. The identity of the protein was confirmed by LC-MS/MS analysis, and its MW (72 kDa) and [...] Read more.
Intracellular alcohol oxidase (AOX) was isolated from the basidiomycetous white rot fungus Cerrena unicolor FCL139. The enzyme was semi-purified (13-fold) using two-step chromatography with 30% activity recovery. The identity of the protein was confirmed by LC-MS/MS analysis, and its MW (72 kDa) and pI (6.18) were also determined. The kinetics parameters of the AOX reaction towards various substrates were analysed, which proved that, in addition to methanol (4.36 ± 0.27% of the oxidised substrate), AOX most potently oxidises aromatic alcohols, such as 4-hydroxybenzyl alcohol (14.0 ± 0.8%), benzyl alcohol (4.2 ± 0.3%), anisyl alcohol (7.6 ± 0.4%), and veratryl alcohol (5.0 ± 0.3%). Moreover, the influence of selected commercially available proteases on the biocatalytic properties of AOX from C. unicolor was studied. It was proved that the digested enzyme lost its catalytic potential properties except when incubated with pepsin, which significantly boosted its activity up to 123%. Full article
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