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Molecular Enzymology: Advances and Applications

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Microbiology".

Deadline for manuscript submissions: closed (31 May 2022) | Viewed by 40017

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Dr. Vijai Kumar Gupta

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AgroBioSciences (AgBS) and Chemical & Biochemical Sciences (CBS) Department, University Mohammed VI Polytechnic (UM6P), Lot 660, Hay Moulay Rachid Ben Guerir, 43150, Morocco
Interests: bioactive natural products, microbial biotechnology, applied mycology, enzyme & bioprocess technology, biomass to bioproducts development
Special Issues, Collections and Topics in MDPI journals

Prof. Jiri Damborsky

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Loschmidt Laboratories, Department of Experimental Biology & RECETOX, Faculty of Science, Masaryk University Kamenice 5/A13, 625 00 Brno, Czech Republic
Interests: protein expression, next generation sequencing, functional genomics, recombinant proteins production & purification, biocatalysis, enzyme catalysis, enzyme engineering

Prof. Dr. Gustavo Molina

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Institute of Science and Technology-UFVJM, Diamantina, Minas Gerais, Brazil
Interests: food science and biotechnology; industrial biotechnology; bioconersion processes; bioactive potential of metabolites and ingredients
Special Issues, Collections and Topics in MDPI journals

Prof. Kumar Vivek

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Centre for Rural Development and Technology, Indian Institute of Technology Delhi, New Delhi, India
Interests: valorising waste; biotransformation; process intensification; environmental engineering; chemical engineering, solid waste management

Dr. Zeba Usmani

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Department of Chemistry and Biotechnology, ERA Chair of Green Chemistry, Tallinn University of Technology, Tallinn 12612, Estonia
Interests: microbial biotechnology; enzymatic studies; biodegradation; biomass valorization; green chemistry; environmental sustainability

Special Issue Information

Dear Colleagues,

Microbes are the key for the production of various valuable enzymes and the application of these enzymes to bioproduct development. Microbial enzymes offer extensive and increasingly significant advantages over chemical catalysts since they are derived from renewable resources and are biodegradable. Molecular enzyme technology has become one of the vital research areas in the field of natural sciences. Over five hundred industrial enzymes are being used for many applications in the agri-food-pharma-environment and other related sectors and constitute a multibillion USD annual market globally. From the molecular enzymology perspective, microbial bioengineering and applied biological sciences approaches, like metabolic engineering, next-generation sequencing, functional genomics, systems, and synthetic biology are the key to engineering microbial cell factories to produce tailor-made enzyme bioprocess. The growing demand for tailor-made enzymes from microorganisms for various applications requires the development of new biosynthetic and bioengineering tools, produced from fungi and bacterial systems. Microbial enzyme engineering includes biotechnological innovation, chemical engineering, drug developments, and applied biorefineries development systems. The application of nanotechnology in enzyme bioprocess design and production has opened new avenues for the application of enzymes in the various sectors, especially in biopharmaceutical and drug delivery systems, helping in designing new and novel recombinant proteins and glycans.

This Special Issue also welcomes submissions exploiting diverse and novel microbes from various extremes/hotspots as pillars for the industry and academic research to develop microbial molecular enzymology platform with potential applications in biopharmaceuticals, biochemicals, and several other relevant sectors.

This Special Issue will publish articles including reviews and research papers with an emphasis on enzyme production and formulations.

Dr. Vijai Kumar Gupta
Prof. Jiri Damborsky
Prof. Kumar Vivek
Dr. Zeba Usmani
Prof. Molina Gustavo
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

microbial enzymes
biosynthesis and bioengineering
drug development and targets
enzymes in the environment
engineered enzymes
enzymes in agri-food
enzymatic formulations
enzyme engineering
enzymes in biomedical sciences
green chemistry/technology
glycans
molecular evolution
nanocatalyst and nanotechnology
pharma enzymes
recombinant proteins production and purification
system and synthetic biology

Published Papers (11 papers)

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Research

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15 pages, 3242 KiB

Open AccessArticle

Effects of Module Truncation of a New Alginate Lyase VxAly7C from Marine Vibrio xiamenensis QY104 on Biochemical Characteristics and Product Distribution

by Luyao Tang, Mengmeng Bao, Ying Wang, Zheng Fu, Feng Han and Wengong Yu

Int. J. Mol. Sci. 2022, 23(9), 4795; https://doi.org/10.3390/ijms23094795 - 27 Apr 2022

Cited by 6 | Viewed by 1630

Abstract

Alginate lyase has received extensive attention as an important tool for oligosaccharide preparation, pharmaceutical production, and energy biotransformation. Noncatalytic module carbohydrate-binding modules (CBM) have a major impact on the function of alginate lyases. Although the effects of two different families of CBMs on enzyme characteristics have been reported, the effect of two combined CBM32s on enzyme function has not been elucidated. Herein, we cloned and expressed a new multimodular alginate lyase, VxAly7C, from Vibrioxiamenensis QY104, consisting of two CBM32s at N-terminus and a polysaccharide lyase family 7 (PL7) at C-terminus. To explore the function of CBM32s in VxAly7C, full-length (VxAly7C-FL) and two truncated mutants, VxAly7C-TM1 (with the first CBM32 deleted) and VxAly7C-TM2 (with both CBM32s deleted), were characterized. The catalytic efficiency of recombinant VxAly7C-TM2 was 1.82 and 4.25 times higher than that of VxAly7C-TM1 and VxAly7C-FL, respectively, indicating that CBM32s had an antagonistic effect. However, CBM32s improved the temperature stability, the adaptability in an alkaline environment, and the preference for polyG. Moreover, CBM32s contributed to the production of tri- and tetrasaccharides, significantly affecting the end-product distribution. This study advances the understanding of module function and provides a reference for broader enzymatic applications and further enzymatic improvement and assembly. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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16 pages, 4255 KiB

Open AccessArticle

Discovery of Five New Ethylene-Forming Enzymes for Clean Production of Ethylene in E. coli

by Yixuan Cui, Ying Jiang, Meng Xiao, Muhammad Zeeshan Munir, Sadaf Riaz, Faiz Rasul and Maurycy Daroch

Int. J. Mol. Sci. 2022, 23(9), 4500; https://doi.org/10.3390/ijms23094500 - 19 Apr 2022

Cited by 2 | Viewed by 2174

Abstract

Ethylene is an essential platform chemical with a conjugated double bond, which can produce many secondary chemical products through copolymerisation. At present, ethylene production is mainly from petroleum fractionation and cracking, which are unsustainable in the long term, and harmful to our environment. Therefore, a hot research field is seeking a cleaner method for ethylene production. Based on the model ethylene-forming enzyme (Efe) AAD16440.1 (6vp4.1.A) from Pseudomonas syringae pv. phaseolicol, we evaluated five putative Efe protein sequences using the data derived from phylogenetic analyses and the conservation of their catalytic structures. Then, pBAD expression frameworks were constructed, and relevant enzymes were expressed in E. coli BL21. Finally, enzymatic activity in vitro and in vivo was detected to demonstrate their catalytic activity. Our results show that the activity in vitro measured by the conversion of α-ketoglutarate was from 0.21–0.72 μmol ethylene/mg/min, which varied across the temperatures. In cells, the activity of the new Efes was 12.28–147.43 μmol/gDCW/h (DCW, dry cellular weight). Both results prove that all the five putative Efes could produce ethylene. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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14 pages, 4023 KiB

Open AccessArticle

Structural Analysis of the Ancestral Haloalkane Dehalogenase AncLinB-DmbA

by Andrii Mazur, Pavel Grinkevich, Radka Chaloupkova, Petra Havlickova, Barbora Kascakova, Michal Kuty, Jiri Damborsky, Ivana Kuta Smatanova and Tatyana Prudnikova

Int. J. Mol. Sci. 2021, 22(21), 11992; https://doi.org/10.3390/ijms222111992 - 05 Nov 2021

Viewed by 2093

Abstract

Haloalkane dehalogenases (EC 3.8.1.5) play an important role in hydrolytic degradation of halogenated compounds, resulting in a halide ion, a proton, and an alcohol. They are used in biocatalysis, bioremediation, and biosensing of environmental pollutants and also for molecular tagging in cell biology. The method of ancestral sequence reconstruction leads to prediction of sequences of ancestral enzymes allowing their experimental characterization. Based on the sequences of modern haloalkane dehalogenases from the subfamily II, the most common ancestor of thoroughly characterized enzymes LinB from Sphingobium japonicum UT26 and DmbA from Mycobacterium bovis 5033/66 was in silico predicted, recombinantly produced and structurally characterized. The ancestral enzyme AncLinB-DmbA was crystallized using the sitting-drop vapor-diffusion method, yielding rod-like crystals that diffracted X-rays to 1.5 Å resolution. Structural comparison of AncLinB-DmbA with their closely related descendants LinB and DmbA revealed some differences in overall structure and tunnel architecture. Newly prepared AncLinB-DmbA has the highest active site cavity volume and the biggest entrance radius on the main tunnel in comparison to descendant enzymes. Ancestral sequence reconstruction is a powerful technique to study molecular evolution and design robust proteins for enzyme technologies. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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17 pages, 5531 KiB

Open AccessArticle

Structural Characterization of EnpA D,L-Endopeptidase from Enterococcus faecalis Prophage Provides Insights into Substrate Specificity of M23 Peptidases

by Piotr Henryk Małecki, Paweł Mitkowski, Elżbieta Jagielska, Karolina Trochimiak, Stéphane Mesnage and Izabela Sabała

Int. J. Mol. Sci. 2021, 22(13), 7136; https://doi.org/10.3390/ijms22137136 - 01 Jul 2021

Cited by 5 | Viewed by 2798

Abstract

The best-characterized members of the M23 family are glycyl-glycine hydrolases, such as lysostaphin (Lss) from Staphylococcus simulans or LytM from Staphylococcus aureus. Recently, enzymes with broad specificities were reported, such as EnpA_CD from Enterococcus faecalis, that cleaves D,L peptide bond between the stem peptide and a cross-bridge. Previously, the activity of EnpA_CD was demonstrated only on isolated peptidoglycan fragments. Herein we report conditions in which EnpA_CD lyses bacterial cells live with very high efficiency demonstrating great bacteriolytic potential, though limited to a low ionic strength environment. We have solved the structure of the EnpA_CD H109A inactive variant and analyzed it in the context of related peptidoglycan hydrolases structures to reveal the bases for the specificity determination. All M23 structures share a very conserved β-sheet core which constitutes the rigid bottom of the substrate-binding groove and active site, while variable loops create the walls of the deep and narrow binding cleft. A detailed analysis of the binding groove architecture, specificity of M23 enzymes and D,L peptidases demonstrates that the substrate groove, which is particularly deep and narrow, is accessible preferably for peptides composed of amino acids with short side chains or subsequent L and D-isomers. As a result, the bottom of the groove is involved in interactions with the main chain of the substrate while the side chains are protruding in one plane towards the groove opening. We concluded that the selectivity of the substrates is based on their conformations allowed only for polyglycine chains and alternating chirality of the amino acids. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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28 pages, 8398 KiB

Open AccessArticle

Secretome Analysis of Arabidopsis–Trichoderma atroviride Interaction Unveils New Roles for the Plant Glutamate:Glyoxylate Aminotransferase GGAT1 in Plant Growth Induced by the Fungus and Resistance against Botrytis cinerea

by María del Carmen González-López, Saúl Jijón-Moreno, Mitzuko Dautt-Castro, Cesaré Ovando-Vázquez, Tamar Ziv, Benjamin A. Horwitz and Sergio Casas-Flores

Int. J. Mol. Sci. 2021, 22(13), 6804; https://doi.org/10.3390/ijms22136804 - 24 Jun 2021

Cited by 11 | Viewed by 3897

Abstract

The establishment of plant–fungus mutualistic interaction requires bidirectional molecular crosstalk. Therefore, the analysis of the interacting organisms secretomes would help to understand how such relationships are established. Here, a gel-free shotgun proteomics approach was used to identify the secreted proteins of the plant Arabidopsis thaliana and the mutualistic fungus Trichoderma atroviride during their interaction. A total of 126 proteins of Arabidopsis and 1027 of T. atroviride were identified. Among them, 118 and 780 were differentially modulated, respectively. Bioinformatic analysis unveiled that both organisms’ secretomes were enriched with enzymes. In T. atroviride, glycosidases, aspartic endopeptidases, and dehydrogenases increased in response to Arabidopsis. Additionally, amidases, protein-serine/threonine kinases, and hydro-lyases showed decreased levels. Furthermore, peroxidases, cysteine endopeptidases, and enzymes related to the catabolism of secondary metabolites increased in the plant secretome. In contrast, pathogenesis-related proteins and protease inhibitors decreased in response to the fungus. Notably, the glutamate:glyoxylate aminotransferase GGAT1 was secreted by Arabidopsis during its interaction with T. atroviride. Our study showed that GGAT1 is partially required for plant growth stimulation and on the induction of the plant systemic resistance by T. atroviride. Additionally, GGAT1 seems to participate in the negative regulation of the plant systemic resistance against B. cinerea through a mechanism involving H₂O₂ production. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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17 pages, 2398 KiB

Open AccessArticle

Molecular Characterization of Xyloglucanase cel74a from Trichoderma reesei

by Douglas Christian Borges Lopes, Cláudia Batista Carraro, Roberto Nascimento Silva and Renato Graciano de Paula

Int. J. Mol. Sci. 2021, 22(9), 4545; https://doi.org/10.3390/ijms22094545 - 27 Apr 2021

Cited by 4 | Viewed by 2048

Abstract

Background: The filamentous fungus Trichoderma reesei is used on an industrial scale to produce enzymes of biotechnological interest. This fungus has a complex cellulolytic system involved in the degradation of lignocellulosic biomass. However, several aspects related to the regulation of the expression of holocellulolytic genes and the production of cellulases by this fungus are still understood. Methods: Here, we constructed a null mutant strain for the xyloglucanase cel74a gene and performed the characterization of the Δcel74a strain to evaluate the genetic regulation of the holocellulases during sugarcane bagasse (SCB) cultivation. Results: Our results demonstrate that the deletion of xyloglucanase cel74a may impact the regulation of holocellulase expression during SCB cultivation. The expression of cellulases cel7a, cel7b, and cel6a was reduced in Δcel74a strain, while the hemicellulases xyn1 and xyn2 were increased in the presence of SCB. The cel74a mutation also affected the xyloglucan hydrolysis patterns. In addition, CEL74A activity was modulated in the presence of calcium, suggesting that this ion may be required for efficient degradation of xyloglucan. Conclusions: CEL74A affects the regulation of holocellulolytic genes and the efficient degradation of SCB in T. reesei. This data makes a significant contribution to our understanding of the carbon utilization of fungal strains as a whole. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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17 pages, 1981 KiB

Open AccessArticle

Enhanced Production of the Mical Redox Domain for Enzymology and F-actin Disassembly Assays

by Jimok Yoon, Heng Wu, Ruei-Jiun Hung and Jonathan R. Terman

Int. J. Mol. Sci. 2021, 22(4), 1991; https://doi.org/10.3390/ijms22041991 - 17 Feb 2021

Cited by 3 | Viewed by 2471

Abstract

To change their behaviors, cells require actin proteins to assemble together into long polymers/filaments—and so a critical goal is to understand the factors that control this actin filament (F-actin) assembly and stability. We have identified a family of unusual actin regulators, the MICALs, which are flavoprotein monooxygenase/hydroxylase enzymes that associate with flavin adenine dinucleotide (FAD) and use the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH) in Redox reactions. F-actin is a specific substrate for these MICAL Redox enzymes, which oxidize specific amino acids within actin to destabilize actin filaments. Furthermore, this MICAL-catalyzed reaction is reversed by another family of Redox enzymes (SelR/MsrB enzymes)—thereby revealing a reversible Redox signaling process and biochemical mechanism regulating actin dynamics. Interestingly, in addition to the MICALs’ Redox enzymatic portion through which MICALs covalently modify and affect actin, MICALs have multiple other domains. Less is known about the roles of these other MICAL domains. Here we provide approaches for obtaining high levels of recombinant protein for the Redox only portion of Mical and demonstrate its catalytic and F-actin disassembly activity. These results provide a ground state for future work aimed at defining the role of the other domains of Mical — including characterizing their effects on Mical’s Redox enzymatic and F-actin disassembly activity. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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18 pages, 4431 KiB

Open AccessArticle

Molecular Dissection of Escherichia coli CpdB: Roles of the N Domain in Catalysis and Phosphate Inhibition, and of the C Domain in Substrate Specificity and Adenosine Inhibition

by Iralis López-Villamizar, Alicia Cabezas, Rosa María Pinto, José Canales, João Meireles Ribeiro, Joaquim Rui Rodrigues, María Jesús Costas and José Carlos Cameselle

Int. J. Mol. Sci. 2021, 22(4), 1977; https://doi.org/10.3390/ijms22041977 - 17 Feb 2021

Cited by 6 | Viewed by 2386

Abstract

CpdB is a 3′-nucleotidase/2′3′-cyclic nucleotide phosphodiesterase, active also with reasonable efficiency on cyclic dinucleotides like c-di-AMP (3′,5′-cyclic diadenosine monophosphate) and c-di-GMP (3′,5′-cyclic diadenosine monophosphate). These are regulators of bacterial physiology, but are also pathogen-associated molecular patterns recognized by STING to induce IFN-β response in infected hosts. The cpdB gene of Gram-negative and its homologs of gram-positive bacteria are virulence factors. Their protein products are extracytoplasmic enzymes (either periplasmic or cell–wall anchored) and can hydrolyze extracellular cyclic dinucleotides, thus reducing the innate immune responses of infected hosts. This makes CpdB(-like) enzymes potential targets for novel therapeutic strategies in infectious diseases, bringing about the necessity to gain insight into the molecular bases of their catalytic behavior. We have dissected the two-domain structure of Escherichia coli CpdB to study the role of its N-terminal and C-terminal domains (CpdB_Ndom and CpdB_Cdom). The specificity, kinetics and inhibitor sensitivity of point mutants of CpdB, and truncated proteins CpdB_Ndom and CpdB_Cdom were investigated. CpdB_Ndom contains the catalytic site, is inhibited by phosphate but not by adenosine, while CpdB_Cdom is inactive but contains a substrate-binding site that determines substrate specificity and adenosine inhibition of CpdB. Among CpdB substrates, 3′-AMP, cyclic dinucleotides and linear dinucleotides are strongly dependent on the CpdB_Cdom binding site for activity, as the isolated CpdB_Ndom showed much-diminished activity on them. In contrast, 2′,3′-cyclic mononucleotides and bis-4-nitrophenylphosphate were actively hydrolyzed by CpdB_Ndom, indicating that they are rather independent of the CpdB_Cdom binding site. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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12 pages, 2934 KiB

Open AccessArticle

Enhanced Heterologous Production of Glycosyltransferase UGT76G1 by Co-Expression of Endogenous prpD and malK in Escherichia coli and Its Transglycosylation Application in Production of Rebaudioside

by Wenju Shu, Hongchen Zheng, Xiaoping Fu, Jie Zhen, Ming Tan, Jianyong Xu, Xingya Zhao, Shibin Yang, Hui Song and Yanhe Ma

Int. J. Mol. Sci. 2020, 21(16), 5752; https://doi.org/10.3390/ijms21165752 - 11 Aug 2020

Cited by 21 | Viewed by 3023

Abstract

Steviol glycosides (SGs) with zero calories and high-intensity sweetness are the best substitutes of sugar for the human diet. Uridine diphosphate dependent glycosyltransferase (UGT) UGT76G1, as a key enzyme for the biosynthesis of SGs with a low heterologous expression level, hinders its application. In this study, a suitable fusion partner, Smt3, was found to enhance the soluble expression of UGT76G1 by 60%. Additionally, a novel strategy to improve the expression of Smt3-UGT76G1 was performed, which co-expressed endogenous genes prpD and malK in Escherichia coli. Notably, this is the first report of constructing an efficient E. coli expression system by regulating prpD and malK expression, which remarkably improved the expression of Smt3-UGT76G1 by 200% as a consequence. Using the high-expression strain E. coli BL21 (DE3) M/P-3-S32U produced 1.97 g/L of Smt3-UGT76G1 with a yield rate of 61.6 mg/L/h by fed-batch fermentation in a 10 L fermenter. The final yield of rebadioside A (Reb A) and rebadioside M (Reb M) reached 4.8 g/L and 1.8 g/L, respectively, when catalyzed by Smt3-UGT76G1 in the practical UDP-glucose regeneration transformation system in vitro. This study not only carried out low-cost biotransformation of SGs but also provided a novel strategy for improving expression of heterologous proteins in E. coli. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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Review

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21 pages, 5701 KiB

Open AccessReview

Thrombolytic Enzymes of Microbial Origin: A Review

by Deepti Diwan, Zeba Usmani, Minaxi Sharma, James W. Nelson, Vijay Kumar Thakur, Graham Christie, Gustavo Molina and Vijai Kumar Gupta

Int. J. Mol. Sci. 2021, 22(19), 10468; https://doi.org/10.3390/ijms221910468 - 28 Sep 2021

Cited by 13 | Viewed by 5649

Abstract

Enzyme therapies are attracting significant attention as thrombolytic drugs during the current scenario owing to their great affinity, specificity, catalytic activity, and stability. Among various sources, the application of microbial-derived thrombolytic and fibrinolytic enzymes to prevent and treat vascular occlusion is promising due to their advantageous cost–benefit ratio and large-scale production. Thrombotic complications such as stroke, myocardial infarction, pulmonary embolism, deep venous thrombosis, and peripheral occlusive diseases resulting from blood vessel blockage are the major cause of poor prognosis and mortality. Given the ability of microbial thrombolytic enzymes to dissolve blood clots and prevent any adverse effects, their use as a potential thrombolytic therapy has attracted great interest. A better understanding of the hemostasis and fibrinolytic system may aid in improving the efficacy and safety of this treatment approach over classical thrombolytic agents. Here, we concisely discuss the physiological mechanism of thrombus formation, thrombo-, and fibrinolysis, thrombolytic and fibrinolytic agents isolated from bacteria, fungi, and algae along with their mode of action and the potential application of microbial enzymes in thrombosis therapy. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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20 pages, 1052 KiB

Open AccessReview

Enzyme Therapy: Current Challenges and Future Perspectives

by Miguel de la Fuente, Laura Lombardero, Alfonso Gómez-González, Cristina Solari, Iñigo Angulo-Barturen, Arantxa Acera, Elena Vecino, Egoitz Astigarraga and Gabriel Barreda-Gómez

Int. J. Mol. Sci. 2021, 22(17), 9181; https://doi.org/10.3390/ijms22179181 - 25 Aug 2021

Cited by 51 | Viewed by 9935

Abstract

In recent years, enzymes have risen as promising therapeutic tools for different pathologies, from metabolic deficiencies, such as fibrosis conditions, ocular pathologies or joint problems, to cancer or cardiovascular diseases. Treatments based on the catalytic activity of enzymes are able to convert a wide range of target molecules to restore the correct physiological metabolism. These treatments present several advantages compared to established therapeutic approaches thanks to their affinity and specificity properties. However, enzymes present some challenges, such as short in vivo half-life, lack of targeted action and, in particular, patient immune system reaction against the enzyme. For this reason, it is important to monitor serum immune response during treatment. This can be achieved by conventional techniques (ELISA) but also by new promising tools such as microarrays. These assays have gained popularity due to their high-throughput analysis capacity, their simplicity, and their potential to monitor the immune response of patients during enzyme therapies. In this growing field, research is still ongoing to solve current health problems such as COVID-19. Currently, promising therapeutic alternatives using the angiotensin-converting enzyme 2 (ACE2) are being studied to treat COVID-19. Full article

(This article belongs to the Special Issue Molecular Enzymology: Advances and Applications)

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