Biomedical Applications of Enzymes

Topic Information

Dear Colleagues,

This Special Issue entitled “Biomedical Applications of Enzymes” will focus on studies investigating the versatile roles and utility of enzymes in biology and medicine. The Special Issue will encompass research on enzymes as therapeutics, drug targets and biomarkers. It will also cover research on enzyme function, the identification of enzyme substrates, measuring enzymatic activity, and applications in biochemistry, among other applied disciplines. Our Special Issue will consider original articles, review articles, and commentaries that focus on the following potential topics as well as other articles that can fall within the context:

• Enzymes as therapeutics;
• Enzymes as drug targets;
• Enzymes as biomarkers;
• Enzyme function;
• Enzyme activity;
• Allosteric modulators of enzymatic activity;
• Applications of enzymes in biochemistry;
• Applications of enzymes in food industry;
• Other relevant disciplines.

Dr. Amirata Saei Dibavar
Dr. Roozbeh Eskandari
Dr. Lucia Coppo
Topic Editors

Keywords

Participating Journals

Journal Name	Impact Factor	CiteScore	Launched Year	First Decision (median)	APC
Applied Microbiology applmicrobiol	-	-	2021	14.3 Days	CHF 1000
Biology biology	3.6	5.7	2012	16.4 Days	CHF 2700
Biomedicines biomedicines	3.9	5.2	2013	14.6 Days	CHF 2600
Biomolecules biomolecules	4.8	9.4	2011	18.4 Days	CHF 2700
Proteomes proteomes	4.0	6.5	2013	27.3 Days	CHF 1800

Preprints.org is a multidisciplinary platform offering a preprint service designed to facilitate the early sharing of your research. It supports and empowers your research journey from the very beginning.

MDPI Topics is collaborating with Preprints.org and has established a direct connection between MDPI journals and the platform. Authors are encouraged to take advantage of this opportunity by posting their preprints at Preprints.org prior to publication:

1. Share your research immediately: disseminate your ideas prior to publication and establish priority for your work.
2. Safeguard your intellectual contribution: Protect your ideas with a time-stamped preprint that serves as proof of your research timeline.
3. Boost visibility and impact: Increase the reach and influence of your research by making it accessible to a global audience.
4. Gain early feedback: Receive valuable input and insights from peers before submitting to a journal.
5. Ensure broad indexing: Web of Science (Preprint Citation Index), Google Scholar, Crossref, SHARE, PrePubMed, Scilit and Europe PMC.

Published Papers (9 papers)

Order results

Content type Publication Date

Result details

Normal Extended Compact

Journals

All Applied Microbiology Biology Biomedicines Biomolecules Proteomes

Show export options expand_more Show export options expand_less

Select all

Export citation of selected articles as:

Plain Text BibTeX BibTeX (without abstracts) Endnote Endnote (without abstracts) Tab-delimited RIS

Error

Oops... you haven't selected anything for export.

Ok

clear

attachment

Supplementary material:
Supplementary File 1 (ZIP, 1306 KiB)

19 pages, 2297 KiB  

Open AccessArticle

Potential Application of Recombinant Snake Prothrombin Activator Ecarin in Blood Diagnostics

by Kong-Nan Zhao, Paul Masci, Goce Dimeski, Lambro Johnson, Michael Grant, John de Jersey and Martin F. Lavin

Biomolecules 2022, 12(11), 1704; https://doi.org/10.3390/biom12111704 - 17 Nov 2022

Cited by 2 | Viewed by 3104

Abstract

We describe here the purification and cloning of a codon-optimized form of the snake prothrombin activator ecarin from the saw scaled viper (Echis carinatus) expressed in mammalian cells. Expression of recombinant ecarin (rEcarin) was carried out in human embryonic kidney cells [...] Read more.

We describe here the purification and cloning of a codon-optimized form of the snake prothrombin activator ecarin from the saw scaled viper (Echis carinatus) expressed in mammalian cells. Expression of recombinant ecarin (rEcarin) was carried out in human embryonic kidney cells (HEK) cells under conditions for the development and performance of a novel and scalable recombinant snake ecarin to industry standards. Clotting performance of the rEcarin was established in recalcified citrated whole blood, plasma, and fresh whole blood and found to be comparable to native ecarin (N-Ecarin). Furthermore, hemolysis was observed with N-Ecarin at relatively high doses in both recalcified citrated and fresh whole blood, while clotting was not observed with rEcarin, providing an important advantage for the recombinant form. In addition, rEcarin effectively clotted both recalcified citrated whole blood and fresh whole blood containing different anticoagulants including heparin, warfarin, dabigatran, Fondaparinux, rivaroxaban and apixaban, forming firm clots in the blood collection tubes. These results demonstrate that rEcarin efficiently clots normal blood as well as blood spiked with high concentrations of anticoagulants and has great potential as an additive to blood collection tubes to produce high quality serum for analyte analysis in diagnostic medicine. Full article

(This article belongs to the Topic Biomedical Applications of Enzymes)

►▼ Show Figures

Figure 1

13 pages, 1155 KiB  

Open AccessReview

The Role of Phosphorylation and Acylation in the Regulation of Drug Resistance in Mycobacterium tuberculosis

by Manluan Sun, Sai Ge and Zhaoyang Li

Biomedicines 2022, 10(10), 2592; https://doi.org/10.3390/biomedicines10102592 - 15 Oct 2022

Cited by 11 | Viewed by 3169

Abstract

Tuberculosis is a chronic and lethal infectious disease caused by Mycobacterium tuberculosis. In previous decades, most studies in this area focused on the pathogenesis and drug targets for disease treatments. However, the emergence of drug-resistant strains has increased the difficulty of clinical [...] Read more.

Tuberculosis is a chronic and lethal infectious disease caused by Mycobacterium tuberculosis. In previous decades, most studies in this area focused on the pathogenesis and drug targets for disease treatments. However, the emergence of drug-resistant strains has increased the difficulty of clinical trials over time. Now, more post-translational modified proteins in Mycobacterium tuberculosis have been discovered. Evidence suggests that these proteins have the ability to influence tuberculosis drug resistance. Hence, this paper systematically summarizes updated research on the impacts of protein acylation and phosphorylation on the acquisition of drug resistance in Mycobacterium tuberculosis through acylation and phosphorylation protein regulating processes. This provides us with a better understanding of the mechanism of antituberculosis drugs and may contribute to a reduction the harm that tuberculosis brings to society, as well as aiding in the discovery of new drug targets and therapeutic regimen adjustments in the future. Full article

(This article belongs to the Topic Biomedical Applications of Enzymes)

►▼ Show Figures

Graphical abstract

12 pages, 6430 KiB  

Open AccessArticle

Chemical Scalpel: An Experimental Collagenase-Based Treatment for Peritoneal Adhesions

by Javier Barambio, Mariano García-Arranz, Pedro Villarejo Campos, Juan Felipe Vélez Pinto, Luz Vega Clemente, Soledad García Gómez-Heras, Héctor Guadalajara and Damián García-Olmo

Biology 2022, 11(8), 1159; https://doi.org/10.3390/biology11081159 - 2 Aug 2022

Cited by 2 | Viewed by 2924

Abstract

(1) Background: Abdominal adhesions are a common disease appearing after any type of abdominal surgery and may prolong surgical time and cause intestinal obstruction, infertility, or chronic pain. We propose the use of intraperitoneal collagenase to perform chemical adhesiolysis based on the pathophysiology [...] Read more.

(1) Background: Abdominal adhesions are a common disease appearing after any type of abdominal surgery and may prolong surgical time and cause intestinal obstruction, infertility, or chronic pain. We propose the use of intraperitoneal collagenase to perform chemical adhesiolysis based on the pathophysiology and histology of adhesions. (2) Methods: We generated an adhesion model with intraperitoneal polypropylene meshes. Four months later, we evaluated the efficacy of the treatment in blinded form, i.e., 0.05% collagenase vs. placebo at 37 °C for 20 min. Protocol 1: Ten rats with ten mesh fragments, in which an attempt was made to remove the maximum number of meshes in a 5-min period. Protocol 2: Six rats with four mesh fragments in the sides of the abdominal cavity in which adhesiolysis was performed using a device that measures burst pressure. (3) Results: Protocol 1: 42% efficacy in the collagenase group versus 8% in the control group (p < 0.013). Protocol 2: 188.25 mmHg (SD 69.65) in the collagenase group vs. 325.76 mmHg (SD 50.25) in the control group (p < 0.001). (4) Conclusions: Collagenase allows for the safe and effective chemical adhesiolysis in this experimental model of adhesions. Full article

(This article belongs to the Topic Biomedical Applications of Enzymes)

►▼ Show Figures

Figure 1

16 pages, 1810 KiB  

Open AccessReview

AMPK and Diseases: State of the Art Regulation by AMPK-Targeting Molecules

by Olga Tarasiuk, Matteo Miceli, Alessandro Di Domizio and Gabriella Nicolini

Biology 2022, 11(7), 1041; https://doi.org/10.3390/biology11071041 - 11 Jul 2022

Cited by 16 | Viewed by 5768

Abstract

5′-adenosine monophosphate (AMP)-activated protein kinase (AMPK) is an enzyme that regulates cellular energy homeostasis, glucose, fatty acid uptake, and oxidation at low cellular ATP levels. AMPK plays an important role in several molecular mechanisms and physiological conditions. It has been shown that AMPK [...] Read more.

5′-adenosine monophosphate (AMP)-activated protein kinase (AMPK) is an enzyme that regulates cellular energy homeostasis, glucose, fatty acid uptake, and oxidation at low cellular ATP levels. AMPK plays an important role in several molecular mechanisms and physiological conditions. It has been shown that AMPK can be dysregulated in different chronic diseases, such as inflammation, diabetes, obesity, and cancer. Due to its fundamental role in physiological and pathological cellular processes, AMPK is considered one of the most important targets for treating different diseases. Over decades, different AMPK targeting compounds have been discovered, starting from those that activate AMPK indirectly by altering intracellular AMP:ATP ratio to compounds that activate AMPK directly by binding to its activation sites. However, indirect altering of intracellular AMP:ATP ratio influences different cellular processes and induces side effects. Direct AMPK activators showed more promising results in eliminating side effects as well as the possibility to engineer drugs for specific AMPK isoforms activation. In this review, we discuss AMPK targeting drugs, especially concentrating on those compounds that activate AMPK by mimicking AMP. These compounds are poorly described in the literature and still, a lot of questions remain unanswered about the exact mechanism of AMP regulation. Future investigation of the mechanism of AMP binding will make it possible to develop new compounds that, in combination with others, can activate AMPK in a synergistic manner. Full article

(This article belongs to the Topic Biomedical Applications of Enzymes)

►▼ Show Figures

Figure 1

13 pages, 27373 KiB  

Open AccessArticle

Potential Effect of Enzymatic Porcine Placental Hydrolysate (EPPH) to Improve Alcoholic Liver Disease (ALD) by Promoting Lipolysis in the Liver

by Hak Yong Lee, Young Mi Park, Dong Yeop Shin, Kwang Hyun Park, Min Ju Kim, Sun Myung Yoon, Keun Nam Kim, Hye Jeong Yang, Min Jung Kim, Soo-Cheol Choi and In-Ah Lee

Biology 2022, 11(7), 1012; https://doi.org/10.3390/biology11071012 - 6 Jul 2022

Cited by 4 | Viewed by 2372

Abstract

Alcoholic liver disease is associated with the production of highly reactive free radicals by ethanol and its metabolites. Free radicals not only induce liver oxidation and damage tissues, but also stimulate an inflammatory response in hepatocytes, leading to severe liver disease. In order [...] Read more.

Alcoholic liver disease is associated with the production of highly reactive free radicals by ethanol and its metabolites. Free radicals not only induce liver oxidation and damage tissues, but also stimulate an inflammatory response in hepatocytes, leading to severe liver disease. In order to improve alcoholic liver disease, enzymatic porcine placenta hydrolysate was studied by exploring various materials. Enzymatic porcine placenta hydrolysate (EPPH) contains various amino acids, peptides, and proteins, and is used as a useful substance in the body. In this study, changes were confirmed in indicators related to the antioxidant efficacy of EPPH in vitro and in vivo. EPPH inhibits an EtOH-induced decrease in superoxide dismutase and catalase activity through inhibition of free radicals without endogenous cytotoxicity. EPPH has been observed to have a partial effect on common liver function factors such as liver weight, ALT, AST, ALP, and GGT. In addition, EPPH affected changes in fat regulators and inflammatory cytokines in blood biochemical assays. It was confirmed that EPPH was involved in fat metabolism in hepatocytes by regulating PPARα in an alcoholic liver disease animal model. Therefore, EPPH strongly modulates Bcl-2 and BAX involved in apoptosis, thereby exhibiting cytochrome P450 (CYP)-inhibitory effects in alcoholic liver disease cells. As a result, this study confirmed that EPPH is a substance that can help liver health by improving liver disease in an alcoholic liver disease animal model. Full article

(This article belongs to the Topic Biomedical Applications of Enzymes)

►▼ Show Figures

Figure 1

attachment

Supplementary material:
Supplementary File 1 (ZIP, 1411 KiB)

21 pages, 10959 KiB  

Open AccessArticle

l-Ornithine-N5-monooxygenase (PvdA) Substrate Analogue Inhibitors for Pseudomonas aeruginosa Infections Treatment: Drug Repurposing Computational Studies

by Joseph Christina Rosy, Ewa Babkiewicz, Piotr Maszczyk, Piotr Mrówka, Banoth Karan Kumar, Sankaranarayanan Murugesan, Selvaraj Kunjiappan and Krishnan Sundar

Biomolecules 2022, 12(7), 887; https://doi.org/10.3390/biom12070887 - 25 Jun 2022

Cited by 4 | Viewed by 2769

Abstract

Pseudomonas aeruginosa is an opportunistic pathogen that can cause acute and severe infections. Increasing resistance to antibiotics has given rise to the urgent need for an alternative antimicrobial agent. A promising strategy is the inhibition of iron sequestration in the bacteria. The current [...] Read more.

Pseudomonas aeruginosa is an opportunistic pathogen that can cause acute and severe infections. Increasing resistance to antibiotics has given rise to the urgent need for an alternative antimicrobial agent. A promising strategy is the inhibition of iron sequestration in the bacteria. The current work aimed to screen for inhibitors of pyoverdine-mediated iron sequestration in P. aeruginosa. As a drug target, we choose l-ornithine-N5-monooxygenase (PvdA), an enzyme involved in the biosynthesis of pyoverdine that catalyzes the FAD-dependent hydroxylation of the side chain amine of ornithine. As drug repurposing is a fast and cost-efficient way of discovering new applications for known drugs, the approach may help to solve emerging clinical problems. In this study, we use data about molecules from drug banks for screening. A total of 15 drugs that are similar in structure to l-ornithine, the substrate of PvdA, and 30 drugs that are sub-structures of l-ornithine were virtually docked against PvdA. N-2-succinyl ornithine and cilazapril were found to be the top binders with a binding energy of −12.8 and −9.1 kcal mol⁻¹, respectively. As the drug-likeness and ADME properties of the drugs were also found to be promising, molecular dynamics studies were performed to further confirm the stability of the complexes. The results of this in silico study indicate that N-2-succinyl ornithine could potentially be explored as a drug for the treatment of P. aeruginosa infections. Full article

(This article belongs to the Topic Biomedical Applications of Enzymes)

►▼ Show Figures

Figure 1

24 pages, 9421 KiB  

Open AccessReview

Filamentous Thermosensitive Mutant Z: An Appealing Target for Emerging Pathogens and a Trek on Its Natural Inhibitors

by Manisha Gurnani, Abhishek Chauhan, Anuj Ranjan, Hardeep Singh Tuli, Mustfa F. Alkhanani, Shafiul Haque, Kuldeep Dhama, Rup Lal and Tanu Jindal

Biology 2022, 11(5), 624; https://doi.org/10.3390/biology11050624 - 20 Apr 2022

Cited by 3 | Viewed by 3755

Abstract

Antibiotic resistance is a major emerging issue in the health care sector, as highlighted by the WHO. Filamentous Thermosensitive mutant Z (Fts-Z) is gaining significant attention in the scientific community as a potential anti-bacterial target for fighting antibiotic resistance among several pathogenic bacteria. [...] Read more.

Antibiotic resistance is a major emerging issue in the health care sector, as highlighted by the WHO. Filamentous Thermosensitive mutant Z (Fts-Z) is gaining significant attention in the scientific community as a potential anti-bacterial target for fighting antibiotic resistance among several pathogenic bacteria. The Fts-Z plays a key role in bacterial cell division by allowing Z ring formation. Several in vitro and in silico experiments have demonstrated that inhibition of Fts-Z can lead to filamentous growth of the cells, and finally, cell death occurs. Many natural compounds that have successfully inhibited Fts-Z are also studied. This review article intended to highlight the structural–functional aspect of Fts-Z that leads to Z-ring formation and its contribution to the biochemistry and physiology of cells. The current trend of natural inhibitors of Fts-Z protein is also covered. Full article

(This article belongs to the Topic Biomedical Applications of Enzymes)

►▼ Show Figures

Figure 1

17 pages, 2927 KiB  

Open AccessArticle

Sulphoraphane Affinity-Based Chromatography for the Purification of Myrosinase from Lepidium sativum Seeds

by Helena Galádová, Zoltán Polozsányi, Albert Breier and Martin Šimkovič

Biomolecules 2022, 12(3), 406; https://doi.org/10.3390/biom12030406 - 5 Mar 2022

Cited by 14 | Viewed by 3753

Abstract

Sulforaphane and other natural isothiocyanates released from the respective plant glucosinolates by the plant enzyme myrosinase (β-thioglucoside glucohydrolase) show extensive anticancer and antimicrobial effects. In this study, myrosinase from garden cress (Lepidium sativum) seeds was purified to electrophoretic homogeneity by a [...] Read more.

Sulforaphane and other natural isothiocyanates released from the respective plant glucosinolates by the plant enzyme myrosinase (β-thioglucoside glucohydrolase) show extensive anticancer and antimicrobial effects. In this study, myrosinase from garden cress (Lepidium sativum) seeds was purified to electrophoretic homogeneity by a fast and easy strategy consisting of fractionation by isoelectric precipitation with ammonium sulphate (AS) and affinity chromatography using sulforaphane (SFN) attached to cellulose resin. The overall purification of enzyme with respect to crude extract was 169-fold and recovery of 37%. Under non-reducing conditions, two protein bands exhibiting myrosinase activity with masses of about 114 and 122 kDa, respectively, and a 58 kDa protein band with no activity were detected by SDS-PAGE and zymography on polyacrylamide gel. MALDI-Tof/Tof of tryptic fragments obtained from the respective protein bands detected sequence motifs homologous to the regions responsible for glycoside-substrate binding and similarities to members of the enzyme subfamilies β-glucosidases and myrosinases GH. The enzyme hydrolyzed both the natural (sinigrin, sinalbin, glucoraphanin) and the synthetic (p-nitrophenol-β-D-glucopyranoside (pNPG)) substrates. The highest catalytic activity of purified enzyme was achieved against sinigrin. The K_M and V_max values of the enzyme for sinigrin were found to be 0.57 mM, and 1.3 mM/s, respectively. The enzyme was strongly activated by 30 μM ascorbic acid. The optimum temperature and pH for enzyme was 50 °C and pH 6.0, respectively. The purified enzyme could be stored at 4 °C and slightly acidic pH for at least 45 days without a significant decrease in specific activity. Full article

(This article belongs to the Topic Biomedical Applications of Enzymes)

►▼ Show Figures

Figure 1

attachment

Supplementary material:
Supplementary File 1 (ZIP, 242 KiB)

15 pages, 2434 KiB  

Open AccessArticle

Broccoli Myrosinase cDNA Expression in Escherichia coli and Saccharomyces cerevisiae

by Carolina Curiqueo, Andrea Mahn and Antonio Castillo

Biomolecules 2022, 12(2), 233; https://doi.org/10.3390/biom12020233 - 30 Jan 2022

Cited by 5 | Viewed by 3985

Abstract

Myrosinases (EC 3.2.1.147) are enzymes known for the generation of hydrolysis products that have a potential beneficial effect on human health. Their reaction mechanisms are widely studied, in order to improve and optimize secondary metabolite production processes. In this work, kinetic and biochemical [...] Read more.

Myrosinases (EC 3.2.1.147) are enzymes known for the generation of hydrolysis products that have a potential beneficial effect on human health. Their reaction mechanisms are widely studied, in order to improve and optimize secondary metabolite production processes. In this work, kinetic and biochemical properties of the broccoli myrosinase enzyme produced from its cDNA cloned in Escherichia coli and Saccharomyces cerevisiae were investigated. The results revealed that the thermal stability of the enzyme produced in S. cerevisiae was slightly higher (30 to 60 °C) than that of myrosinase produced in E. coli (20 to 50 °C). The effect of pH on the enzymatic activity was similar in both enzymes, with pH 3 being the optimum value under the reaction conditions used. The kinetic behavior of both enzymes was adjusted to the Michaelis–Menten model. The catalytic efficiency was up to 4 times higher in myrosinase produced in S. cerevisiae, compared to myrosinase produced in E. coli. The glycosylations present in the enzyme would be related to the formation of a dimeric quaternary structure and would not play an essential role in enzymatic activity, since both enzymes were biologically active. These results will probably allow the development of strategies for the production of bioactive metabolites of medical interest. Full article

(This article belongs to the Topic Biomedical Applications of Enzymes)

►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less

Select all

Export citation of selected articles as:

Plain Text BibTeX BibTeX (without abstracts) Endnote Endnote (without abstracts) Tab-delimited RIS

 

Error

Oops... you haven't selected anything for export.

Ok

clear

Displaying articles 1-9