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Brazilian Journal of Microbiology :... Dec 2022Glutathione (GSH) and peroxidase (POD) are biomolecules of interest in the global market; thus, it is desirable to seek ways to increase their production. Magnetic field...
Glutathione (GSH) and peroxidase (POD) are biomolecules of interest in the global market; thus, it is desirable to seek ways to increase their production. Magnetic field (MF) application is one of the technologies used in cultivation that has shown promising results to increase bioproducts. Therefore, this study aimed at evaluating the influence of MFs on GSH and POD production by Saccharomyces cerevisiae ATCC 7754. Different periods of MF application (35 mT) were evaluated over 72 h. The highest GSH production was reached in 48 h of cultivation in assays MF 0-24 (155.32 ± 9.12 mg L) and MF 0-72 (149.27 ± 3.62 mg L), which showed an increase of 121.9 % and 113 %, respectively, by comparison with the control without any MF application. The highest POD activity was achieved when MFs were applied throughout the culture (36.31 U mg) and POD productivity of 0.72 U mg h. MF application throughout cultivation proved to be a promising strategy since all responses increased, i.e., GSH concentration, GSH productivity, POD activity, and POD productivity increased 113.7 %, 113 %, 20.4 %, and 28.6 %, respectively. This study is one of the first to consider MFs as a viable and low-cost alternative to produce GSH and POD in bioprocesses.
Topics: Saccharomyces cerevisiae; Peroxidase; Glutathione; Peroxidases; Oxidoreductases; Magnetic Fields; Antioxidants
PubMed: 36199005
DOI: 10.1007/s42770-022-00836-9 -
Ultrasonics Sonochemistry Mar 2021The activation mechanism of peroxidase by ultrasound was investigated. The catalysis performance of peroxidase with ultrasound treatment was prior to the controls...
The activation mechanism of peroxidase by ultrasound was investigated. The catalysis performance of peroxidase with ultrasound treatment was prior to the controls determined by UV-visible spectra and Fourier transform infrared spectra. The transformation of tryptophan residues in peroxidase led to the increase of a-helix and anti-parallel content in the secondary structure, and the content of p-sheet, p-turn and random coil in the secondary structure. In addition, under the atomic force microscope, under ultrasonic treatment, the large molecular clusters of tyrosinase are broken down into small molecular clusters. The current results showed that the activity of peroxidase is activated under ultrasonic treatment, which is mainly caused by ultrasound without conformational change, the catalytic center is exposed, and the affinity with the substrate is stronger.
Topics: Enzyme Activation; Peroxidase; Spectrum Analysis; Ultrasonic Waves
PubMed: 33096324
DOI: 10.1016/j.ultsonch.2020.105362 -
Molecules (Basel, Switzerland) Jul 2022The peroxidase-like activity of vitamin B6 (VB6) was firstly demonstrated by catalyzing the peroxidase chromogenic substrate 3,3',5,5'-tetramethylbenzidine (TMB) at the...
The peroxidase-like activity of vitamin B6 (VB6) was firstly demonstrated by catalyzing the peroxidase chromogenic substrate 3,3',5,5'-tetramethylbenzidine (TMB) at the existence of HO. The influence of different factors on the catalytic property of VB6, including pH, temperature, VB6 concentration, and incubation time, were investigated. The steady-state kinetic study results indicate that VB6 possesses higher affinity to HO than natural horseradish peroxidase and some other peroxidase mimics. Besides, the radical quenching experiment results confirm that hydroxyl radical (•OH) accounts for the catalytic process. Based on the excellent peroxidase-like catalytic activity of VB6, the colorimetric methods for HO and gallic acid (GA) detection were developed by measuring the absorbance variance of the catalytic system. Under the optimal conditions, the linear ranges of the methods for HO and GA determination with good selectivity are 50.0-600.0 μM and 10.0-50.0 μM, respectively. In addition, the developed method was applied in the detection of HO in milk samples and evaluation of total antioxidant capacity of different tea infusions. This study may broaden the application prospect of VB6 in environmental and biomedical analysis fields, contribute to profound insight of the physiological functions of VB6, as well as lay foundation for further excavation of small-molecule peroxidase mimics.
Topics: Antioxidants; Biomimetic Materials; Colorimetry; Hydrogen Peroxide; Peroxidase; Peroxidases; Vitamin B 6
PubMed: 35807507
DOI: 10.3390/molecules27134262 -
Chemical Communications (Cambridge,... May 2020Graphdiyne (GDY) is a new recently-synthesized carbon allotrope. We find here that graphdiyne oxide (GDYO), the oxidized form of GDY, can serve as a new kind of carbon...
Graphdiyne (GDY) is a new recently-synthesized carbon allotrope. We find here that graphdiyne oxide (GDYO), the oxidized form of GDY, can serve as a new kind of carbon nanozyme mimicking peroxidase. This finding essentially offers a new platform for fundamental understanding of carbon nanozymes and broadens the application of GDY.
Topics: Carbon; Graphite; Nanostructures; Oxides; Particle Size; Peroxidase; Surface Properties
PubMed: 32319464
DOI: 10.1039/d0cc01840f -
Scientific Reports Aug 2023In recent years, the peroxidase enzymes have generated wide interest in several industrial processes, such as wastewater treatments, food processing, pharmaceuticals,...
In recent years, the peroxidase enzymes have generated wide interest in several industrial processes, such as wastewater treatments, food processing, pharmaceuticals, and the production of fine chemicals. However, the low stability of the peroxidases in the presence of hydrogen peroxide (HO) has limited its commercial use. In the present work, the effect of HO on the inactivation of horseradish peroxidase (HRP) was evaluated. Three states of HRP (E, E, and E) were identified. While in the absence of HO, the resting state E was observed, in the presence of low and high concentrations of HO, E and E were found, respectively. The results showed that HRP catalyzed the HO decomposition, forming the species E, which was catalytically inactive. Results suggest that this loss of enzymatic activity is an intrinsic characteristic of the studied HRP. A model from a modified version of the Dunford mechanism of peroxidases was developed, which was validated against experimental data and findings reported by the literature.
Topics: Horseradish Peroxidase; Hydrogen Peroxide; Kinetics; Peroxidases; Peroxidase
PubMed: 37591893
DOI: 10.1038/s41598-023-39687-1 -
ACS Applied Bio Materials Sep 2023Nanozymes are nanoparticles with intrinsic enzyme-mimicking properties that have become more prevalent because of their ability to outperform conventional enzymes by... (Review)
Review
Nanozymes are nanoparticles with intrinsic enzyme-mimicking properties that have become more prevalent because of their ability to outperform conventional enzymes by overcoming their drawbacks related to stability, cost, and storage. Nanozymes have the potential to manipulate active sites of natural enzymes, which is why they are considered promising candidates to function as enzyme mimetics. Several microscopy- and spectroscopy-based techniques have been used for the characterization of nanozymes. To date, a wide range of nanozymes, including catalase, oxidase, peroxidase, and superoxide dismutase, have been designed to effectively mimic natural enzymes. The activity of nanozymes can be controlled by regulating the structural and morphological aspects of the nanozymes. Nanozymes have multifaceted benefits, which is why they are exploited on a large scale for their application in the biomedical sector. The versatility of nanozymes aids in monitoring and treating cancer, other neurodegenerative diseases, and metabolic disorders. Due to the compelling advantages of nanozymes, significant research advancements have been made in this area. Although a wide range of nanozymes act as potent mimetics of natural enzymes, their activity and specificities are suboptimal, and there is still room for their diversification for analytical purposes. Designing diverse nanozyme systems that are sensitive to one or more substrates through specialized techniques has been the subject of an in-depth study. Hence, we believe that stimuli-responsive nanozymes may open avenues for diagnosis and treatment by fusing the catalytic activity and intrinsic nanomaterial properties of nanozyme systems.
Topics: Nanostructures; Nanoparticles; Peroxidase; Peroxidases; Microscopy
PubMed: 37590090
DOI: 10.1021/acsabm.3c00253 -
Journal of Inorganic Biochemistry Oct 2023The dehaloperoxidase-hemoglobin (DHP), first isolated from the coelom of a marine terebellid polychaete, Amphitrite ornata, is an example of a multi-functional heme... (Comparative Study)
Comparative Study
The dehaloperoxidase-hemoglobin (DHP), first isolated from the coelom of a marine terebellid polychaete, Amphitrite ornata, is an example of a multi-functional heme enzyme. Long known for its reversible oxygen (O) binding, further studies have established DHP activity as a peroxidase, oxidase, oxygenase, and peroxygenase. The specific reactivity depends on substrate binding at various internal and external binding sites. This study focuses on comparison of the binding and reactivity of the substrate 2,4-dichlorophenol (DCP) in the isoforms DHPA and B. There is strong interest in the degradation of DCP because of its wide use in the chemical industry, presence in waste streams, and particular reactivity to form dioxins, some of the most toxic compounds known. The catalytic efficiency is 3.5 times higher for DCP oxidation in DHPB than DHPA by a peroxidase mechanism. However, DHPA and B both show self-inhibition even at modest concentrations of DCP. This phenomenon is analogous to the self-inhibition of 2,4,6-trichlorophenol (TCP) at higher concentration. The activation energies of the electron transfer steps in DCP in DHPA and DHPB are 19.3 ± 2.5 and 24.3 ± 3.2 kJ/mol, respectively, compared to 37.2 ± 6.5 kJ/mol in horseradish peroxidase (HRP), which may be a result of the more facile electron transfer of an internally bound substrate in DHPA. The x-ray crystal structure of DHPA bound with DCP determined at 1.48 Å resolution, shows tight substrate binding inside the heme pocket of DHPA (PDB 8EJN). This research contributes to the studies of DHP as a naturally occurring bioremediation enzyme capable of oxidizing a wide range of environmental pollutants.
Topics: Chlorophenols; Coloring Agents; Heme; Peroxidase; Peroxidases; Phenols
PubMed: 37480762
DOI: 10.1016/j.jinorgbio.2023.112332 -
Chemistry (Weinheim An Der Bergstrasse,... Mar 2022Carbon dots (CDs) have recently emerged as antibacterial agents and have attracted considerable attention owing to their fascinating merits of small size, facile...
Carbon dots (CDs) have recently emerged as antibacterial agents and have attracted considerable attention owing to their fascinating merits of small size, facile fabrication, and surface functionalization. Most of them are involved in external light activation or hybridization with other functional nanomaterials. Herein, we present peroxidase-like Cu-doped CDs (Cu-CDs) for in vitro antibacterial applications. The unique peroxidase-mimicking property of the Cu-CDs was demonstrated by tetramethylbenzidine chromogenic assay, electron paramagnetic resonance spectra, and hydroxy radical probe. Escherichia coli and Staphylococcus aureus were chosen as representative gram-negative/positive models against which Cu-CDs exhibited superior antimicrobial activity even at a dosage down to 5 μg/mL. A possible mechanism of action was that the Cu-CDs triggered a catalytic redox reaction of endogenous H O and glutathione depletion in the bacteria cells, with subsequent oxidative stress and membrane disruption. This work provides a new strategy for the design of microenvironment-responsive antimicrobial nano-agents.
Topics: Anti-Bacterial Agents; Carbon; Copper; Oxidative Stress; Peroxidase; Peroxidases; Quantum Dots
PubMed: 35083795
DOI: 10.1002/chem.202104174 -
Biosensors Oct 2022Nanozymes, as artificial enzymes with the biological action of natural enzymes, have enormous potential in the fields of disease diagnosis, bacteriostasis, biosensing,...
Nanozymes, as artificial enzymes with the biological action of natural enzymes, have enormous potential in the fields of disease diagnosis, bacteriostasis, biosensing, etc. In this work, the NiCuS nanoflower was successfully synthesized through a one-step hydrothermal method. A combined strategy of Ni doping and morphology design was employed to adjust its electronic structure and active sites, endowing the NiCuS nanoflower with excellent peroxidase-like activity. Therefore, it can catalyze the decomposition of HO to generate •OH with higher antibacterial activity, establishing a broad-spectrum antibacterial system based on the NiCuS nanoflower against and , which avoids the harm of a high concentration of HO. Additionally, the colorless substrate TMB can be catalytically oxidized into blue ox-TMB via •OH. As a result, a colorimetric technique with rapid and accurate detection of ascorbic acid (AA) by the unaided eye was designed, in view of the specific inhibition effect towards the oxidation of TMB. This detection platform has a wide linear range (10~800 μM) with a low limit of detection (0.84 μM) and exhibits a satisfactory selectivity toward the detection of AA. This study sheds new light on the application of copper-containing nanozymes in the fields of biomedicine and bioassay.
Topics: Peroxidase; Hydrogen Peroxide; Copper; Staphylococcus aureus; Escherichia coli; Peroxidases; Ascorbic Acid; Anti-Bacterial Agents; Biosensing Techniques
PubMed: 36291011
DOI: 10.3390/bios12100874 -
Anais Da Academia Brasileira de Ciencias 2023The present study aimed to investigate the response of soybean cultivars with different susceptibility levels to the root-knot nematode Meloidogyne javanica at varied...
The present study aimed to investigate the response of soybean cultivars with different susceptibility levels to the root-knot nematode Meloidogyne javanica at varied time intervals by analyzing the initial plant-nematode interaction using antioxidant enzymes as oxidative stress markers. A 4 × 4 × 2 factorial method with 5 repetitions was used to analyze 4 soybean cultivars at 4 different collection times-6, 12, 24, and 48 h-with and without M. javanica inoculation. The parameters evaluated were the activities of antioxidant enzymes phenol peroxidase (POX) and ascorbate peroxidase (APX); the concentrations of hydrogen peroxide (H2O2) and malondialdehyde (MDA); and the number of M. javanica juveniles penetrated into each plant. H2O2 concentration varied among the cultivars with and without inoculation and at different collection times as indicated by MDA concentration and POX and APX activities, demonstrating a rapid response of the host to an infection by M. javanica. Oxidative stress caused by M. javanica did not vary among the soybean cultivars regardless of their susceptibility level; however, the antioxidant enzymes POX and APX responded according to the susceptibility level of the cultivars.
Topics: Animals; Antioxidants; Glycine max; Tylenchoidea; Hydrogen Peroxide; Oxidative Stress; Peroxidases; Peroxidase; Ascorbate Peroxidases
PubMed: 37436197
DOI: 10.1590/0001-3765202320201328