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1.
Biomolecules ; 14(6)2024 Jun 14.
Artigo em Inglês | MEDLINE | ID: mdl-38927099

RESUMO

The antioxidant defense mechanisms play a critical role in mitigating the deleterious effects of reactive oxygen species (ROS). Catalase stands out as a paramount enzymatic antioxidant. It efficiently catalyzes the decomposition of hydrogen peroxide (H2O2) into water and oxygen, a potentially harmful byproduct of cellular metabolism. This reaction detoxifies H2O2 and prevents oxidative damage. Catalase has been extensively studied as a therapeutic antioxidant. Its applications range from direct supplementation in conditions characterized by oxidative stress to gene therapy approaches to enhance endogenous catalase activity. The enzyme's stability, bioavailability, and the specificity of its delivery to target tissues are significant hurdles. Furthermore, studies employing conventional catalase formulations often face issues related to enzyme purity, activity, and longevity in the biological milieu. Addressing these challenges necessitates rigorous scientific inquiry and well-designed clinical trials. Such trials must be underpinned by sound experimental designs, incorporating advanced catalase formulations or novel delivery systems that can overcome existing limitations. Enhancing catalase's stability, specificity, and longevity in vivo could unlock its full therapeutic potential. It is necessary to understand the role of catalase in disease-specific contexts, paving the way for precision antioxidant therapy that could significantly impact the treatment of diseases associated with oxidative stress.


Assuntos
Antioxidantes , Catalase , Estresse Oxidativo , Catalase/metabolismo , Catalase/química , Humanos , Estresse Oxidativo/efeitos dos fármacos , Animais , Antioxidantes/metabolismo , Espécies Reativas de Oxigênio/metabolismo , Peróxido de Hidrogênio/metabolismo , Terapia Genética/métodos
2.
Food Chem ; 455: 139889, 2024 Oct 15.
Artigo em Inglês | MEDLINE | ID: mdl-38833865

RESUMO

The development of nondestructive technology for the detection of seed viability is challenging. In this study, to establish a green and effective method for the viability assessment of single maize seeds, a two-stage seed viability detection method was proposed. The catalase (CAT) activity and malondialdehyde (MDA) content were selected as the most key biochemical components affecting maize seed viability, and regression prediction models were developed based on their hyperspectral information and a data fusion strategy. Qualitative discrimination models for seed viability evaluation were constructed based on the predicted response values of the selected key biochemical components. The results showed that the double components thresholds strategy achieved the highest discrimination accuracy (92.9%), providing a crucial approach for the rapid and environmentally friendly detection of seed viability.


Assuntos
Catalase , Malondialdeído , Sementes , Zea mays , Zea mays/química , Zea mays/metabolismo , Zea mays/crescimento & desenvolvimento , Sementes/química , Sementes/crescimento & desenvolvimento , Sementes/metabolismo , Malondialdeído/metabolismo , Malondialdeído/análise , Catalase/metabolismo , Catalase/química , Proteínas de Plantas/metabolismo , Proteínas de Plantas/química , Germinação , Química Verde
3.
Food Chem Toxicol ; 160: 112801, 2022 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-34974130

RESUMO

In this research retrieval effects of natural yellow (NY) on the performance of carmoisine (CAR) inhibited bovine liver catalase (BLC) was studied using multispectral and theoretical methods. Kinetic studies showed that CAR inhibited BLC through competitive inhibition (IC50 value of 2.24 × 10-6 M) while the addition of NY recover the activity of CAR-BLC up to 82% in comparison with the control enzyme. Circular dichroism data revealed that NY can repair the structural changes of BLC, affected by CAR. Furthermore, an equilibrium dialysis study indicated that NY could reduce the stability of the CAR-catalase complex. The surface plasmon resonance (SPR) data analysis indicated a high affinity of NY to BLC compared to CAR and the binding of NY led to a decrease in the affinity of the enzyme to the inhibitor. On the other hand, fluorescence and molecular docking studies showed that the quenching mechanism of BLC by CAR occurs through a static quenching process, and van der Waals forces and hydrogen bonding play a crucial role in the binding of CAR to BLC. MLSD data demonstrated that NY could increase the binding energy of CAR-BLC complex from -7.72 kJ mol-1 to -5.9 kJ mol-1, leading to complex instability and catalase activity salvage.


Assuntos
Catalase/antagonistas & inibidores , Catalase/química , Curcumina/química , Corantes de Alimentos/química , Naftalenossulfonatos/química , Animais , Bovinos , Dicroísmo Circular , Proposta de Concorrência , Ligação de Hidrogênio , Cinética , Simulação de Acoplamento Molecular , Ressonância de Plasmônio de Superfície
4.
Environ Sci Pollut Res Int ; 27(7): 7280-7288, 2020 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-31883072

RESUMO

In this study, crucian carp (Carassius auratus) was exposed to the increasing concentrations of municipal sewage treatment plant effluent (MSTPE) for 15 days, and the activities of antioxidant enzymes including superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), and acetylcholinesterase (AChE), together with the contents of malondialdehyde (MDA) and glutathione (GSH) in the liver of C. auratus were investigated. Moreover, the integrated biomarker response (IBR) approach was applied to assess the adverse effects of MSTPE in freshwater. The aim of the study was to provide an effective biological indicator for evaluating the toxicity effects and ecological risks of MSTPE in the freshwater environment quantitatively. Results showed that MSTPE could cause oxidative damage to the liver of C. auratus, which reflected through the increasing MDA content over the exposure period. MSTPE also led to the biochemical responses of antioxidant defense in C. auratus liver, such as the enhancement of SOD, CAT, and GPx activities, as well as the inhibition of AChE activity and GSH content. It was found that MDA, SOD, GPx, and GSH could be used as the biomarkers for reflecting the adverse effects of MSTPE in the receiving freshwater on the 12th day of exposure. A significant increase of IBR values was observed as the increasing concentration of MSTPE, and the IBR values presented a significant positive correlation (r = 0.891, P < 0.05) with the increasing concentrations of MSTPE, indicating that IBR approach is a promising tool for assessing the toxicity effects of MSTPE in environmental freshwater.


Assuntos
Carpas , Catalase/química , Fígado/química , Superóxido Dismutase/química , Poluentes Químicos da Água , Animais , Biomarcadores , Carpa Dourada , Esgotos
5.
Biosci Biotechnol Biochem ; 84(1): 118-125, 2020 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-31516066

RESUMO

We developed an enzymatic assay system enabling easy quantification of 4-aminobutyric acid (GABA). The reaction of GABA aminotransferase obtained from Streptomyces decoyicus NBRC 13977 was combined to those of the previously developed glutamate assay system using glutamate oxidase and peroxidase. The three-enzyme system allowing GABA-dependent dye formation due to the oxidative coupling between 4-aminoantipyrine and Trinder's reagent enabled accurate quantification of 0.2 - 150 mg/L GABA. A pretreatment mixture consisting of glutamate oxidase, ascorbate oxidase and catalase eliminating glutamate, ascorbate, and hydrogen peroxide, respectively, was also prepared to remove those inhibitory substances from samples. Thus, constructed assay kit was used to measure the GABA content in tomato samples. The results were almost the same as that obtained by the conventional method using liquid chromatography-tandem mass spectrometry. The kit will become a promising tool especially for the on-site measurement of GABA content in agricultural products.


Assuntos
4-Aminobutirato Transaminase/química , Aminoácido Oxirredutases/química , Colorimetria/métodos , Ensaios Enzimáticos/métodos , Peroxidase/química , Ácido gama-Aminobutírico/análise , Ampirona/química , Ascorbato Oxidase/química , Catalase/química , Cromatografia Líquida , Ensaios Enzimáticos/economia , Compostos Férricos/química , Ácido Glutâmico/química , Peróxido de Hidrogênio/química , Solanum lycopersicum/química , Acoplamento Oxidativo , Proteínas Recombinantes , Streptomyces/enzimologia , Espectrometria de Massas em Tandem
6.
Chemosphere ; 207: 725-741, 2018 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-29859485

RESUMO

The present study aimed to evaluate the responses of different biochemicals parameters associated with environmental pollution in the digestive gland of the gastropod mollusc Stramonita haemastoma. Physiochemical parameters and trace metal elements (Copper (Cu), Zinc (Zn), Chromium (Cr), Cadmium (Cd) and Lead (Pb)) were measured in seawater. Spatiotemporal variations in reduced glutathione (GSH), malondialdehyde (MDA) and metallothionein (Mt) as well as the specific activities of glutathione S-transferase (GST) and catalase (CAT) were evaluated in digestive gland of this species during a one-year period in 2013-2014. Samples collection was conducted at three sites. The results obtained showed seasonal fluctuations in GST and CAT activities and in the rate of Mt content. In addition, intersite variations in GSH, MDA, Mt and CAT were recorded in individuals. Also, trace metal elements concentrations determined by season in the digestive gland revealed spatial and temporal variations for Cu and Zn but they are below the limit of detection for Cd and Pb. The highest values were generally recorded in spring for Cu and in winter for Zn. In this first regional study using in S. haemastoma as a model, the biomarkers measured were seen to be inducible parameters to evaluate the health state of the organism and the overall quality of the study sites.


Assuntos
Catalase/química , Biomarcadores Ambientais/fisiologia , Glutationa/química , Malondialdeído/química , Metalotioneína/química , Metais/efeitos adversos , Oligoelementos/química , Mar Mediterrâneo
7.
Talanta ; 144: 915-21, 2015 Nov 01.
Artigo em Inglês | MEDLINE | ID: mdl-26452908

RESUMO

Creatinine is one of many markers used to investigate kidney function. This paper describes a low-cost enzymatic paper-based analytical device (enz-PAD) for determining urine creatinine. The disposable dead volumes of creatinine enzyme reagents from an automatic analyser cassette were utilised. Whatman No. 3 paper was cut into long rectangular shapes (4×40 mm(2)) on which the enzyme reagents, R1 and R2, were adsorbed in two consecutive regions. The assay was performed by immersing test strips into urine samples contained in microwells to allow creatinine in the sample to react with immobilised active ingredients and, then, traverse via capillary action to the detection area where chromogen products accumulated. The method is based on hydrogen peroxide (H2O2) formation via creatinine conversion using creatininase, creatinase, and sarcosine oxidase. The liberated H2O2 reacts with 4-aminophenazone and 2,4,6-triiodo-3-hydroxybenzoic acid to form quinoneimine with a pink-red colour at the detection zone. The linear range of the creatinine assay was 2.5-25 mg dL(-1) (r(2)=0.983), and the detection limit was 2.0 mg dL(-1). The colorimetric enz-PAD for the creatinine assay was highly correlated with a conventional alkaline picrate method when real urine samples were evaluated (r(2)=0.977; n=40). This simple and nearly zero-cost paper-based device provides a novel alternative method for screening urinary creatinine and will be highly beneficial for developing countries.


Assuntos
Creatinina/urina , Ensaios Enzimáticos/métodos , Papel , Ascorbato Oxidase/química , Catalase/química , Colorimetria/métodos , Custos e Análise de Custo , Creatinina/química , Ensaios Enzimáticos/economia , Humanos , Peroxidase/química , Sarcosina Oxidase/química , Ureo-Hidrolases/química
8.
J Pharm Sci ; 104(11): 3710-3721, 2015 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-26305147

RESUMO

Microscale (MS) freeze-drying offers rapid process cycles for early-stage formulation development. The effects of the MS approach on the secondary structures of two model proteins, lysozyme and catalase, were compared with pilot-scale (PS) vial freeze-drying. The secondary structures were assessed by attenuated total reflection Fourier transformed infrared spectroscopy. Formulations were made with increasing sucrose-protein ratios. Freeze-drying protocols involved regular cooling without thermal treatment and annealing with MS and PS equipment, and cooling rate variations with the MS. Principal component analysis of smoothed second-derivative amide I spectra revealed sucrose-protein ratio-dependent shifts toward α-helical structures. Transferability of sucrose-protein formulations from MS to PS vial freeze-drying was evidenced at regular cooling rates. Local differences in protein secondary structures between the bottom and top of sucrose-catalase samples could be detected at the sucrose-catalase ratios of 1 and 2, this being related to the initial filling height and ice crystal morphology. Annealing revealed temperature, protein, formulation, and sample location-dependent effects influencing surface morphology at the top, or causing protein secondary structure perturbation at the bottom. With the MS approach, protein secondary structure differences at different cooling rates could be detected for sucrose-lysozyme samples at the sucrose-lysozyme ratio of 1.


Assuntos
Catalase/química , Liofilização/métodos , Muramidase/química , Animais , Bovinos , Galinhas , Excipientes/química , Liofilização/economia , Análise de Componente Principal , Estrutura Secundária de Proteína , Sacarose/química
9.
Acta Crystallogr D Biol Crystallogr ; 70(Pt 3): 647-57, 2014 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-24598734

RESUMO

Increasing the probability of obtaining protein crystals in crystallization screening is always an important goal for protein crystallography. In this paper, a new method called the cross-diffusion microbatch (CDM) method is presented, which aims to efficiently promote protein crystallization and increase the chance of obtaining protein crystals. In this method, a very simple crystallization plate was designed in which all crystallization droplets are in one sealed space, so that a variety of volatile components from one droplet can diffuse into any other droplet via vapour diffusion. Crystallization screening and reproducibility tests indicate that this method could be a potentially powerful technique in practical protein crystallization screening. It can help to obtain crystals with higher probability and at a lower cost, while using a simple and easy procedure.


Assuntos
Cristalização/métodos , Proteínas/química , Acetiltransferases/química , Acetiltransferases/genética , Animais , Catalase/química , Galinhas , Quimotripsinogênio/química , Concanavalina A/química , Cristalização/economia , Muramidase/química , Proteínas/economia , Proteínas Recombinantes/química , Reprodutibilidade dos Testes
10.
Bioresour Technol ; 101(14): 5213-21, 2010 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-20206510

RESUMO

Activated sludge is widely used to treat industrial wastewater, but its efficiency is affected by a variety of factors, including toxic substances such as tetrahydrofuran (THF). In this study, we examined the toxicity of THF at different concentrations (0-320 mM) on the microbial community in activated sludge. A remarkable dose-dependent decrease in the total organic compound removal rate and culturable bacteria and fungi was observed. At THF concentrations higher than 160 mM, a decrease in pH to 3.0 was observed. The activities of five enzymes (catalase, dehydrogenase, urease, phosphatase and protease) analyzed were all significantly inhibited (p<0.01) at THF concentrations higher than 160 mM, especially dehydrogenase activity, which lost 95.4% of its activity at 320 mM THF. Microbial community analysis by PCR-DGGE revealed a substantial shift in the community structure and a reduction in diversity at a low THF concentration (20mM). These results suggest that THF is much more toxic than reported in the literature, indicating its acute toxicity to microorganisms.


Assuntos
Técnicas Microbiológicas/métodos , Poluentes Químicos da Água/análise , Purificação da Água/métodos , Catalase/química , Análise por Conglomerados , Furanos/toxicidade , Concentração de Íons de Hidrogênio , Compostos Orgânicos/química , Oxirredutases/química , Monoéster Fosfórico Hidrolases/química , Filogenia , Esgotos , Urease/química
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