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1.
Chinese Journal of Biotechnology ; (12): 4215-4230, 2021.
Article in Chinese | WPRIM | ID: wpr-921500

ABSTRACT

Threonine aldolases catalyze the aldol condensation of aldehydes with glycine to furnish β-hydroxy-α-amino acid with two stereogenic centers in a single reaction. This is one of the most promising green methods for the synthesis of optically pure β-hydroxy-α-amino acid with high atomic economy and less negative environmental impact. Several threonine aldolases from different origins have been identified and characterized. The insufficient -carbon stereoselectivity and the challenges of balancing kinetic versus thermodynamic control to achieve the optimal optical purity and yield hampered the application of threonine aldolases. This review summarizes the recent advances in discovery, catalytic mechanism, high-throughput screening, molecular engineering and applications of threonine aldolases, with the aim to provide some insights for further research in this field.


Subject(s)
Amino Acids , Catalysis , Glycine , Glycine Hydroxymethyltransferase/metabolism , Kinetics , Substrate Specificity , Threonine
2.
Chinese Journal of Biotechnology ; (12): 4169-4186, 2021.
Article in Chinese | WPRIM | ID: wpr-921497

ABSTRACT

Glycoside compounds are widely used in medicine, food, surfactant, and cosmetics. The glycosidase-catalyzed synthesis of glycoside can be operated at mild reaction conditions with low material cost. The glycosidase-catalyzed processes include reverse hydrolysis and transglycosylation, appropriately reducing the water activity in both processes may effectively improve the catalytic efficiency of glucosidase. However, glucosidase is prone to be deactivated at low water activity. Thus, glucosidase was immobilized to maintain its activity in the low water activity environment, and even in neat organic solvent system. This article summarizes the advances in glycosidase immobilization in the past 30 years, including single or comprehensive immobilization techniques, and immobilization techniques combined with genetic engineering, with the aim to provide a reference for the synthesis of glycosides using immobilized glycosidases.


Subject(s)
Catalysis , Enzymes, Immobilized , Glycoside Hydrolases/genetics , Glycosides/biosynthesis , Hydrolysis
3.
Chinese Journal of Biotechnology ; (12): 4015-4023, 2021.
Article in Chinese | WPRIM | ID: wpr-921482

ABSTRACT

Metal-organic frameworks (MOFs) are formed by self-assembly of metal ions or clusters with organic ligands, and are widely used in the fields of catalysis, sensing, energy and biomedicine. Recently, biological composites based on MOFs have attracted increasing attention. MOFs can be used as a platform for encapsulating bioactive substances due to the advantages such as large pore capacity, large specific surface area and diverse structure composition. These features can protect bioactive substances from adverse conditions, e.g. high temperature, high pressure, and organic solvents, thus improving the anti-adversity of bioactive substances. This review summarizes the advances of using MOFs as protective coatings to improve the anti-adversity of different bioactive substances, and introduces the synthesis strategy of MOFs-based biological composites, with the aim to promote the practical application of MOFs-based biological composites.


Subject(s)
Catalysis , Ions , Metal-Organic Frameworks , Metals
4.
Chinese Journal of Biotechnology ; (12): 2256-2271, 2021.
Article in Chinese | WPRIM | ID: wpr-887794

ABSTRACT

The development of biotechnology and the in-depth research on disease mechanisms have led to increased application of enzymes in the treatment of diseases. In addition, enzymes have shown great potential in drug manufacturing, particularly in production of non-natural organic compounds, due to the advantages of mild reaction conditions, high catalytic efficiency, high specificity, high selectivity and few side reactions. Moreover, the application of genetic engineering, chemical modification of enzymes and immobilization technologies have further improved the function of enzymes. This review summarized the advances of using enzymes as drugs for disease treatment or as catalysts for drug manufacturing, followed by discussing challenges, potential solutions and future perspectives on the application of enzymes in the medical and pharmaceutical field.


Subject(s)
Biocatalysis , Biotechnology , Catalysis , Drug Compounding , Enzymes/metabolism
5.
Chinese Journal of Biotechnology ; (12): 541-560, 2021.
Article in Chinese | WPRIM | ID: wpr-878581

ABSTRACT

Nano-metallic materials are playing an important role in the application of medicine, catalysis, antibacterial and anti-toxin due to their obvious advantages, including nanocrystalline strengthening effect, high photo-absorptivity, high surface energy and single magnetic region performance. In recent years, with the increasing consumption of global petrochemical resources and the aggravation of environmental pollution, nanomaterials based on bio-based molecules have aroused great concern. Bio-based molecules refer to small molecules and macromolecules directly or indirectly derived from biomass. They usually have good biocompatibility, low toxicity, degradability, wide source and low price. Besides, most bio-based molecules have unique physical, chemical properties and physiological activity, such as optical activity, acid/alkali amphoteric property, hydrophilic property and easy coordination with metal ions. Thus, the corresponding nano-materials based on bio-based molecules also have unique functions, such as anti-inflammatory, anti-cancer, anti-oxidation, antiviral fall blood sugar and blood fat etc. In this paper, we give a comprehensive overview of the preparation and application of nano-metallic materials based on bio-based molecules in recent years.


Subject(s)
Anti-Infective Agents , Catalysis , Metals , Nanostructures
6.
Chinese Journal of Biotechnology ; (12): 868-878, 2020.
Article in Chinese | WPRIM | ID: wpr-826889

ABSTRACT

2-Haloacid dehalogenases (EC 3.8.1.X) catalyze the hydrolytic dehalogenation of 2-haloacids, releasing halogen ions and producing corresponding 2-hydroxyacids. The enzymes not only degrade xenobiotic halogenated pollutants, but also show wide substrate profile and astonishing efficiency for enantiomer resolution, making them valuable in environmental protection and the green synthesis of optically pure chiral compounds. A variety of 2-haloacid dehalogenases have been biochemically characterized so far. Further studies have been made in protein crystal structures and catalytic mechanisms. Here, we review the recent progresses of 2-haloacid dehalogenases in their source, protein structures, reaction mechanisms, catalytic properties and application. We also suggest further research directions for 2-haloacid dehalogenase.


Subject(s)
Catalysis , Halogenation , Hydrolases , Chemistry , Metabolism , Hydrolysis , Research , Substrate Specificity
7.
Chinese Journal of Biotechnology ; (12): 1346-1355, 2020.
Article in Chinese | WPRIM | ID: wpr-826842

ABSTRACT

Cytochrome P450 monooxygenases as powerful biocatalysts catalyze a wide range of chemical reactions to facilitate exogenous substances metabolism and biosynthesis of natural products. In order to explore new catalytic reactions and increase the number of P450 biocatalysts used in synthetic biology, a new self-sufficient cytochrome P450 monooxygenase (P450(VpMO)), belongs to CYP116B class, was mined from Variovorax paradoxus S110 genome and expressed in Escherichia coli. Based on characterization of the enzymatic properties, it shows that the optimal pH and temperature for P450(VpMO) reaction activity are 8.0 and 45 °C, respectively. P450(VpMO) is relatively stable at temperatures below 35 °C. The Km and kcat of P450(VpMO) toward 4-Methoxyacetophenone are 0.458 mmol/L and 2.438 min⁻¹, respectively. Importantly, P450(VpMO) was able to catalyze the demethylation reaction for a range of substrates containing methoxy group. Its demethylation reactivity is reasonably better than other P450s belongs to CYP116B class, particularly, for 4-methoxyacetophenone with a great conversion efficiency at 91%, showing that P450(VpMO) could be used as a great biocatalyst candidate for further analysis.


Subject(s)
Catalysis , Comamonadaceae , Genetics , Cytochrome P-450 Enzyme System , Genetics , Metabolism , Gene Expression , Synthetic Biology
8.
Chinese Journal of Biotechnology ; (12): 2732-2740, 2020.
Article in Chinese | WPRIM | ID: wpr-878525

ABSTRACT

Dihydroorotate dehydrogenase is a flavin-dependent mitochondrial enzyme to catalyze the fourth step of the de novo synthesis of pyrimidine and to oxidize dihydroorotate to orotate. By selectively inhibiting dihydroorotate dehydrogenase, thereby inhibiting pyrimidine synthesis, the enzyme has been developed for the treatment of cancer, autoimmune diseases, bacterial or viral infections, parasitic diseases and so on. The development of inhibitory drugs requires a detailed understanding of the structural characteristics and catalytic cycle mechanism of dihydroorotate dehydrogenase. Therefore, this paper reviews these two aspects, and indicates perspectives of these inhibitors in clinical application.


Subject(s)
Catalysis , Mitochondria/metabolism , Oxidation-Reduction , Oxidoreductases Acting on CH-CH Group Donors/metabolism
9.
Chinese Journal of Biotechnology ; (12): 2139-2150, 2020.
Article in Chinese | WPRIM | ID: wpr-878473

ABSTRACT

Thioredoxin reductase (TrxR) is one class of the most important antioxidant selenoproteins and is involved in regulating tumor genesis and progression. It has been reported that naphthoquinones can target and inhibit TrxR1 activity therefore produce reactive oxygen species (ROS) mediated by TrxR1, resulting into cellular redox imbalance and making the naphthoquinone compounds to become potential antitumor chemotherapy drugs. The purpose of this work is to explore the interaction between TrxR1 and menadione using biochemical and mass-spectrometric (MS) analyses, to further reveal the detailed mechanisms of TrxR1-mediated naphthoquinone reduction and inhibition of TrxR1 by naphthoquinone compounds. Using the site-directed mutagenesis and recombinantly expressed TrxR1 variants, we measured the steady-state kinetic parameters of menadione reduction mediated by TrxR1 and its variants, performed the inhibition analysis of menadione on TrxR1 activity, and eventually identified the interaction between menadione and TrxR1 through MS analysis. We found that Sec-to-Cys mutation at residue of 498 significantly enhanced the efficiency of TrxR1-mediated menadione reduction, though the Sec⁴⁹⁸ is capable to catalyze the menadione reduction, indicating that TrxR1-mediated menadione reduction is dominantly in a Se-independent manner. Mutation experiments showed that Cys⁴⁹⁸ is mainly responsible for menadione catalysis in comparison to Cys⁴⁹⁷, while the N-terminal Cys⁶⁴ is slightly stronger than Cys⁵⁹ regarding the menadione reduction. LC-MS results detected that TrxR1 was arylated with one molecule of menadione, suggesting that menadione irreversibly modified the hyper-reactive Sec residue at the C-terminus of selenoprotein TrxR1. This study revealed that TrxR1 catalyzes the reduction of menadione in a Se-independent manner meanwhile its activity is irreversibly inhibited by menadione. Hereby it will be useful for the research and development of naphthoquinone anticancer drugs targeting TrxR1.


Subject(s)
Catalysis , Drug Development , Oxidation-Reduction , Thioredoxin Reductase 1/metabolism , Vitamin K 3/metabolism
10.
Chinese Journal of Biotechnology ; (12): 2001-2016, 2020.
Article in Chinese | WPRIM | ID: wpr-878461

ABSTRACT

Pictet-Spenglerases (P-Sases) catalyze the Pictet-Spengler (P-S) reactions and exhibit high stereoselectivity and regioselectivity under mild conditions. The typical P-S reaction refers to the condensation and recyclization of β-arylethylamine with aldehyde or ketone under acidic conditions to form tetrahydroisoquinoline and β-carboline alkaloid derivatives. The related enzymatic products of P-Sases are the backbones of various bioactive compounds, including clinical drugs: morphine, noscapine, quinine, berberine, ajmaline, morphine. Furthermore, the activity of P-Sases in stereoselective and regioselective catalysis is also valuable for chemoenzymatic synthesis. Therefore, this review summarizes the research progress in the discovery, functional identification, biological characteristics and catalytic applications of P-Sases, which provide the useful theoretical reference in future P-Sases research and development.


Subject(s)
Alkaloids/chemistry , Catalysis , Enzymes/metabolism , Research/trends , Tetrahydroisoquinolines/chemistry
11.
Braz. arch. biol. technol ; 63: e20180573, 2020. tab, graf
Article in English | LILACS | ID: biblio-1132185

ABSTRACT

Abstract This work reports the study of the potential application of Zn/TiO2 catalysts, obtained by the sol-gel method, in processes of environmental decontamination through the reactions of photodegradation of textile dye, followed by electrospray mass spectrometry. The catalysts synthesis was performed according to a 2² factorial design with repetition at the central point. The characterization techniques used were: N2 adsorption measurements (BET method), scanning electron microscopy with energy dispersive X-ray (MEV/EDS), X-ray diffraction and point of zero charge (PZC). The photocatalytic tests were performed in batch in the presence of sunlight, and to evaluate the degradation kinetics study, a rapid direct injection electrospray mass spectrometry (DI-ESI-MS) method has been developed. By the photocatalytic tests, the calcination temperature of 400 °C has shown the best results of discoloration for the reactive Orange-122 dye (99.76%) in a reaction time of 2h. The discoloration kinetics were a pseudo-first order, and a statistical analysis was performed to investigate the effects of the variables and to optimize the conditions of discoloration to the dye. After the reactional time of 2 h, an ion of m/z 441.5 was detected by ESI-MS, indicating that the photocatalytic process was effective for the degradation of the dye to secondary compounds.


Subject(s)
Azo Compounds/toxicity , Biodegradation, Environmental , Decontamination/methods , Tandem Mass Spectrometry/methods , Environmental Restoration and Remediation/methods , Waste Water , Photochemistry , Textiles/toxicity , Microscopy, Electron, Scanning , Catalysis , Catalytic Domain , Spectrometry, Mass, Electrospray Ionization , Coloring Agents , Photobioreactors , Models, Theoretical
12.
Braz. arch. biol. technol ; 63: e20180614, 2020. tab, graf
Article in English | LILACS | ID: biblio-1132182

ABSTRACT

Abstract The organic compound caffeine when detected in environmental matrices such as surface waters and groundwater is considered as an emerging contaminant, in which its effects are still unknown. Therefore, in the present research, zinc oxide-based catalysts impregnated with iron and silver were prepared for the reaction of caffeine degradation by heterogeneous photocatalysis. The wet impregnation method with excess solvent was applied to the preparation of the materials, later they were characterized by adsorption of N2, X-ray diffraction and photoacoustic spectroscopy. Then, the photodegradation, photolysis and adsorption tests were carried out, in which it was observed that only the presence of the radiation or photocatalysts could not sufficiently degrade the caffeine, however when combined radiation with all the catalysts studied here presented degradation above 70% at the end of 300 minutes of the reaction, and the best catalyst studied was that containing 8% Ag in non-calcined ZnO. Thus, these results point out that the methodology employed in this research, both for the preparation of the catalysts and in the process of the photocatalysis reaction, was efficient in the degradation of the emerging contaminant, caffeine, which could later be used for a mixture of other contaminants.


Subject(s)
Silver/chemistry , Zinc Oxide/chemistry , Caffeine/chemistry , Catalysis , Photochemical Processes , Adsorption , Bioreactors , Iron/chemistry
13.
Chinese Journal of Biotechnology ; (12): 351-362, 2019.
Article in Chinese | WPRIM | ID: wpr-771371

ABSTRACT

Baeyer-Villiger monooxygenases, a well-studied class of flavin-dependent enzymes, catalyze the conversion of ketones to lactones or esters and the oxygenation of heteroatoms, which possesses great practical prospect in synthetic chemistry and biocatalysis. In this review, we focus on Baeyer-Villiger oxidations involved in biosynthesis of microbial secondary metabolites and discuss the characteristics of these Baeyer-Villiger oxidations and Baeyer-Villiger monooxygenases, to provide reference for the protein engineering of Baeyer-Villiger monooxygenases.


Subject(s)
Biocatalysis , Catalysis , Mixed Function Oxygenases , Oxidation-Reduction , Protein Engineering
14.
Chinese Journal of Biotechnology ; (12): 816-826, 2019.
Article in Chinese | WPRIM | ID: wpr-771328

ABSTRACT

A new method to express oligomerized feruloyl esterase (FAE) in Pichia pastoris GS115 to improve the catalytic efficiency was developed. It was realized by fusing the foldon domain at the C-terminus of FAE, and the fusion protein was purified by histidine tag. Fusion of the feruloyl esterase with the foldon domain resulted spontaneously forming a trimer FAE to improve the catalytic performance. The oligomerized FAE and monomeric FAE were obtained by purification. The apparent molecular weight of the oligomerized FAE was about 110 kDa, while the monomeric FAE about 40 kDa, and the optimum temperature of the oligomerized FAE was 50 °C, which is the same as the monomeric one. The optimal pH of the oligomerized FAE is 5.0, while the optimal pH of the monomer FAE is 6.0. When compared with the monomeric ones, the catalytic efficiency (kcat/Km) of the oligomerized FAE increased 7.57-folds. The catalytic constant (kcat) of the oligomerized FAE increased 3.42-folds. The oligomerized FAE induced by foldon have advantages in the catalytic performances, which represents a simple and effective enzyme-engineering tool. The method proposed here for improving the catalytic efficiency of FAE would have great potentials for improving the catalytic efficiency of other enzymes.


Subject(s)
Carboxylic Ester Hydrolases , Metabolism , Catalysis , Molecular Weight , Pichia , Genetics , Metabolism , Polymerization , Protein Engineering , Substrate Specificity
15.
Electron. j. biotechnol ; 31: 10-16, Jan. 2018. graf, tab, ilust
Article in English | LILACS | ID: biblio-1022030

ABSTRACT

Background: Biodegradation is a reliable approach for efficiently eliminating persistent pollutants such as chlorpyrifos. Despite many bacteria or fungi isolated from contaminated environment and capable of degrading chlorpyrifos, limited enzymes responsible for its degradation have been identified, let alone the catalytic mechanism of the enzymes. Results: In present study, the gene cpd encoding a chlorpyrifos hydrolase was cloned by analysis of genomic sequence of Paracoccus sp. TRP. Phylogenetic analysis and BLAST indicated that CPD was a novel member of organophosphate hydrolases. The purified CPD enzyme, with conserved catalytic triad (Ser155-Asp251-His281) and motif Gly-Asp-Ser-Ala-Gly, was significantly inhibited by PMSF, a serine modifier. Molecular docking between CPD and chlorpyrifos showed that Ser155 was adjacent to chlorpyrifos, which indicated that Ser155 may be the active amino acid involved in chlorpyrifos degradation. This speculation was confirmed by site-directed mutagenesis of Ser155Ala accounting for the decreased activity of CPD towards chlorpyrifos. According to the key role of Ser155 in chlorpyrifos degradation and molecular docking conformation, the nucleophilic catalytic mechanism for chlorpyrifos degradation by CPD was proposed. Conclusion: The novel enzyme CPD was capable of hydrolyze chlorpyrifos and Ser155 played key role during degradation of chlorpyrifos.


Subject(s)
Paracoccus/enzymology , Chlorpyrifos/metabolism , Esterases/metabolism , Organophosphates/metabolism , Biodegradation, Environmental , Catalysis , Mutagenesis , Cloning, Molecular , Sequence Analysis , Esterases/isolation & purification , Esterases/genetics , Hydrolysis , Metals/metabolism
16.
Electron. j. biotechnol ; 28: 7-13, July. 2017. tab, graf, ilus
Article in English | LILACS | ID: biblio-1015723

ABSTRACT

Background: Laccases are copper-containing enzymes which have been used as green biocatalysts for many industrial processes. Although bacterial laccases have high stabilities which facilitate their application under harsh conditions, their activities and production yields are usually very low. In this work, we attempt to use a combinatorial strategy, including site-directed mutagenesis, codon and cultivation optimization, for improving the productivity of a thermo-alkali stable bacterial laccase in Pichia pastoris. Results: A D500G mutant of Bacillus licheniformis LS04 laccase, which was constructed by site-directed mutagenesis, demonstrated 2.1-fold higher activity when expressed in P. pastoris. The D500G variant retained similar catalytic characteristics to the wild-type laccase, and could efficiently decolorize synthetic dyes at alkaline conditions. Various cultivation factors such as medium components, pH and temperature were investigated for their effects on laccase expression. After cultivation optimization, a laccase activity of 347 ± 7 U/L was finally achieved for D500G after 3 d of induction, which was about 9.3 times higher than that of wild-type enzyme. The protein yield under the optimized conditions was about 59 mg/L for D500G. Conclusions: The productivity of the thermo-alkali stable laccase from B. licheniformis expressed in P. pastoris was significantly improved through the combination of site-directed mutagenesis and optimization of the cultivation process. The mutant enzyme retains good stability under high temperature and alkaline conditions, and is a good candidate for industrial application in dye decolorization.


Subject(s)
Pichia/metabolism , Laccase/biosynthesis , Laccase/genetics , Bacillus licheniformis/enzymology , Temperature , Yeasts , Enzyme Stability , Catalysis , Mutagenesis , Laccase/metabolism , Coloring Agents/metabolism , Hydrogen-Ion Concentration
17.
Electron. j. biotechnol ; 28: 87-94, July. 2017. tab, graf
Article in English | LILACS | ID: biblio-1015957

ABSTRACT

Background: Inferior Tieguanyin oolong tea leaves were treated with tannase. The content and bioactivity of catechins in extracts from the treated tea leaves were investigated to assess the improvement in the quality of inferior Tieguanyin oolong tea. Results: Analysis showed that after treatment, the esterified catechin content decreased by 23.5%, whereas non-galloylated catechin and gallic acid contents increased by 15.3% and 182%, respectively. The extracts from tannase-treated tea leaves showed reduced ability to bind to BSA and decreased tea cream levels. The extracts also exhibited increased antioxidant ability to scavenge OH and DPPH radicals, increased ferric reducing power, and decreased inhibitory effects on pancreatic α-amylase and lipase activities. Conclusions: These results suggested that tannase treatment could improve the quality of inferior Tieguanyin oolong tea leaves.


Subject(s)
Tea/enzymology , Carboxylic Ester Hydrolases/metabolism , Tea/metabolism , Tea/chemistry , Temperature , Catalysis , Catechin/analysis , Plant Leaves/enzymology , Fermentation , Hydrolysis , Lipase/antagonists & inhibitors , Lipase/metabolism , Antioxidants
18.
Electron. j. biotechnol ; 25: 13-20, ene. 2017. ilus, graf
Article in English | LILACS | ID: biblio-1008291

ABSTRACT

Background: A simple and efficient strategy for agarase immobilization was developed with carboxyl-functionalized magnetic nanoparticles (CMNPs) as support. The CMNPs and immobilized agarase (agarase-CMNPs) were characterized by transmission electron microscopy, dynamic light scattering, vibrating sample magnetometry, scanning electron microscopy, X-ray diffraction, thermogravimetric analysis, and zeta-potential analysis. The hydrolyzed products were separated and detected by ESI-TOF-MS. Results: The agarase-CMNPs exhibited a regular spherical shape with a mean diameter of 12 nm, whereas their average size in the aqueous solution was 43.7 nm as measured by dynamic light scattering. These results indicated that agarase-CMNPs had water swelling properties. Saturation magnetizations were 44 and 29 emu/g for the carriers and agarase-CMNPs, respectively. Thus, the particles had superparamagnetic characteristics, and agarase was successfully immobilized onto the supports. Agaro-oligosaccharides were prepared with agar as substrate using agarase-CMNPs as biocatalyst. The catalytic activity of agarase-CMNPs was unchanged after six reuses. The ESI-TOF mass spectrogram showed that the major products hydrolyzed by agarase-CMNPs after six recycle uses were neoagarotetraose, neoagarohexaose, and neoagarooctaose. Meanwhile, the end-products after 90 min of enzymatic treatment by agarase-CMNPs were neoagarobiose and neoagarotetraose. Conclusions: The enhanced agarase properties upon immobilization suggested that CMNPs can be effective carriers for agarase immobilization. Agarase-CMNPs can be remarkably used in developing systems for repeated batch production of agar-derived oligosaccharides.


Subject(s)
Oligosaccharides/metabolism , Enzymes, Immobilized , Magnetite Nanoparticles/chemistry , Glycoside Hydrolases/metabolism , Thermogravimetry , X-Ray Diffraction , Enzyme Stability , Catalysis , Microscopy, Electron, Transmission , Magnetometry , Dynamic Light Scattering , Glycoside Hydrolases/chemistry
19.
Article in English | WPRIM | ID: wpr-812557

ABSTRACT

The present study was designed to construct the structurally diverse library of tetrahydroprotoberberines (THPBs) by combining the methods of chemical nonselective demethylation and microbial glycosylation. HPLC-MS/MS analyses tentatively identified 12 de-methylated and 9 glycosylated derivates of THPBs and 5 rarely oxidized glycosides of THPBs in the library. Through this effort, we achieved not only a variety of the THPBs and their glycosides but also tested the catalytic characteristics and capabilities of G. deliquescens NRRL 1086.


Subject(s)
Berberine Alkaloids , Chemistry , Metabolism , Biotransformation , Catalysis , Gliocladium , Metabolism , Glycosides , Chemistry , Metabolism , Glycosylation , Molecular Structure
20.
Rev. bras. epidemiol ; 18(supl.2): 158-169, Out.-Dez. 2015. tab, graf
Article in English | LILACS | ID: lil-776701

ABSTRACT

RESUMO: Objetivo: Analisar as diferenças regionais e os fatores associados à prática de atividade física no lazer em adultos participantes da Pesquisa Nacional de Saúde, de 2013. Métodos: Este estudo foi realizado com os dados da Pesquisa Nacional de Saúde, realizada em 2013 com uma amostra aproximada de 63.000 adultos (18+ anos). Para cada uma das cinco regiões do Brasil foi calculada a prevalência de adultos ativos no lazer, sendo classificados como ativos aqueles participantes que praticaram pelo menos 150 minutos por semana de atividades físicas no lazer. Resultados: A prevalência de ativos no lazer variou de 21,9% no Sul a 24,4% no Centro-Oeste. Homens foram 1,48 (IC95% 1,40 - 1,57) vezes mais ativos que as mulheres, sendo a região Norte aquela que apresentou maior diferença entre sexos. A prevalência de ativos foi 67% menor entre aqueles com 75+ anos quando comparado ao grupo de 18-24 anos, sendo que esta diferença foi mais acentuada na região Norte. Aqueles com maior grau de instrução foram, em média, três vezes mais ativos que os participantes com menor grau de instrução. Em termos de grau de instrução, a menor diferença observada ocorreu no Nordeste. Conclusões: Apesar das pequenas variações na prevalência de prática de atividade física no lazer entre as regiões, quando são considerados subgrupos populacionais, diferenças importantes são observadas. Estes resultados sugerem a necessidade de ações de promoção de atividade física com diferentes abordagens em cada uma das cinco regiões do Brasil.


ABSTRACT: Objective: To analyze the regional differences and factors associated with physical activity during the leisure time in the adult participants of the National Health Survey, 2013. Methods: This study was carried out with the data from the National Health Survey, conducted in 2013 with an approximate sample of 63,000 adults (18+ years). For each of the five regions of Brazil, the prevalence of physically active adults during the leisure time was calculated, and the participants were classified as active if they practiced at least 150 minutes per week of physical activity during leisure time. Results: The prevalence of individuals who were active during the leisure time varied from 21.9% in the south to 24.4% in the midwest. The men were 1.48 (95%CI 1.40-1.57) times more active than women, with the northern region showing the highest difference between the sexes. The prevalence of active individuals was 67% lower among those aged 75+ years when compared with the 18-24 age group, and this difference was more marked in the north. Those with higher levels of education were on average three times more active than the participants with lower education levels. In terms of education level, the lowest difference was observed in the northeast. Conclusion: Despite the slight variations in the prevalence of physical activity during the leisure time among the regions, when population subgroups are considered, important differences were observed. These results suggest the need for promotion initiatives on physical activity with different approaches in each of the five regions of Brazil.


Subject(s)
Biocompatible Materials , Hydrogels , Temperature , Catalysis , Kinetics
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