Navegando por Assunto "Enzimas"

Agora exibindo 1 - 10 de 10

Análise de lacases de microrganismos com aplicações em biorremediação usando ferramentas de bioinformática
(2022-10-21) Silva, Andrey Giordane Costa; Buarque, Diego de Souza; http://lattes.cnpq.br/7609652740088882; http://lattes.cnpq.br/8075252796586989
The improper disposal and dumping of household waste, industrial waste, electronic waste, fertilizers, pesticides can elevate environmental concentrations of contaminants that cause significant impacts on human health and biodiversity. Given this problem, the development of technologies that assist in the environmental treatment of sites contaminated by these xenobiotics is of great importance. An applicable method for environmental remediation is biodegradation by enzymatic catalysis. Fungal lacases (in particular those of the genus Trametes) have a great potential for application in the area of wastewater treatment and bioremediation. Thus, a sequence analysis becomes important for the determination of lacases from some microorganisms. For this, we used the 1KYA, which represents the code of an active lacase structure from T. versicolor present in the Protein Data Bank (PDB). This structure is complexed to the ligand 2,5-xylidine, which is derived from commercially used solvents. Through this analysis, it is possible to understand structural factors important for the enzyme to detoxify environmentally harmful compounds, such as 2,5-xylidine. The structures and binding sites were analyzed using the BIOVIA Discovery Studio Visualizer 2021 program, where we were able to identify the amino acid residues and bonds that are part of the lacase 1KYA site that interact with 2,5-xylidine. To identify important structural factors in the sequences of lacases from microorganisms, a comparison was made in the primary sequence of the active lacase (1KYA) with a known sequence of the lacase from Trametes versicolor to determine what would be the degree of homology between them and if all amino acids that are part of the active site identified. By checking the degree of homology between different types of lacases from different organisms, it was possible to identify sequences of 16 microorganisms with a percentage equal to or greater than 79.56%. In addition, it was possible to identify the amino acid residues conserved in lacases from different organisms and the residues that changed among the sequences of this enzyme.
Análise estrutural e uso de lacase de camarão para a degradação de antraceno
(2022-10-19) Silva, Larissa Celestino da; Buarque, Diego de Souza; http://lattes.cnpq.br/7609652740088882; http://lattes.cnpq.br/5589996843765879
Through the large population growth and technological development, the use of natural resources has become increasingly present and constant, also causing concerns, measures and solutions related to the environment. In this context, the oil spill has affected aquatic ecosystems. Furthermore, petroleum comprises a series of polycyclic aromatic hydrocarbons, which are not very volatile and are deposited at the bottom of aquatic environments. Therefore, the use of laccase enzymes can be used to combat petroleum hydrocarbons. The structure of the L. vannamei laccase showed conserved domains characteristic of this enzyme, such as those that are important for copper centers, since they are responsible for carrying out the oxidation of aromatic compounds. In addition, the sequence of this enzyme showed a higher percentage of identity when compared to the laccases of other organisms, this fact can be characterized due to the number of identical positions existing between their amino acid sequences. The present work addressed the use of bioinformatics tools to understand the structure of the laccase and, consequently, test the activity of the enzyme in the degradation of the anthracene hydrocarbon.
Avaliação da qualidade do pão francês de massa congelada com diferentes combinações de melhorador de farinha de trigo
(2019-12-11) Melo, Juliana Hellen da Silva; Ribeiro, Daniele Silva; http://lattes.cnpq.br/1517959077516490; http://lattes.cnpq.br/3926147757738357
The growth in the number of bakeries and the increase in the consumption of bread has contributed to new investments in this sector, such as the frozen bread market, which is on the rise. This new trend is attracting the attention of bakeries, allowing greater practicality, standardization of the product, cost reduction and increase in the shelf life of the dough. The mass freezing effect can be minimized through the use of better wheat flour and ingredients used, making it possible to improve the quality of the final product through its application. The present work sought to evaluate five formulations, being a standard, the French type of frozen dough, changing the content of the best flour; content of mixtures of enzymes (glucose oxidase - Gox, alpha amylase, phospholipase and hemicellulase), emulsifiers and oxidants, observing an interaction of these, in order to obtain breads within the quality standards; specific volume, shape, lash opening, loss of mass and bread yield. As a result, with the exception of the F5 or control application (F2, F3 and F4), which concentrate more flour oxidizing agents (ascorbic acid, ADA), emulsifiers (Datem and SSL) and enzymes (alpha amylase and gox) resulting in a greater specific volume of bread, being classified as very large, as well as the standard pattern. The lash opening was around 50 mm for all formulations, except for F2, which may have been influenced by the concentration of enzymes. For the shape of the loaves, all are spherical. There was no statistical difference in water loss and yield. It can be concluded that the breads selected from the four frozen pasta formulations studied include satisfactory values, in general, in relation to the recommended parameters, compared to the standard standard. In this way, a company has new formulations that can replace the best commercial. However, the adoption of the F5 application was suggested, due to the better specified volume.
Caracterização físico-química de lacase do camarão litopenaeus vannamei e o uso dessa enzima para a degradação de corantes
(2022-10-17) Marcolino, Girlanne de Medeiros; Buarque, Diego de Souza; http://lattes.cnpq.br/7609652740088882; http://lattes.cnpq.br/2508802546465708
Aiming at bioremediation to combat impacts caused by textile effluents, the present study aimed to determine the physicochemical parameters of the enzyme and to evaluate the effect of laccases from the main shrimp species cultivated in Brazil (Litopenaeus vannamei). Thus, with the enzyme already partially purified, the determination of the activity of laccases was carried out, using the substrate ABTS and Choline, later, the physicochemical parameters were determined, and finally, the effect of laccase enzymes on the degradation of dyes was analyzed. phenol red, coomassie brilliant blue r, bromophenol blue and methylene blue. With this, the enzymes already partially purified, together with ABTS, it can be observed that it did not obtain specificity with the substrate, thus, there was no activity. With this, the substrate Colina was used to determine the physicochemical parameters, where it was able to react with the enzyme and presented an optimal alkaline pH (pH 9.5) and obtained its optimal temperature at 100°C. After that, the percentage of degradation was calculated through the absorbance per minute, in the absence and in the presence of laccase, obtaining a satisfactory result for the degradation of the bromophenol blue dye. Thus, laccase was able to degrade one of the dyes, for future studies which will allow use laccases as an important enzyme against dyes.
O conteúdo enzimas no ensino de Química: um panorama das propostas difundidas em periódicos nacionais
(2023-09-21) Silva, Viviane Oliveira da; Marcelino Júnior, Cristiano de Almeida Cardoso; http://lattes.cnpq.br/7518586937701331
The research carried out was documentary, descriptive and exploratory in nature, and approaches investigations into the state of knowledge with the main objective of offering a panoramic view of an important part of Brazilian academic production on the teaching of enzymes content, through the analysis of published articles in some of the main national journals in which the Chemical Education community disseminates the results of its studies. Articles published in 12 (twelve) journals with Qualis CAPES were adopted as primary documents. The methodological path was designed in line with Morosini's perspective, following the steps of the annotated, systematized, categorized and propositional bibliography. Of a total of 8,303 articles consulted, 56 dealt with enzymes, but only 13 (thirteen) constituted the research corpus, as they were aimed at teaching enzymes. A content analysis allowed the establishment of categorization of the findings. These works are preferably aimed at Higher Education, 10 articles, while 4 articles are aimed at Secondary Education and 2 at Technological Education; 3 works propose activities aimed at more than one level of education. The main genres of work are: i) educational research: 4 articles; ii) development of experimental activity: 7 articles; and iii) report of teaching experience, 2 articles. Experimentation is the main theme in 10 of the articles investigated – 9 on enzyme activity and 1 on enzyme properties, while modeling is the theme in the other 3 articles. The contents covered are enzymatic activity (catalysis), inhibition and inactivation; enzyme functions; and enzyme-substrate model. In the articles, the relationship between experimentation + enzymatic activity (9) is prioritized, when compared to the other categories: modeling + enzyme-substrate model (3) and experimentation + properties (1). Activities with low-cost experiments, both aimed at Higher Education and Secondary Education, are the main teaching strategies used. Modeling with 3D or computational models is also used, as well as video classes with simulated experiments and an adapted educational game. It is also important to invest in the development of proposals that consider training processes at different levels of Chemistry education, including higher education. In this sense, it is necessary to encourage the provision of training moments that stimulate discussions and reflections in the teaching and training of teachers, and other professionals, on computational modeling for didactic purposes. In association with these aspects, a field of interest that still lacks action is non-face-to-face teaching. Therefore, it is necessary to encourage the development of studies and the production of teaching instruments/products on enzyme content for virtual teaching, mainly with the resources of Digital Information and Communication Technologies. It is also important to encourage the development of strategies that are options for experimentation and modeling.
Desenvolvimento de processo biotecnológico para obtenção de frutosiltransferase a partir de linhagens de aspergillus spp. utilizando resíduos agroindustriais
(2018-08-20) Silva, Marcos Fellipe da; Porto, Tatiana Souza; Oliveira, Rodrigo Lira de; http://lattes.cnpq.br/8523811836244962; http://lattes.cnpq.br/8029060415742712; http://lattes.cnpq.br/5668322074655881
Fructosyltransferase is an enzyme involved in the conversion of sucrose to fructooligosaccharides, sugars that have received special attention because to their biological and functional properties, which act mainly as prebiotics. This enzyme, as well as other biomolecules can be obtained through biotechnological processes, using several types of microorganisms, among these processes, solid-state fermentation stands out because it allows the use of agroindustrial residues, besides promoting high production rates of biomolecules of interest. The present study had as objective to investigate the variables that influence the production of fructosyltransferase from Aspergillus spp. using agroindustrial residues as well as characterize the crude extract. The best results were found in the species Aspergillus tamarii URM4634, to which it did not show production of mycotoxins, fermented in the soybean meal. From the factorial design it was verified that the best condition was observed using 3 g of substrate, 15% concentration of sucrose solution and 60% of moisture for 72 hours, obtaining 209.11 and 53.90 μmol / mL / min of hydrolytic and transfructosylation activities, respectively. In the evaluation of the growth of fungal biomass, the highest development in 36 hours of fermentation, observing a content of 132 mg / g of glucosamine, in this same analysis it was verified that the best time for production of fructosyltransferase, using the conditions of the best condition of planning were obtained in the 96-hour period, obtaining 221.53 and 66.90 μmol / mL / min of hydrolytic and trans-fructosylation activities, respectively. The enzyme produced presented values of Km 54.73 and 369.68 μmol/mL and Vmáx 227.27 and 50.66 μmol/mL/min for hydrolytic and transfructosylation activities, respectively. The optimal temperature for both activities was 60ºC, as well as pH 6.0. The fructosyltransferase presented stability in the temperature ranges of 30-50 ° C and pH 4.0-5.0. It was also observed that the Mn2 + ion showed to be an activator of the hydrolytic activity, whereas Na + presented the same effect in the transfructosylation activity. In general, all results are promising for the biotechnological production of fructosyltransferase, demonstrating high saccharose hydrolysis and transfer of the fructosyl groupings, potentially being applied in bioprocesses that aim at the synthesis of fructo-oligosaccharides.
Estágio supervisionado obrigatório em biotecnologia industrial
(2018-12-28) França, Pedro Renann Lopes de; Porto, Tatiana Souza; http://lattes.cnpq.br/8029060415742712; http://lattes.cnpq.br/8709917109875708
Metais pesados interferem na atividade de enzimas do tipo lacases do camarão Litopenaeus vannamei?
(2021-03-05) Bezerra, Amanda Letícia Florentino Mandú; Buarque, Diego de Souza; http://lattes.cnpq.br/7609652740088882; http://lattes.cnpq.br/6110225182789262
The contamination of aquatic environments with potentially toxic chemical elements and organic compounds (pesticides, hydrocarbons, dyes, etc.) has been notorious due to the industrial activity. In such a context, there has been an increase regarding the use of shrimp farming residues as sources of molecules with applications in bioremediation, such as laccase enzymes, which present a degradation activity of various contaminants such as aromatic hydrocarbons, phenols, pesticides, dyes, among others. However, such contaminants are discarded in water along with potentially toxic chemical elements and these can interfere in the enzymatic activity of enzyme bioremediation in such a variety of contaminants. Then, it is important to understand whether the enzymes will remain active even with the presence of potentially toxic chemical elements. Consequently, this work aims to evaluate the effect of potentially toxic chemical elements on laccase enzymes from the crude extracts from the shrimp Litopenaeus vannamei hepatopancreas. The effect of metals was also evidenced in metalloproteinases in the same extract to understand whether the presence of these enzymes interfere on the interaction of metals with laccases. To determine the effect of the potentially toxic metals (nickel, mercury, copper, cadmium and zinc in concentrations between 0.001 and 10 mM), they were incubated (separately) with the extracts. Subsequently, the percentage of the residual activity of laccases and metalloproteinases was verified compared with a control without potentially toxic metals (100%). None of the potentially toxic metals between 0.001 and 1 mM (concentration above the allowable values) were able to inhibit the tested enzymes. Furthermore, 10 mM of nickel chloride also were not able to inhibit the activity of laccases and metalloproteinases. On the other hand, the 10 mM chlorides of mercury, copper and cadmium were able to significantly increase laccase’s activity, while chlorides of mercury and copper inhibited metalloproteinases. In its turn, the 10 mM zinc sulfate inhibited both laccases and metalloproteinases. Therefore, it is concluded that the majority of the tested potentially toxic metals were able to interfere in the laccase enzymes activity in the extract of hepatopancreas from L. vannamei.
Produção de enzimas utilizando resíduos de café como substrato em processos fermentativos: uma revisão
(2021-12-07) Alves, Ywkelly de Lima; Bezerra, Raquel Pedrosa; Costa, Romero Marcos Pedrosa Brandão; http://lattes.cnpq.br/1797280118220965; http://lattes.cnpq.br/1466206759539320; http://lattes.cnpq.br/2310542251305353
Microbial enzymes stand out due to their numerous biotechnological applications, and allied to this, the possibility of using residues as a substrate in the fermentation process can bring advantages in production on an industrial scale. Coffee residues, for example, have been shown to be a good means of obtaining a variety of enzymes. Thus, the objective of this work was to carry out a systematic review of the use of three different types of coffee residues for enzyme production, through fermentation processes, in order to identify the main classes of enzymes produced and the microorganisms used as fermenting agents, such as fungi, bacteria, cyanobacteria and microalgae. Thus, a bibliographic search was carried out in the databases since the last decade using the keywords “waste pulp coffee and enzyme” and, through inclusion and exclusion criteria, 26 articles were selected. About 30.76% of the works were produced in Indonesia and pointed to cellulase as the main enzyme produced. Solid state fermentation (SSF) was the most used process for the production of enzymes, representing 92.59%, and the fungi of the genus Aspergillus were most widely used in this process, with 23.07% of occurrence in the articles. Among coffee residues, pulp had the highest occurrence, appearing in 76.92% of the articles. Furthermore, fermentation time, residue volume, temperature and pH were essential parameters in the final result of obtaining the enzymes. Thus, it was observed that the coffee residue has potential as a substrate for obtaining different enzymes, mainly cellulosic ones, using fungi, especially those of the Aspergillus genus, in solid fermentation processes.
Produção de lacases por Aspergillus serratalhadensis URM 79/18 utilizando subprodutos agroindustriais
(2022-10-05) Ferreira, Julyanne Victória dos Santos; Porto, Ana Lúcia Figueiredo; Batista, Juanize Matias da Silva; http://lattes.cnpq.br/6699725036732885; http://lattes.cnpq.br/4989617783837981; http://lattes.cnpq.br/8901230412759036
Laccases are copper-containing ligninolytic enzymes and are known to be excellent oxidizing agents in the presence of oxygen. Among the ligninolytic enzymes, laccases are the most widely studied group, being known as green catalysts, as they promote the direct reduction of molecular oxygen to water without the formation of unwanted by-products. Currently, laccases are secreted mainly by fungi of the phyla Ascomycota and Basidiomycota and have a variety of industrial applications that include the discoloration and degradation of dyes and textile effluents, detergents for fabric bleaching, tooth whiteners for oral hygiene, pulp bleaching in the textile industry. fabrics and paper and in the deconstruction of lignocellulosic biomass. Therefore, the present study aimed at the production of laccases by solid state (FES) and submerged (FS) fermentation of Aspergillus serratalhadensis URM 79/18, a microorganism isolated from the Caatinga soil, using as substrates agro-industrial residues, wheat bran, soy flour, manioc and orange peel. The qualitative test performed by adding 3 Mm of ABTS substrate to PDA medium was positive for extracellular laccase production, confirmed by the formation of a green halo measuring about 34 mm. The orange peel substrate used in FES inhibited fungal growth up to 96 h of fermentation, and consequently there was no enzymatic production with this substrate. Laccase activity was determined using ABTS as substrate, so the highest enzyme activity was 305.56 U/mL obtained after 48h of FES at 30°C in wheat bran substrate, the second highest laccase production was 296 .29 U/mL also from FES, but in the manioc peel substrate and with a fermentation time of 72 hours. For the FS, the MS-2 medium modified by the use of ABTS as an inducer and also by the nutrient solution containing several metal ions was used, the substrates used were wheat bran and soybean flour in the fermentation time of 48 hours, being the highest activity of laccase in the FS obtained with the MS-2 medium modified by the nutrient solution and the addition of ABTS, being 0.1944 U/mL with wheat bran as substrate. Therefore, the recent fungal strain A. serratalhadensis is a laccase producer and has an ideal performance in solid-state fermentation, especially when the agro-industrial residue of wheat bran is used as a substrate, demonstrating its potential for the biotechnology industry.