TCC - Bacharelado em Ciências Biológicas (UAST)
URI permanente para esta coleçãohttps://arandu.ufrpe.br/handle/123456789/2932
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Resultados da Pesquisa
Item 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/8075252796586989The 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.Item 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/2508802546465708Aiming 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.Item 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/5589996843765879Through 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.Item 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/6110225182789262The 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.