Programa de Pós-Graduação em Biotecnologia - PPGBIOTEC/ICB
URI Permanente desta comunidadehttps://repositorio.ufpa.br/handle/2011/6089
O Programa de Pós-Graduação em Biotecnologia (PPGBIOTEC) é um programa do Instituto de Ciências Biológicas (ICB) da Universidade Federal do Pará (UFPA). O PPGBIOTEC fornece a base teórica para o desenvolvimento de projetos em duas áreas de concentração e quatro linhas de pesquisa, definidas de acordo com a competência e experiência de orientação dos docentes do programa: Área de Bioprospecção: linhas de pesquisa: (i) química orgânica de biomoléculas e metabolômica; e (ii) genômica, transcriptômica, proteômica e bioinformática de microrganismos e plantas (Bactéria, Archaea e Eukarya). Área de Biotecnologia Aplicada: linhas de pesquisa: (i) saúde humana e veterinária; e (ii) produção de insumos e processos industriais.
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Item Acesso aberto (Open Access) Caracterização molecular in silico de uma mono-oxigenase lítica de polissacarídeo cianobacteriana(Universidade Federal do Pará, 2024-03) VIRGOLINO, Rodrigo Rodrigues; GONÇALVES, Evonnildo Costa; http://lattes.cnpq.br/8652560763793265; https://orcid.org/0000-0003-2221-1995 País de Nacionalidade BrasilLytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that catalyze the oxidative cleavage of β(1-4) glycosidic bonds and have attracted great attention due to importance in increasing the efficiency in degradation of recalcitrant polymeric substrates, in synergism with the action of hydrolytic enzymes, as an accessory function. However, LPMOs act via oxidative cleavage rather than hydrolysis. In industrial applications, LPMOs of fungal origin are the most frequent, while other taxonomic groups have been described as possible alternative sources of these enzymes. In the present study, we aimed to identify and characterize in silico a LPMO of cyanobacterial origin with putative functions in chitin depolymerization. The search for sequence similarity and conservation of domains with other characterized LPMOs identified a 289 AA protein from the cyanobacterium Mastigocoleus testarum of the Nostocales Order, being a probable LPMO of the CAZy-AA10 class. This protein is referred to as MtLPMO10. Phylogenetic analysis revealed that MtLPMO10 is homologous to the Tma12 protein from the fern Tectaria macrodonta, with 52.11% identity, which was the first LPMO characterized as originating from the plant kingdom. The occurrence of shared structural and functional patterns with other AA10 class LPMOs, as well as the existence of variations in these established patterns, contributed to the understanding of the biological functions of this class of enzymes. The predicted protein tertiary arrangement by the AlphaFold server pointed out structural features common to LPMOs, especially a histidine brace composed of His31 and His132 and an immunoglobulin-like domain consisting of antiparallel beta strands. Molecular dynamics simulation (MD) allowed evaluating the enzyme-substrate affinity, using an initial pose based on data obtained from the literature. There was stability of the MtLPMO10-chitoheptaose complex during 100ns of MD, while the MtLPMO10-celloheptaose complex broke apart in 30ns of MD. Also, there was a shorter Cu(I)-H4 distance in the first complex compared to the Cu(I)-H1 distance (averages 6.0 ± 0.7 Å and 7.9 ± 0.7 Å, respectively), suggesting a C4-type regioselectivity, as defined for Tma12. This study highlights the existence of lytic polysaccharide monooxygenases in cyanobacteria and paves the way for further investigations related to this enigmatic class of enzymes and their potential use in biotechnological applications.Item Acesso aberto (Open Access) Prospeção de aminoácidos tipo micosporinas (MAAs) em cianobactérias da Amazônia oriental(Universidade Federal do Pará, 2014-06-30) ARAÚJO, Sanclayver Corrêa; GONÇALVES, Evonnildo Costa; http://lattes.cnpq.br/8652560763793265Mycosporine-like amino acids (MAAs) are low molecular weight water soluble compounds wuich biosynthesis was thought to occur via shikimate pathway in bacteria, phytoplankton and macroalgae. Recently evidences show its biosynthesis via the pentose pathway in a cyanobacterium. Due to its high extinction molar coefficient in UV region, they provide protection against the damaging effects of UV radiation and have potential for use in sunscreens. In previous works it was described a biosynthetic cluster for shinorine with the enzymes dehydroquinate synthase, present in the shikimate pathway, O-methyltransferase, and ATP-grasp and NRPS-like enzymes. It was observed that the enzyme 2-epi-5-epi-valiolone synthase, which link the pentose pathway with MAAs production would lead to formation of 4-deoxygadusol, precursor of MAAs. In this work a genomics approach was carried out so find these genes so that MAAs production potential in Amazonian cyanobacteria of the Coleção Amazônica de Cianobactérias e Microalgas, CACIAM 14, CACIAM 53, CACIAM 54 and CACIAM 57 strains was assessed, as well as an analysis through capillary chromatography coupled to electrospray mass spectrometryof the metabolites in CACIAM 14. The genes Dehydroquinate synthase and o-methyltransferase were found in all the strains studied. The genes of pentose pathway Ribulose-phosphate-3-epimerase and transketolase were detected in the strains CACIAM 14, CACIAM 53 and CACIAM 57, what may suggest that in these strains MAAs could be produced by both pathways while in CACIAM 57 MAAs could be produced by shikimate pathway only. In CACIAM 14 strain, fragments of mass to charge relationship 186 and 197 were found in the same retention time of a precursor ion of m/z 333, what could be related to shinorine. Therefore, the strains CACIAM 53, 54 and 57 are potentially producers of MAAs due to possessing biosynthetic genes and CACIAM 14 is shinorine producer.