EMCM - Capítulos de Livros

URI Permanente para esta coleçãohttps://repositorio.ufrn.br/handle/123456789/32511

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Evaluation of heterologous protein expression at different concentrations of MGSO4 and IPTG in Escherichia Coli W110
(Atena Editora, 2019) Santos, Yago Queiroz dos; Carelli, Gabriella Silva Campos; Veras, Bruno Oliveira de; Cruz, Joelton Igor Oliveira da; Moura, Geovanna Maria Medeiros; Marques Neto, Antônio Moreira; França, Anderson Felipe Jácome de
Since the improvement of gene sequencing techniques, the expression of heterologous proteins is gaining increasing relevance given the possibility of large-scale production when compared to the isolation of these same molecules in their original sources. However, heterologous expression systems continue to require for a suitable induction relevant amounts of synthetic molecules like IPTG (Isopropyl β-D-1-thiogalactopyranoside) which have toxicity and cost limitation when used in large scale. Thus, the objective of this work was to evaluate the effects of bivalent salts such as MgSO4 in association with IPTG on heterologous expression system pDMI.1 for a possible better cost-benefit proposal in the current heterologous protein expression protocol. Magnesium Sulfate contributes to an increase in bacterial physiology as a whole, inducing a higher protein expression acting as an indirect and alternative inducer in these conditions, with the advantages of presenting low cost and low cellular toxicity. Based on these obtained data, we propose the usage of low MgSO4 molar concentrations in current heterologous protein expression protocols performed in our group for the pDMI.1 vector. Additional studies are still needed in order to evaluate the effects of this salt on different expression systems at wide range of microorganisms
Phylogenetic analysis and identification of a cellulase producing Bacillus Sp. Strain by 16s RRNA sequencing
(Atena Editora, 2019) Santos, Yago Queiroz dos; França, Anderson Felipe Jácome de; Veras, Bruno Oliveira de; Carelli, Gabriella Silva Campos; Moura, Geovanna Maria Medeiros; Cruz, Joelton Igor Oliveira da; Oliveira, Fernanda Granja da Silva; Oliveira, João Ricardhis Saturnino de; Amorim, Luciclaudio Cassimiro de; Santos, Elizeu Antunes dos
The microorganisms belonging to genus Bacillus include a wide spectra and ubiquitous group of bacteria that can be found from the forest soil, to marine ecosystems occurring in association with a variety of aquatic organisms such as scleractinian corals present in the intertidal boulders. Therefore, these microorganisms are exposed to various abiotic stresses that cause ecological selection for a physiologically adapted microbiota to such extremes of temperature and salinity. In this work, we isolated and characterized a cellulase from a marine bacterial strain and indentified its specie by 16S rRNA sequencing followed by a BLAST analysis. The cellulolytic strain called SR22 showed to be a gram-positive spore-forming bacilli, facultative anaerobe, and catalase positive, as well as negative for indole, H2S production, and citrate utilization; those findings led us to consider the isolate belonging to the genus Bacillus, which was confirmed by the phylogenetic analysis, which revealed that the SR22 strain formed a clade with Bacillus subtilis. Its nucleotide sequence was deposited in GenBank as Accession No. MH119099 and the degree of sequence similarity of strain SR22 to Bacillus sp. was 99%. Taken together, the present data indicate the present celulase-positive indentified strain as a potential and useful candidate for industrial applications that employs celulase degrading processes like second-generation bioethanol and paper industries being still necessary further studies to complete characterize this microorganism secretome
Potential pharmacological applications of lectins
(Atena Editora, 2020) Cruz, Joelton Igor Oliveira da; Rabêlo, Luciana Maria Araújo; França, Anderson Felipe Jácome de; Veras, Bruno Oliveira de; Santos, Yago Queiroz dos; Moura, Geovanna Maria de Medeiros; Marques Neto, Antônio Moreira; Lima, Rayana Vanessa da Costa; Carelli, Gabriella Silva Campos
The word lectin is derived from the Latin legere which means “to choose” or “to select” and was introduced in biochemistry in the second half of the 20th century. Such molecules are characterized as glycoproteins that generally do not have an enzymatic role while have at least one non-catalytic domain − lectins are reversibly and specifically associated with simple and complex carbohydrates. Lectins differ from all other proteins through this type of connection with carbohydrates, promoting the ability to agglutinate cells through interaction with specific glycids having a non-immune origin. The present work aims to review the specialized literature in order to list the potential pharmacological applications derived from lectin-carbohydrate specificity in its most varied approaches
Proteases and their inhibitors in coagulation and inflammation
(Atena Editora, 2020) Santos, Jorge Anderson Nascimento dos; Marques Neto, Antônio Moreira; França, Anderson Felipe Jácome de; Santos, Yago Queiroz dos; Carelli, Gabriella Silva Campos; Cruz, Joelton Igor Oliveira da; Rabêlo, Luciana Maria Araújo; Veras, Bruno Oliveira de; Moura, Geovanna Maria de Medeiros
Proteases or peptidases are molecules that promote cleavage through the hydrolysis of peptide bonds present in proteins and polypeptides, transforming them into smaller amino acid or polypeptide residues. The group of serine proteases is predominant in peptidases and is found in almost all living organisms, constituting the family of proteases best characterized and physiologically versatile. Within the serine proteases are protease inhibitors, proteins capable of blocking and / or inhibiting the catalytic activity of proteolytic enzymes, being found naturally in most living organisms. In serine protease inhibitors, two distinct categories have already been classified, entrapment inhibitors and high affinity inhibitors. The hemostatic system participates in maintaining balance in living organisms, maintaining adequate blood pressure and perfusion, controlling bleeding caused by damage to blood vessels, through processes known as coagulation, where most factors in the coagulation cascade are serine proteases or cofactors . Among the most important serine proteases that act in the coagulation cascade are some coagulation factors (II, VII, IX, X, XI, XII, for example), the vasodilating molecule kallikrein, which is also a serine protease that acts on various substrates releasing vasoactive peptides, exercising their natural functions. In disorders in this cascade, medicine uses inhibitors with anticoagulant action, managing to reverse or inhibit these diseases. In inflammatory reactions, which is an essential step for controlling microbial invasion or tissue damage, as well as for maintaining tissue homeostasis, neutrophils secrete serine proteases such as neutrophil elastase (NE1), proteinase 3 (PR3) and cathepsin G ( CG), which are components of one of the most important molecular arsenals for the defense of the organism. Therefore, these facts suggest that new studies in this area are of great relevance to the evolution of science and medicine

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