Publications by authors named "Cleide Mara Faria Soares"

13 Publications

  • Page 1 of 1

Influence of seasonality on the physicochemical properties of Lam. Seed oil and their oleochemical potential.

Food Chem (Oxf) 2022 Jul 27;4:100068. Epub 2021 Dec 27.

Universidade Tiradentes, Av. Murilo Dantas, 300, Farolândia, Aracaju, SE 49032-490, Brazil.

The effect of abiotic factors, such as weather and climate can alter the properties of vegetable oils. In this work, the effects of the refining process and pre-drying of Moringa oleifera Lam. seeds collected in the dry and rainy seasons (seasonality) were evaluated on the characteristics of the extracted oils. The refined and crude dry season oils had lower acidity and moisture content than the dry and raw rainy season oils. Oleic acid (C18:1) showed the highest concentration in the different Moringa oils studied. The results suggest that dry season oils are more suitable for application as feedstocks in the cosmetic, food, medicinal and pharmaceutical industries. Furthermore, refining proved to be efficient in removing free fatty acids and in lightening the oil.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.fochms.2021.100068DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8991620PMC
July 2022

Evaluation of Enzymatic Tunnels in the Biotransformation of α-Tocopherol Esters.

Front Bioeng Biotechnol 2021 21;9:805059. Epub 2022 Jan 21.

Graduate Program in Industrial Biotechnology, Tiradentes University (UNIT), Aracaju, Brazil.

α-Tocopherol is a molecule obtained primarily from plant sources that are important for the pharmaceutical and cosmetics industry. However, this component has some limitations such as sensitivity to oxygen, presence of light, and high temperatures. For this molecule to become more widely used, it is important to carry out a structural modification so that there is better stability and thus it can carry out its activities. To carry out this structural modification, some modifications are carried out, including the application of biotransformation using enzymes as biocatalysts. Thus, the application of a computational tool that helps in understanding the transport mechanisms of molecules in the tunnels present in the enzymatic structures is of fundamental importance because it promotes a computational screening facilitating bench applications. The aim of this work was to perform a computational analysis of the biotransformation of α-tocopherol into tocopherol esters, observing the tunnels present in the enzymatic structures as well as the energies which correspond to the transport of molecules. To carry out this work, 9 lipases from different organisms were selected; their structures were analyzed by identifying the tunnels (quantity, conformation, and possibility of transport) and later the calculations of substrate transport for the biotransformation reaction in the identified tunnels were carried out. Additionally, the transport of the product obtained in the reaction through the tunnels was also carried out. In this work, the quantity of existing tunnels in the morphological conformational characteristics in the lipases was verified. Thus, the enzymes with fewer tunnels were RML (3 tunnels), LBC and RNL (4 tunnels), PBLL (5 tunnels), CALB (6 tunnels), HLG (7 tunnels), and LCR and LTL (8 tunnels) and followed by the enzyme LPP with the largest number of tunnels (39 tunnels). However, the enzyme that was most likely to transport substrates in terms of α-tocopherol biotransformation (in relation to the E and E energies of ligands and products) was CALB, as it obtains conformational and transport characteristics of molecules with a particularity. The most conditions of transport analysis were α-tocopherol tunnel 3 (E: -4.6 kcal/mol; E: 1.1 kcal/mol), vinyl acetate tunnel 1 (E: -2.4 kcal/mol; E: 0.1 kcal/mol), and tocopherol acetate tunnel 2 (E: -3.7 kcal/mol; E: 2 kcal/mol).
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.3389/fbioe.2021.805059DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8814584PMC
January 2022

Development of an ethanolic two-phase system (ETPS) based on polypropylene glycol 2000 + ethylene glycol + ethanol for separation of hydrophobic compounds.

Chem Commun (Camb) 2021 Mar;57(17):2156-2159

Tiradentes University, Av. Murilo Dantas, 300, CEP: 49032-490, Aracaju, SE, Brazil. and Institute of Technology and Research, Av. Murilo Dantas, 300, Prédio do ITP, CEP: 49032-490, Aracaju, SE, Brazil.

This work reports, for the first time, an Ethanolic Two-Phase System (ETPS) based on polypropylene glycol 2000 (PPG 2000), mono-, di-, tri-ethylene glycol, and ethanol. An ionic liquid (IL) (1-butyl-3-methylpyridinium chloride) was used as an adjuvant. This ETPS shows promising results for the extraction of highly hydrophobic compounds. Bixin (model of hydrophobic compounds) migrates completely to the PPG 2000-rich phase, while ascorbic acid (hydrophilic compound) migrated to the opposite phase.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1039/d0cc01542cDOI Listing
March 2021

Oleochemistry potential from Brazil northeastern exotic plants.

Biochimie 2020 Nov 14;178:96-104. Epub 2020 Sep 14.

Universidade Tiradentes, Av. Murilo Dantas, 300, Farolândia, Aracaju, SE, 49032-490, Brazil; Instituto de Tecnologia e Pesquisa, Av. Murilo Dantas, 300, Prédio Do ITP, Farolândia, Aracaju, SE, 49032-490, Brazil. Electronic address:

Caatinga is a Brazilian semi-arid ecosystem that stands out for presenting unique environmental characteristics with a dry, spiny and deciduous shrub/forest vegetation with several species that can be renewable oil sources with potential applicability in oleochemical and nutrition. Caatinga oilseeds have a high content of unsaturated fatty acids, phytosterols and sterols, and this composition is related to its nutritional potential. The present review summarizes the knowledge on the oil contents and fatty acid profiles of seeds from six representatives caatinga species. It was observed that plants species like Caju (Anacardium occidentale L.), Favela (Cnidoscolus quercifolius Pohl), Licuri (Syagrus coronata (Mart.) Becc.), Pinhão-bravo (Jatropha mollissima Pohl Baill), Pequi (Caryocar brasiliense Camb) and Oiticica (Licania rígida Benth) contains approximately 33.1, 33.5, 49.2, 18.3, 70.16 and 57.0% w/w of oil, respectively, on a dry weight basis. Their fatty acid profiles are mostly saturated for Licuri oil, with a high content of lauric acid (up to 40%) and unsaturated for Favela, Pinhão-bravo, Cashew nut, Pequi and Oiticica oils. Oiticica oil shows a high concentration of unusual conjugated polyunsaturated fatty acids, like α-Eleostearic and Licanic acid with 16.90 and 43.20% w/w, respectively.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.biochi.2020.09.002DOI Listing
November 2020

Immobilization of Low-Cost Alternative Vegetable Peroxidase ( L. peroxidase): Choice of Support/Technique and Characterization.

Molecules 2020 Aug 12;25(16). Epub 2020 Aug 12.

Programa de Pós-Graduação em Biotecnologia Industrial, Tiradentes University, 49032-490 Aracaju, SE, Brazil.

In the present work the radish ( L.) was used as the low-cost alternative source of peroxidase. The enzyme was immobilized in different supports: coconut fiber (CF), calcium alginate microspheres (CAMs) and silica SBA-15/albumin hybrid (HB). Physical adsorption (PA) and covalent binding (CB) as immobilization techniques were evaluated. Immobilized biocatalysts (IBs) obtained were physicochemical and morphologically characterized by SEM, FTIR and TGA. Also, optimum pH/temperature and operational stability were determined. For all supports, the immobilization by covalent binding provided the higher immobilization efficiencies-immobilization yield (IY%) of 89.99 ± 0.38% and 77.74 ± 0.42% for HB and CF, respectively. For CAMs the activity recovery (AR) was of 11.83 ± 0.68%. All IBs showed optimum pH at 6.0. Regarding optimum temperature of the biocatalysts, HB-CB and CAM-CB maintained the original optimum temperature of the free enzyme (40 °C). HB-CB showed higher operational stability, maintaining around 65% of the initial activity after four consecutive cycles. SEM, FTIR and TGA results suggest the enzyme presence on the IBs. Radish peroxidase immobilized on HB support by covalent binding is promising in future biotechnological applications.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.3390/molecules25163668DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7466051PMC
August 2020

Brazilian Red Propolis: Extracts Production, Physicochemical Characterization, and Cytotoxicity Profile for Antitumor Activity.

Biomolecules 2020 05 6;10(5). Epub 2020 May 6.

Tiradentes University (UNIT), Av. Murilo Dantas, 300, Aracaju 49010-390, Brazil.

Brazilian red propolis has been proposed as a new source of compounds with cytotoxic activity. Red propolis is a resinous material of vegetal origin, synthesized from the bees of the Appis mellifera family, with recognized biological properties. To obtain actives of low polarity and high cytotoxic profile from red propolis, in this work, we proposed a new solvent accelerated extraction method. A complete 2 factorial design was carried out to evaluate the influence of the independent variables or factors (e.g., temperature, number of cycles, and extraction time) on the dependent variable or response (i.e., yield of production). The extracts were analyzed by gas chromatography coupled with mass spectrometry for the identification of chemical compounds. Gas chromatography analysis revealed the presence of hydrocarbons, alcohols, ketones, ethers, and terpenes, such as lupeol, lupenone, and lupeol acetate, in most of the obtained extracts. To evaluate the cytotoxicity profile of the obtained bioactives, the 3-(4,5-dimethyl-2-thiazole)-2,5-diphenyl-2--tetrazolium bromide colorimetric assay was performed in different tumor cell lines (HCT116 and PC3). The results show that the extract obtained from 70 °C and one cycle of extraction of 10 min exhibited the highest cytotoxic activity against the tested cell lines. The highest yield, however, did not indicate the highest cytotoxic activity, but the optimal extraction conditions were indeed dependent on the temperature (i.e., 70 °C).
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.3390/biom10050726DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7277404PMC
May 2020

Liquid-Liquid extraction of phenolic compounds in systems based on acetonitrile + water + polyvinylpyrrolidone at 298.15 K.

Data Brief 2018 Oct 27;20:2045-2053. Epub 2018 Sep 27.

Tiradentes University, Av. Murilo Dantas 300, Farolândia, 49032-490 Aracaju, SE, Brazil.

This paper contains data related to the research paper entitled "Organic two-phase system based on acetonitrile + water + polyvinylpyrrolidone, a novel concept of liquid-liquid equilibrium: phase diagrams and phenolic compounds partitioning". Data of phase equilibrium were obtained using the cloud point method. After this step, some blending points were chosen to perform the phenolic compounds partitioning (gallic acid, quercetin dihydrate and cyanidin 3-O-glucoside chloride).
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.dib.2018.09.067DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6178207PMC
October 2018

Aqueous Two-Phase Systems formed by Biocompatible and Biodegradable Polysaccharides and Acetonitrile.

Sep Purif Technol 2014 Nov;136:74-80

Programa de Pós-Graduação em Engenharia de Processos, Universidade Tiradentes, Av. Murilo Dantas 300, Farolândia. CEP: 49032-490, Aracaju-SE, Brazil ; Instituto de Tecnologia e Pesquisa. Av. Murilo Dantas, 300. CEP: 49032-490, Aracaju - SE, Brazil.

In this work, it is shown that novel aqueous two-phase systems can be formed by the combination of acetonitrile and polysaccharides, namely dextran. Several ternary phase diagrams were determined at 25 °C for the systems composed of water + acetonitrile + dextran. The effect of the dextran molecular weight (6,000, 40,000 and 100,000 g.mol) was ascertained toward their ability to undergo liquid-liquid demixing. An increase in the dextran molecular weight favors the phase separation. Furthermore, the effect of temperature (25, 35 and 45 °C) was evaluated for the system constituted by the dextran of higher molecular weight. Lower temperatures are favorable for phase separation since lower amounts of dextran and acetonitrile are required for the creation of aqueous two-phase systems. In general, acetonitrile is enriched in the top phase while dextran is majorly concentrated in the bottom phase. The applicability of this new type of two-phase systems as liquid-liquid extraction approaches was also evaluated by the study of the partition behavior of a well-known antioxidant - vanillin - and used here as a model biomolecule. The optimized conditions led to an extraction efficiency of vanillin of 95% at the acetonitrile-rich phase.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.seppur.2014.08.020DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4340543PMC
November 2014

New strategy to apply perfluorodecalin as an oxygen carrier in lipase production: minimisation and reuse.

Bioprocess Biosyst Eng 2015 Apr 26;38(4):721-8. Epub 2014 Oct 26.

Programa de Pós-Graduação em Engenharia de Processos, Universidade Tiradentes, Av. Murilo Dantas 300, Farolândia, Aracaju, 49032-490, Brazil.

A novel strategy for the production of lipase by Bacillus sp. ITP-001 in a stirred tank fermenter using perfluorodecalin (PFD) was studied. Firstly, a response surface methodology 2(2) with three central points was employed to optimise the effect of agitation speed and aeration rate in lipase production. According to the response from the experimental designs, 300 rpm (revolutions per minute) and 0.5 vvm (air volume/liquid volume per minute) were found to provide the best condition (lipolytic activity: LA = 3,140.76 U mL(-1)). Then, the influence of PFD concentration on the fermentation process was evaluated. Incorporation of PFD at all concentrations above 1% had no statistically significant influence on lipase production, that is, the previous optimisation allowed the reduction of the amount of PFD added besides increasing lipase production. Furthermore, PFD could be used in three sequential fermentations without altering the statistical production of lipase, reducing by 67% the cost of PFD addition.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1007/s00449-014-1312-4DOI Listing
April 2015

Encapsulation in a sol-gel matrix of lipase from Aspergillus niger obtained by bioconversion of a novel agricultural residue.

Bioprocess Biosyst Eng 2014 Sep 22;37(9):1781-8. Epub 2014 Feb 22.

Department of Food Technology, Federal University of Sergipe, Avenida Marechal Rondon s/n, São Cristóvão, Sergipe, CEP: 49100-000, Brazil.

Lipase from Aspergillus niger was obtained from the solid-state fermentation of a novel agroindustrial residue, pumpkin seed flour. The partially purified enzyme was encapsulated in a sol-gel matrix, resulting in an immobilization yield of 71.4 %. The optimum pH levels of the free and encapsulated enzymes were 4.0 and 3.0, respectively. The encapsulated enzyme showed greater thermal stability at temperatures of 45 and 60 °C than the free enzyme. The positive influence of the encapsulation process was observed on the thermal stability of the enzyme, since a longer half-life t 1/2 and lower deactivation constant were obtained with the encapsulated lipase when compared with the free lipase. Kinetic parameters were found to follow the Michaelis-Menten equation. The K m values indicated that the encapsulation process reduced enzyme-substrate affinity and the V max was about 31.3 % lower than that obtained with the free lipase. The operational stability was investigated, showing 50 % relative activity up to six cycles of reuse at pH 3.0 at 37 °C. Nevertheless, the production of lipase from agroindustrial residue associated with an efficient immobilization method, which promotes good catalytic properties of the enzyme, makes the process economically viable for future industrial applications.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1007/s00449-014-1151-3DOI Listing
September 2014

Characterization of biocatalysts prepared with Thermomyces lanuginosus lipase and different silica precursors, dried using aerogel and xerogel techniques.

Appl Biochem Biotechnol 2014 Jan;172(1):263-74

The use of lipases in industrial processes can result in products with high levels of purity and at the same time reduce pollutant generation and improve both selectivity and yields. In this work, lipase from Thermomyces lanuginosus was immobilized using two different techniques. The first involves the hydrolysis/polycondensation of a silica precursor (tetramethoxysilane (TMOS)) at neutral pH and ambient temperature, and the second one uses tetraethoxysilane (TEOS) as the silica precursor, involving the hydrolysis and polycondensation of the alkoxide in appropriate solvents. After immobilization, the enzymatic preparations were dried using the aerogel and xerogel techniques and then characterized in terms of their hydrolytic activities using a titrimetric method with olive oil and by the formation of 2-phenylethyl acetate in a transesterification reaction. The morphological properties of the materials were characterized using scanning electron microscopy, measurements of the surface area and pore size and volume, thermogravimetric analysis, and exploratory differential calorimetry. The results of the work indicate that the use of different silica precursors (TEOS or TMOS) and different drying techniques (aerogel or xerogel) can significantly affect the properties of the resulting biocatalyst. Drying with supercritical CO2 provided higher enzymatic activities and pore sizes and was therefore preferable to drying, using the xerogel technique. Thermogravimetric analysis and differential scanning calorimetry analyses revealed differences in behavior between the two biocatalyst preparations due to the compounds present.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1007/s12010-013-0533-3DOI Listing
January 2014

Protic ionic liquid as additive on lipase immobilization using silica sol-gel.

Enzyme Microb Technol 2013 Mar 31;52(3):141-50. Epub 2012 Dec 31.

UNIT, Universidade Tiradentes, Instituto de Tecnologia e Pesquisa-ITP, Av. Murilo Dantas, 300, Prédio do ITP, Farolândia, Aracaju, SE, Brazil.

Ionic liquids (ILs) have evolved as a new type of non-aqueous solvents for biocatalysis, mainly due to their unique and tunable physical properties. A number of recent review papers have described a variety of enzymatic reactions conducted in IL solutions, on the other hand, to improve the enzyme's activity and stability in ILs; major methods being explored include the enzyme immobilization (on solid support, sol-gel, etc.), protic ionic liquids used as an additive process. The immobilization of the lipase from Burkholderia cepacia by the sol-gel technique using protic ionic liquids (PIL) as additives to protect against inactivation of the lipase due to release of alcohol and shrinkage of the gel during the sol-gel process was investigated in this study. The influence of various factors such as the length of the alkyl chain of protic ionic liquids (monoethanolamine-based) and a concentration range between 0.5 and 3.0% (w/v) were evaluated. The resulting hydrophobic matrices and immobilized lipases were characterised with regard to specific surface area, adsorption-desorption isotherms, pore volume (V(p)) and size (d(p)) according to nitrogen adsorption and scanning electron microscopy (SEM), physico-chemical properties (thermogravimetric - TG, differential scanning calorimetry - DSC and Fourier transform infrared spectroscopy - FTIR) and the potential for ethyl ester and emulsifier production. The total activity yields (Y(a)) for matrices of immobilized lipase employing protic ionic liquids as additives always resulted in higher values compared with the sample absent the protic ionic liquids, which represents 35-fold increase in recovery of enzymatic activity using the more hydrophobic protic ionic liquids. Compared with arrays of the immobilized biocatalyst without additive, in general, the immobilized biocatalyst in the presence of protic ionic liquids showed increased values of surface area (143-245 m(2) g(-1)) and pore size (19-38 Å). Immobilization with protic ionic liquids also favoured reduced mass loss according to TG curves (always less than 42.9%) when compared to the immobilized matrix without protic ionic liquids (45.1%), except for the sample containing 3.0% protic ionic liquids (46.5%), verified by thermogravimetric analysis. Ionic liquids containing a more hydrophobic alkyl group in the cationic moiety were beneficial for recovery of the activity of the immobilized lipase. The physico-chemical characterization confirmed the presence of the enzyme and its immobilized derivatives obtained in this study by identifying the presence of amino groups, and profiling enthalpy changes of mass loss.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1016/j.enzmictec.2012.12.007DOI Listing
March 2013

Methods and supports for immobilization and stabilization of cyclomaltodextrin glucanotransferase from Thermoanaerobacter.

Appl Biochem Biotechnol 2008 Mar 16;146(1-3):189-201. Epub 2008 Jan 16.

Chemical Engineering Department, State University of Maringa, Maringa, PR, Brazil.

Thermoanaerobacter cyclomaltodextrin glucanotransferase (CGTase) was immobilized using different supports and immobilization methods to study the effect on activity recovery. The enzyme covalently attached into glyoxyl-silica showed low activity recovery of 1.5%. The hydrophobic adsorption of the enzyme on Octadecyl-Sepabeads yielded also low activity recovery, 3.83%, and the enzyme could easily leak from the support at low ionic strength, although the immobilization yield was satisfactory, approximately 76%. The CGTase encapsulated in a sol-gel matrix gave an activity recovery of 6.94% and maximum cyclization activity at 60 degrees C, at pH 6.0. The half-time life at 60 degrees C, pH 6.0, in the presence of substrate was 100 min, which was lower than that of the free enzyme. The best activity recovery in this work (6.94%) is approximately five times smaller than that obtained previously using glyoxyl-agarose as support and covalent immobilization. Thus, the best support and method we tested so far for immobilization of CGTase is covalent attachment on glyoxyl-agarose.
View Article and Find Full Text PDF

Download full-text PDF

Source
http://dx.doi.org/10.1007/s12010-007-8092-0DOI Listing
March 2008
-->