Publications by authors named "Eliane P Cipolatti"

With the growth of the chemical industry over the last decade, the need for cheaper (and more environmentally friendly) alternatives to petrochemicals of ever-increasing cost has grown steadily. Oleochemicals and biodiesel (OC/BD) are considered as green alternatives to petroleum derivatives, because they come from renewable oils and fats. OC/BD are currently produced by the traditional energy intensive chemical catalyzed methods, which have several economic and environmental drawbacks.

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The use of new materials in the field of biofuel production has been represented as a step in the development of remarkable catalysts. The use of lipases in the production of biodiesel is often seen as a cost-limiting step, as the operating expenses in recovering such catalysts can lead to unfeasible market expectations. In this study, hydroxyapatite (HAp) particles were evaluated as a support to immobilize commercial lipase, following application in ethyl ester synthesis.

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The use of lipases from animal sources for the synthesis of new biocatalysts is barely studied in the literature. The present work focused on the immobilization of lipases from kid goat's and lamb's epiglottis in different ionic supports. For this, anionic supports (monoaminoethyl-N-aminoethyl-agarose (MANAE) and diethylaminoethyl-agarose (DEAE)) and cationic supports (carboxymethyl-agarose and sulfopropyl-agarose) were used.

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This study deals with lipase immobilization on micro- and mesoporous silica-based materials. The effects of the type of support (silica MCM-41, zeolite HZSM-5 (SAR 25), zeolite HZSM-5 (SAR 280), and the silica-aluminas Siral 10, Siral 20, and Siral 40) were investigated on the immobilization of lipase B from (CALB) and lipase from (RML). The supports that allowed the highest immobilization efficiencies for the CALB were Siral 40 (91.

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The rising pandemic caused by a coronavirus, resulted in a scientific quest to discover some effective treatments against its etiologic agent, the severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2). This research represented a significant scientific landmark and resulted in many medical advances. However, efforts to understand the viral mechanism of action and how the human body machinery is subverted during the infection are still ongoing.

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Enzymes are biocatalysts known for versatility, selectivity, and brand operating conditions compared to chemical catalysts. However, there are limitations to their large-scale application, such as the high costs of enzymes and their low stability under extreme reaction conditions. Immobilization techniques can efficiently solve these problems; nevertheless, most current methods lead to a significant loss of enzymatic activity and require several steps of activation and functionalization of the supports.

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A suitable immobilized lipase for esters syntheses should be selected considering not only its cost. We evaluated five biocatalysts in syntheses of octyl caprylate, octyl caprate, and octyl laurate, in which conversions higher than 90% were achieved. Novozym 435 and non-commercial preparations (including a dry fermented solid) were selected for short-term octyl laurate syntheses using different biocatalysts loadings.

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This work aimed the application of a new biocatalyst for biodiesel production from residual agro-industrial fatty acids. A recombinant Pichia pastoris displaying lipase from Rhizomucor miehei (RML) on the cell surface, using the PIR-1 anchor system, were prepared using glycerol as the carbon source. The biocatalyst, named RML-PIR1 showed optimum temperature of 45 °C (74.

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Nanobiocatalysts were produced via immobilization of CalB lipase on polyurethane (PU) based nanoparticles and their application on the synthesis of important industrial products was evaluated. Nanoparticles of polyurethane functionalized with poly(ethylene glycol) (PU-PEG) were synthetized through miniemulsion polymerization and the addition of crosslinking agents were evaluated. The nanoparticles were employed as support for CalB and the kinetic parameters were reported.

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The oleaginous yeast R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba () cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The R25L270 lipase efficiently hydrolyzed vegetable and animal oils, and showed selectivity for generating -5,8,11,15,17-eicosapentaenoic acid from sardine oil.

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With the aim of studying the best method for the interaction of polyurethane (PU) foam and Candida antarctica lipase B, different methods of CalB immobilization were studied: adsorption (PU-ADS), bond (using polyethyleneimine) (PU-PEI), ionic adsorption by PEI with cross-linking with glutaraldehyde (PU-PEI-GA) and entrapment (PU). The characterization of immobilized enzyme derivatives was performed by apparent density and Fourier transform infrared spectroscopy. The free enzyme and enzyme preparations were evaluated at different pH values and temperatures.

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With the objective to obtain immobilized Candida antarctica lipase B (CalB) with good activity and improved utilization rate, this study evaluated the influence of enzyme and crodamol concentrations and initiator type on the CalB enzyme immobilization in nanoparticles consisting of poly(methyl methacrylate) (PMMA) obtained by miniemulsion polymerization. The kinetic study of immobilized CalB enzyme in PMMA nanoparticles was evaluated in terms of monomer conversion, particle size, zeta potential, and relative activity. The optimum immobilization condition for CalB was compared with free enzyme in the p-NPL hydrolysis activity measurement.

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The aim of this study was to evaluate fermented rice bran phospholipids, lipids and fatty acid content in a fermentation solid system with Rhizopus oryzae fungus. For this, aliquots were withdrawn every 24h over 120 h. The content of phospholipids was determined by colorimetric method.

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