Ciencia e Ingeniería en Alimentos y Biotecnología

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Subject: search.filters.subject.AISLADOS PROTEICOS

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Now showing 1 - 6 of 6
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    Elaboración de un aislado proteico a partir de la torta de soya residual obtenida en el proceso mecánico de extracción de aceite
    (Universidad Técnica de Ambato. Facultad de Ciencia e Ingeniería en Alimentos y Biotecnología. Carrera de Alimentos, 2024-08) Perez Toasa, John Alexander; Paredes Escobar, Mayra Liliana
    The consumption of plant-based protein has gained relevance in the food industry due to various factors, such as the growing global population, the environmental impact of livestock farming, and the demand for healthier foods. In Ecuador, where child malnutrition is a significant challenge, the development of a protein isolate from residual soybean cake represents a promising solution to improve the availability of high-quality, low-cost proteins. The methodology employed in this study included the mechanical extraction of soybean oil to obtain the residual cake, followed by a process of protein isolation and purification. Stages of milling and sieving of the soybean meal were performed, followed by the solubilization and precipitation of the protein under specific pH conditions. A two by two experimental design was implemented to optimize the pH conditions during protein solubilization (pH 8, 8.5, and 10) and precipitation (pH 4, 4.5, and 5), evaluating their impact on the yield and purity of the protein isolate. The results demonstrated that the oil extraction process is efficient in producing a protein-rich residual fraction. The obtained protein isolate exhibited a complete amino acid profile, with threonine, lysine, and isoleucine at 0.60, 0.61, and 0.61 grams of amino acids/100 grams of protein respectively as the predominant amino acids. These findings highlight the potential of soybean protein isolate as a nutritional supplement, underscoring the importance of processing conditions in the final product's quality.
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    Determinación de la actividad antioxidante y antiinflamatoria de aislados proteicos de harina de chocho (Lupinus mutabilis Sweet) y su digestibilidad gastrointestinal in vitro
    (Universidad Técnica de Ambato. Facultad de Ciencia e Ingeniería en Alimentos. Carrera de Ingeniería Bioquímica, 2019-01) Aguinda Tanguila, Anderson Aldair; Paredes Escobar, Mayra Liliana
    Lupine is a legume, belonging to the family leguminosae (Fabaceae) of the lupinus genus, is a rich source of protein, it contains essential amino acids and unsaturated fats. The interest to study the functional properties of the cunt has increased due to the nutritional quality that it presents in relation to other legumes. In this study, gastrointestinal digestibility, antioxidant and anti-inflammatory activity of lupine protein isolates were evaluated. The protein isolates were obtained by isoelectric precipitation at different pH, presenting in their protein profile bands with molecular weights between 6.5 and 30 kDa. The highest yield (31.4 percent) and the highest protein content (96.9 percent) presented the isolate at pH 5. During the determination of the digestibility, the proteins were hydrolysed in their entirety with pepsin (2000 U for ecach mg) and pancreatin (100 U for each mg), since no polypeptides were observed in duodenal digestion. The antioxidant activity was evaluated by detecting lipid peroxidation, obtaining the best treatment at pH 5 with a concentration of 1000 μg for each ml (41.3 percent) and the anti-inflammatory activity was determined using the protein denaturation method, achieving better treatment the protein concentration of 1000 μg for each ml (18.2 percent). The lupine protein presented antioxidant and anti-inflammatory activity that could serve as a functional element providing added value to Ecuadorian foods.
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    Estudio de la actividad antioxidante de aislados proteicos de harina de haba pallar (Phaseolus Iunatus L.) y su digestibilidad gástrica y duodenal (in vitro)
    (Universidad Técnica de Ambato. Facultad de Ciencia e Ingeniería en Alimentos. Carrera de Ingeniería Bioquímica, 2018-07) Tello Fonseca, Ana Gabriela; Acosta Morales, Dayana Cristina
    In this research, the protein present in the lima - bean (Phaseolus lunatus L.) was isolated by isoelectric precipitation at pH 3, 4, 5 and 6, obtaining a superior yield at pH 6 (32, 58percent more less 0,30). In addition, quantification of protein isolates was carried out using the Biuret and Kjeldahl method, obtaining in both cases the higher protein content in the treatment at pH 5 corresponding to 71,33 percent and 42,31 percent, respectively. The protein isolates were characterized by the SDS-PAGE electrophoresis technique with the use of 2-mercaptoethanol, obtaining from it, high molecular weight protein fractions such as 7 S and 11 S globulins (acid and basic subunit) and 2 S albumins low molecular weight. Gastric digestion (DG) of the protein (in vitro) was carried out at pH 1.2, 2 and 3.2 by the action of the enzyme pepsin and duodenal digestion (DD) was carried out at pH 3.2 with pancreatin, both in the DG and DD, only the high molecular weight fraction corresponding to 7S globulins were digested, while proteins of molecular weight smaller than 45 kDa showed a low digestibility. Biologic activities: such as anti-inflammatory and antioxidant, were evaluated by the protein denaturation and the TBARS method, respectively; using the bean protein at different concentrations (100, 200, 500 and 1000) ug per ml. At pH 3 at a concentration of 1000ug per ml, the highest anti-inflammatory inhibition was obtained, corresponding to 37,55 percent, while at pH 6 the best antioxidant activity (68 percent) was obtained at a concentration of 1000 ug/ml, compared to the other pH studied.
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    Evaluación del grado de Digestibilidad gastrointestinal, Actividad antioxidante y antiinflamatoria in vitro de aislados proteicos de torta de sésamo (Sesamum indicum).
    (Universidad Técnica de Ambato. Facultad de Ciencia e Ingeniería en Alimentos. Carrera de Ingeniería en Alimentos., 2016-07) Poveda Loayza, Tatiana Nathaly; Carrillo Terán, Wilman Ismael
    The extraction, characterization, gastrointestinal digestibility and biological activities (antioxidant and anti-inflammatory) of the proteins present in defatted sesame flour were evaluated in this study. The protein extraction by isoelectric precipitation was obtained, using water and 1M salt solution (NaCl) as solvents, at different pHs of precipitation: 3,0; 4,0; 5,0; 6,0 and 7,0. The higher protein yield was obtained with protein isolate precipitated at pH7,0 with values of 14,73 and 17,21 percent, for water and salt methods, respectively. Protein profiles present in the isolates were identified with bands between 6.5 and 50 KDa with the SDS-PAGE electrophoresis method. 2S albumins, 7S globulins, and subunits acidic and basic of globulins were observed. Sesame proteins were submitted to gastric hydrolysis at pHs: 1,2; 2,0; 3,2; 4,5; 5,5 and were analyzed by SDS-PAGE electrophoresis. Isolates at pH 1.2 and 2.0 with pepsin action were hydrolyzed. This gastric enzyme had no activity at other pHs, isolates remained intact. Duodenal digestion was carried out at pH 3,2. Proteins were hydrolyzed almost entirely except for the 15 kDa protein band. Finally, protein precipitated at pH 7,0 with a concentration of 500 micrograms ml, was the best treatment, presenting the highest antioxidant activity. Using the same pH with 1000 micrograms ml of protein concentration, the protein isolate had higher anti-inflammatory activity respected to the other pHs and protein concentrations tested, with a value of: 43.23 percent.
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    Obtención de aislados proteicos de chía (Salvia hispánica L.) y evaluación in vitro de su digestibilidad gastrointestinal, actividad antiinflamatoria y antioxidante.
    (Universidad Técnica de Ambato. Facultad de Ciencia e Ingeniería en Alimentos. Carrera de Ingeniería en Alimentos., 2016-10) Cárdenas Hidalgo, Marjorie Karina; Carrillo Terán, Wilman Ismael
    Chia is an annual summer plant which is considered one of the most important crops in pre-Columbian societies, World-wide leading producers of chia are Paraguay, Canada, Bolivia, Ethiopia, Argentina, India, Mexico, China, Peru, Ecuador, Australia and Nicaragua. Currently, consumers interest is high food which can contribute to health benefits. Chia is a food species which can potentially meet these requirements. The aim of this study is to analyze the nutritional and functional properties of this seed. The defatted flour of chia is an important source of carbohydrates (31.46 percent), fibers (27.88 percent) and proteins (19.78 percent). To characterize the proteins present in chia, the isolation process by isoelectric precipitation of the protein isolate was carried out. The greater percentage yield was obtained at pH 3.0 (25.53 percent), and was determined obtaining protein by Biuret method (81.03 percent), BCA (44.92 percent) and Dumas (31.54 percent). Furthermore chia protein was analyzed by electrophoresis SDS-PAGE technique. Polypeptides were observed with a molecular weight between 14 and 66 kDa corresponding to globulins 7S and 11S and albumins. Chia proteins were subject to a process of in vitro gastrointestinal digestion, where it was found that they were completely hydrolyzed, indicating that these proteins cannot be considered allergenic are completely hydrolyzed. With regards to the functional properties of the proteins of chia, it was determined that they have anti-inflammatory activity (335.41 percent) of positive control used was diclofenac and antioxidant activity (95.98 percent) with BHT as positive control, in both cases most percent inhibition was found at pH 6.0 to a concentration of 100 micrograms per ml.
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    Caracterización de Aislados proteicos de quinua (Chenopodium quinoa Willd) y su Digestibilidad gástrica y duodenal (in vitro)
    (Universidad Técnica de Ambato. Facultad de Ciencia e Ingeniería en Alimentos. Carrera de Ingeniería en Alimentos., 2016-04) Toapanta Paredes, Mayra Alejandra; Carrillo Terán, Wilman Ismael
    This study was based on the characterization of quinoa protein isolates (Chenopodium quinoa Willd.) and evaluation of its gastric and duodenal in vitro digestibility of defatted quinoa flour. The isolates were obtained at pH 2.0; 3.0; 4.0; 5.0 and 6.0. Best yield was obtained in quinoa protein isolate obtained at pH 4.0 with 6.29 percent more less 0.03, showing a content of protein of 64.97 percent more less 0.13. The content of protein in all isolates was higher than 50 percent. The isolate quinoa protein was characterized by SDS-PAGE. The presence of 7S globulin, 11S globulins (acidic and basic subunit) and 2S albumin were observed. Subsequently, the quinoa protein isolates were hydrolyzed with pepsin 1/20 (SGF) at pH 1.2; 2,0; 3.2; 4.5 and 5.5. These samples were analyzed by SDS-PAGE electrophoresis. The proteins were completely hydrolyzed at pH 1.2 and at pH 2.0 after gastric hydrolysis. At pH 4.5 and 5.5 proteins of quinoa present resistant to hydrolysis with pepsin. After duodenal hydrolysis with a cocktail of proteolytic enzymes (chymotrypsin, trypsin, lipases, colipasas) proteins were completely hydrolyzed. Quinoa hydrolysates at pH 1.2 showed no antioxidant activity at the tested conditions with ORAC method. RP-HPLC analysis of quinoa protein isolated at pH 4.0 showed appearance of chromatographic peaks between 5 and 65 minutes. The chromatographic profile was very complex as separation was not performed with the analytical definition of the different proteins of isolated.