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Physiological-functional Properties Of Milk Whey Proteins [propriedades Fisiológicas-funcionais Das Proteínas Do Soro De Leite]
No full textThis article emphasizes the multifunctional properties of the bovine milk whey proteins, starting with the colostrum where these proteins occur in high concentrations and are reputed as responsible for the protection and passive immunization of the newborn babies. The same proteins found in colostrum in high concentrations are found in milk although at much lower concentrations. The utilization of the milk whey proteins in the form of concentrates or isolates has been found to be highly beneficial to health in the sense of decreasing the risk of infectious as well as chronical and degenerative diseases. In this article emphasis was given to the properties of whey proteins in the form of concentrates or isolates, and their hydrolysates (peptides) as immunostimulants, inhibitors of pathogenic microorganisms and some viruses, including HIV and hepatitis C viruses. In the protection against tumor's development, particularly colon cancer and protection of the gastric mucosa against ulceration by agressive ulcerogenic agents. Various actions of the milk whey protein were pointed out as defense mechanisms for cardiovascular degenerative diseases. Several research work were discussed showing the benefit of using milk whey protein to counteract undesirable metabolic and immunological effect of excessive exercise. Finally the cell growth and regeneration stimulatory properties of the milk whey growth factors were pointed out.174397409Sgarbieri, V.C., (1996) Proteínas Em Alimentos Protéicos: Propriedades- degradaçōes-modificações, 517p. , Sāo Paulo: VarelaZinsly, P.F., Sgarbieri, V.C., Pereira Dias, N.F.G., Jacobucci, H.B., Pacheco, M.T.B., Baldini, V.L.S., Produçāo piloto de concentrados de proteínas de leite bovino: Composição e valor nutritivo (2001) Braz J Food Tecnol, 4, pp. 1-8Maubois, J.-L., Fauquant, J., Famelart, M.-H., Caussin, F., Milk microfiltrate, a convenient starting material for fractionation of whey proteins and derivatives (2001) Proceedings of the 3rd International Whey Conference, pp. 59-72. , 2001Munich. Chicago: American Dairy Products InstituteHambreus, L., Nutritional aspects of milk proteins (1992) Advanced Dairy Chemistry, 1, p. 457. , Fox PL, editor. 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Identification of active peptides from caprine β-lactoglobulin hydrolysed with thermolysin (2002) Int Dairy J, 12, pp. 805-812Nurminen, M.L., Sipola, M., Kaarto, H., Pihlanto-Leppälä, A., Piiola, K., Tossavainen, O., ∝-Lactorphin lowers blood pressure measured by radiotelemetry in normotensive rats and spontaneously hypertensive rats (2000) Life Sci, 66, pp. 1535-1543Sipola, M., Finckenberg, P., Vapaatalo, H., Pihlanto-Leppälä, A., Korhonen, H., Korpela, R., ∝-Lactorphin and β-Lactorphin improve arterial function in spontaneously hypertensive rats (2002) Life Sci, 71, pp. 1245-1253Van Der Vem, C., Grupen, H., Bont, D.B.A., Voragen, A.G.J., Optimization of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology (2002) Int Dairy J, 12, pp. 813-820Léonil, J., Bos, C., Maubois, J.-L., Tomé, D., (2001) Protéines in Lait, Nutrition et Santé, pp. 45-83. , Paris: Tec. & DocTripton, K.D., Ferrando, A.A., Phillips Jr., S.M., Doyle, D., Wolfe, R.R., Postexercise net protein synthesis in human muscle from orally administered amino acids (1999) Am J Physiol, 276, pp. E628-E34Bahr, R., Rejersted, O.M., Effect of feeding and fasting on excess postexercise oxygen consumption (1991) J Appl Physiol, 71, pp. 2088-2093Roy, B.D., Tarnopolsky, M.A., McDougall, J.D., Fowles, J., Yarasheski, K.E., Effect of glucose supplement timing on protein metabolism after resistance training (1997) J Appl Physiol, 82, pp. 1882-1888Jeukendrup, A.E., Wagenmakers, A.J.M., Stegen, J.H.C.H., Gijsen, A.P., Brouns, F., Saris, W.H.M., Carbohydrate ingestion can completely suppress endogenous glucose production during exercise (1999) Am J Physiol, 276, pp. E672-E83Burke, L., Sports foods: A new market for the food industry (2000) Food Austr, 52, p. 405Davis, J.M., Bailey, S.P., Possible mechanisms of central nervous system fatigue during exercise (1987) Med Sci Sports Exerc, 19, pp. S166-S71Henderson, A.S., Black, A.L., Brooks, G.A., Leucine turnover and oxidation in trained rats during exercise (1985) Am J Physiol, 249, pp. 137-144Biolo, G., Williams, B.D., Fleming, R.Y.D., Wolfe, R.R., Insulin actin on muscle protein kinetics and amino acid transport during recovery after resistance exercise (1999) Diabets, 48, pp. 949-957Tassi, E.M.M., (1996) Desenvolvimento de Dietas para O Desempenho Físico. Comparação de Olipeptídios de ∝-Lactalbumina Com a Proteína Intacta Como Fonte Protéico-energética, No Rato [Dissertaçāo], , Campinas: Faculdade de Engenharia de Alimentos, Universidade Estadual de CampinasRamos, A.G., (2001) Utilização Das Proteínas Do Soro Lácteo Por Ratos Jovens [Dissertação], , Campinas: Faculdade de Engenharia de Alimentos, Universidade Estadual de CampinasVan Loon, L.J.C., Saris, W.H.M., Verhagen, H., Wagenmakers, A.J.M., Plasma insulin responses after ingestion of different amino acid or protein mixtures with carbohydrate (2000) Am J Clin Nutr, 72, pp. 96-105Tassi, E.M.M., Amaya-Farfan, J., Azevedo, R.M., Hydrolyzed ∝-lactalbumin as a source of protein to the exercising rat (1998) Nutr Res, 18, pp. 875-881Pimenta, F.M.V., (2002) Efeitos Do Consumo de Hidrolisado Das Proteínas Do Soro Lácteo No Desempenho Físico e No Metabolismo Protéico Do Rato Exercitado [Dissertação], , Campinas: Faculdade de Engenharia de Alimentos, Universidade Estadual de CampinasSmith, L.L., Overtraining, excessive exercise and altered immunity (2003) Sports Med, 33, pp. 347-364Elphich, G.F., Greenwood, B.N., Campisi, J., Fleshner, M., Increase serum nIgM in voluntarily physically active rats: A potential role for B1 cells (2003) J Appl Physiol, 94, pp. 660-667Belford, D.A., Rogers, M.L., Regester, G.O., Francis, G.L., Smithers, G.W., Liepe, I.J., Milk-derived growth factors as serum supplements for the growth of fibroblast and epithelial cells (1995) In Vitro Cell Dev Biol, 31, pp. 752-760Regester, G.O., Belford, D.A., Goddard, C., Howarth, G.S., Smithers, G.W., Copeland, A.C., Prospective clinical application for a growth factor extract from whey: Gut disease and wound repair (1997) Proceedings of the 3rd International Whey Conference, pp. 333-336. , Chicago. 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Protective Effect Of Bovine Milk Whey Protein Concentrate On The Ulceratire Lesions Caused By Subcutaneous Administration Of Indomethacin
No full textThe protective effect of a whey protein concentrate (WPC) was studied in three models of stomach ulcerative lesions induction: subcutaneous injection of indomethacin, and stress induced by either intraperitoneal injection of reserpine, or immobilization and holding in the cold (4°C, 2 hours). Adult Wistar rats (300-400 g) were used for acute (single-dose), repetitive, or subchronic (10 days) administration of WPC prior to treatment with the ulcerogenic factors. The best protection was achieved in the indomethacin model for repetitive and subchronic experiments, reaching 50.1% and 44%, respectively, inhibition of the ulcerative lesions, which was significant at 1% probability (P .05) compared with saline (negative control).73309314Dial, E.J., Lichtenberger, L.M., Milk protection against experimental ulcerogenesis in rats (1987) Dig Dis Sci, 10, pp. 1145-1150McIntosh, G.H., Royle, P.J., Le Leu, R.K., Rogester, G.O., Johnson, M.A., Grinsted, R.L., Renward, R.S., Smithers, G.W., Whey protein as functional food ingredients? (1998) Int Dairy J, 51, pp. 425-434Parodi, P.W., A role for milk protein in cancer prevention (1998) Aust J Dairy Technol, 53, pp. 37-47Sgarbieri, V.C., Food protein and peptides presenting specific protection to human health (1999) Food for Health in the Pacific Rim, pp. 335-352. , Food and Nutrition Press, Inc., Trumbull, CTMatsumoto, H., Shimokawa, Y., Ushida, Y., Toida, T., Hayasawa, H., New biological function of bovine α-lactalbumin: Protective effect against ethanol and stress-induced gastric mucosal injury in rats (2001) Biosci Biotechnol Biochem, 65, pp. 1104-1111Dias, P.C., Flogio, M.A., Possenti, A., Carvalho, J.E., Antiulcerogenic activity of crude hidroalcoholic extract of Rismarinus officinalis L (2000) J Ethnopharmacol, 69, pp. 57-62Borges, P.F.Z., Sgarbieri, V.C., Jacobucci, H.B., Pacheco, M.T.B., Baldini, V.L.S., Produ̧ão piloto de proteína de leite bovino: Composi̧ão e valor nutritivo (2001) Braz J Food Technol, 4, pp. 1-8Bounous, G., Gervais, F., Amer, V., Batist, G., Gold, P., The influence of dietary whey protein on tissue glutathione and diseases of aging (1989) Clin Invest Med, 12, pp. 343-349Bounous, G., Gold, P., The biological activity of undenatured dietary whey protein: Role of glutathione (1991) Clin Invest Med, 14, pp. 296-309Katory, M., Majima, M., Multiple role of inducible cyclooxigenase-2 and its selective inhibitors (1997) Nippon Yakurigaku Zasshi, 109, pp. 247-258Bighetti, A.E., (1999) Atividade Anticulcerogênica do Extrato Bruto e da Cumarina Isolada da Mikania laevigata Schultz Bip, , [disserta̧ão de mestrado em Farmacologia], Faculdade de Ciências Médicas, Universidade Estadual de Campinas, Campinas, BrazilGamberini, M.T., Skorupa, L.A., Soucar, C., Lapa, A.J., Inhibition of gastric secretion by a water extract from Baccharis triptera Mart (1991) Mem Inst Oswaldo Cruz, 86 (SUPPL. II), pp. 137-139Levine, R.J., A method for rapid production of stress ulcers in rats (1971) Peptic Ulcer, pp. 92-97. , (Pfeiffer CJ, ed.), Munksgaard, CopenhagenGupta, M.B., Tangri, K.K., Bhargava, K.P., Mechanism of ulcerogenic activity of reserpine in albino rats (1974) J Pharmacol, 27, pp. 269-271Konturek, S.J., Pawlik, W., Physiology and pharmacology of prostaglandins (1986) Dig Dis Sci, 31 (SUPPL.), pp. 6S-19SKatori, M., Majima, M., Multiple roles of inducible cycloxigenase-2 and its selective inhibitors (1997) Nippon Yakurigaku Zasshi, 109, pp. 247-258Morimoto, Y., Shimohara, K., Oshima, S., Kakayuki, S., Effects of the new antiulcer agent KB-5492 on experimental gastric mucosal lesion and gastric mucosal defensive factors, as compared to those of trepenone and cimetidine (1991) Jpn J Pharmacol, 57, pp. 495-505Das, D., Banerjee, R.K., Effects of stress on the antioxidant enzymes and gastric ulceration (1993) Mol Cell Biochem, 125, pp. 115-125Gupta, M.B., Tangri, K.K., Bhargova, K.P., Mechanism of ulcerogenic activity of reserpine in albino rats (1974) Eur J Pharmacol, 27, pp. 269-271Rosaneli, C.F., Bighetti, A.E., Antônio, M.A., Carvalho, J.E., Sgarbieri, V.C., Efficacy of a whey protein concentrate on the inhibition of stomach ulcerative lesions caused by ethanol ingestion (2002) J Med Food, 5, pp. 225-23
Caracterização de amaranto cultivado em Santa Catarina e sua utilização na produção de pães
Get PDFDissertação (mestrado) - Universidade Federal de Santa Catarina, Centro de Ciências Agrárias, Programa de Pós-graduação em Ciências dos Alimentos, Florianópolis, 2006O Amaranto (Amaranthus cruentus) cultivado no estado de Santa Catarina foi investigado quanto a sua composição centesimal, conteúdo de fibras e perfil de aminoácidos. Também foram produzidos pães enriquecidos com farinha deste pseudo cereal e avaliada a sua aceitabilidade. Para isto, os grãos de amaranto foram moídos e sua farinha foram utilizadas para formular asa receitas de pães. As porcentagens de acréscimo em relação à farinha de trigo foram de 13%, 16% e 20%. Estas formulações foram analisadas quanto à composição centesimal, fibras, perfil de aminoácidos e o produto também foi oferecido a consumidores para avaliar o nível de aceitabilidade dos provadores. As análises físico-químicas demonstraram que a o amaranto cultivado em Santa Catarina corresponde com as características citadas na literatura, quanto ao valor protéico (14,85%). A quantidade de fibras na farinha ultrapassa as quantidades citadas em trabalhos realizados com o amaranto cultivado no Distrito Federal, correspondendo 11,88g/100g, também superior aos resultados estudados até hoje, em torno de 4,5%. Seu conteúdo de lisina também apresentou uma quantidade significativa em relação aos outros cultivares de amaranto no Brasil e em outros países, que apresentaram em torno de 5 % a 6% de lisina. O amaranto cultivado em Santa Catarina apresentou, em média 9% de lisina. Os pães enriquecidos com farinha de amaranto foram analisados também quanto a temperatura de estocagem da farinha, onde uma parte ficou em temperatura ambiente e a outra sob refrigeração, estas apresentaram um conteúdo de fibras alimentares totais de 30, 53g/100g; 9,33% de proteína e 2,75%e 3.75% de lisina para pães sem refrigeração e com refrigeração, respectivamente. A aceitabilidade das quatro(4) receitas foi testada por 100 degustadores, pela escala edônica, e demonstrou que até 20% de farinha de amaranto pode ser acrescida no pão, com isso melhorando assim a qualidade nutricional, sem prejudicar as características nutricionais, visto que houve aceitação de 81% quanto à decisão de compra do pão enriquecido com farinha de amaranto
Functional (technological) Properties Of Yeast Cellular Wall Of Alcoholic Fermentation And Its Glycan, Mannan, And Glycoprotein Fractions [propriedades Funcionais (tecnológicas) Da Parede Celular De Leveduras Da Fermentação Alcoólica E Das Frações Glicana, Manana E Glicoproteína]
No full textThe objectives of the present work were the fractionation, the chemical characterization and the study of functional (technological) properties of the cell wall (CW) of yeast from alcohol fermentation and the subfractions glycan, mannan and glycoprotein. Fractionation was realized by the physico-chemical processes of extraction, centrifugation and spray drying; chemical characterization, by determination of centesimal composition and the functional properties through well-known techniques. In the cellular wall (CW), predominated protein (19%) and soluble fiber (74%). Glycoprotein presented 35.5% protein and 56% soluble fiber. In the mannnan (M) and soluble glycan (SG), the soluble fiber (70%) was predominant, whereas in the insoluble glycan (IG) predominated the insoluble fiber (70.7%). Solubility of the various fractions in aqueous media ranged from 40% to 100% and was not pH dependent. Soluble glycan showed the highest water retention capacity (14.4 g H2O/g sample) and the higher water solubility indices (WSI) were found for mannan (60%) and for glycoprotein (83.8%). The glycans (soluble and insoluble) presented good gelling properties at 12 and 14% solid concentrations. Glycoprotein, mannan and soluble glycan presented excellent emulsifying capacity (1,500 to 2,000 ml oil/g sample). The glycoprotein and soluble glycan emulsitions were the most stable. Addition of ovalbumin (0.2%) in the emulsifying media increased significantly the cellular wall and soluble glycan emulsifying capacity. It also contributed for the stabilization of the mannan (M) and glycans (IG and SG) emultions.262369379Acton, J.C., Saffle, R.L., Stability of oil-in-water emulsion. 1. 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(ed.). ChicagoYeasts and yeast derivatives: Definitions, characteristics, and processing (1987) Food Technology, 41 (2), pp. 122-125. , DZIEZAK, J.D. (ed.). 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Composition And Physicochemical Properties Of Two Protein Fractions Of Bovine Blood Serum
No full textAnimal blood from slaughterhouses represent an important source of food ingredients which have been so far underutilized. Bovine blood production in Brazil was about 3.6 X 106 in the year 2005. Besides wasting a good food quality protein, underutilization of this byproduct from the animal industry is an important cause of soil and water resources pollution. Protein concentration of both freeze-dried and spraydried bovine albumin (BSA) and globulin (BSG) was around 85.0%. Essential Amino Acid Scoring (EAAS) was 72.7% for freeze-dried BSA and 89.3% for BSG. Emulsifying and foaming properties of both protein fractions were good mainly at pH 5.5. Foaming and emulsifying capacity was higher for BSA. Nevertheless, both foam and emulsion stabilities were better for BSG. NaCl tended to decrease both surfactant properties independently of pH. Considering solubility, heat stability, emulsifying and foaming properties, both BSA and BSG should be considered good functional ingredients for the manufacturing of food products. The study not only confirmed data already reported in the literature, but also enabled exploring new features, which amplifies the potential of applications.284964972ACTON, J.C., SAFLE, R.L., Stability of oil-water emulsion 1. Effects of surface tension, level of oil, viscosity and type of meat protein (1970) Journal of Food Science, 35 (9), pp. 852-855AL-MALAH, K.I., AZZAM, M.O.J., OMARI, R.M., Emulsifying properties of BSA in different vegetable oil emulsions using conductivity technique (2000) Food Hydrocolloids, 14 (5), pp. 485-490(1990) Official methods of analysis, 1-2. , AOAC, ASSOCIATION OF OFFICIAL ANALYTICAL CHEMISTS, 15 ed. 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Effects of processing history and composition (1986) Netherlands Milk and Dairy Journal, 40, pp. 41-48DUARTE, R.T., SIMÕES, M.C.C., SGARBIERI, V.C., Bovine blood components: Fractionation, composition and nutritive value (1999) Journal of Agricultural and Food Chemistry, 47 (1), pp. 231-236ELIZALDE, B.E., BARTHOLOMAI, G.B., PILOSOF, A.M.R., The effect of pH on the relationship between hydrophilic/lipophilic characteristics and emulsification properties of soy proteins (1996) Food Science and Technology-Lebensmittel-Wissenschaft & Technologie, 29 (4), pp. 334-339ELIZALDE, B.E., Kinetics of liquid drainage from proteinstabilized foams (1991) Journal of Food Science, 56 (1), pp. 24-26ENGLARD, S., SEIFTER, S., Precipitation techniques (1990) Methods in Enzymology, 182FAO/WHO/UNU. FOOD AND AGRICULTURE ORGANIZATION/WORLD HEALTH ORGANIZATION. Report of a Joint FAO/WHO Expert Consultation on Protein Quality Evaluation. Bethesda, Maryland, 1990FRIBERG, S. E. Emulsion Stability. In Food Emulsions. Friberg, S. ELarsson, K. (Eds.). 3 ed. Nova York: [s.n.], 1976. 582 pGOMEZ-JUAREZ, C., Protein recovery from slaughterhouse wastes (1999) Bioresource Technology, 70 (2), pp. 129-133GRAHAM, D.E., PHILLIPS, M.C., Proteins at liquid interfaces. I. Kinectics of adsorption and surface denaturation (1979) Journal of Colloid Interface Science, 70 (2), pp. 403-414HOWELL, N.K., TAYLOR, C., Effect of ascorbic acid on the foaming and gelling of globular proteins (1995) International Journal of Food Science and Technology, 30 (3), pp. 321-334IBGE - INSTITUTO BRASILEIRO DE GEOGRAFIA E ESTATÍSTICA. Produção Animal, n. 4, 40 Trimestre, 2006. Disponível em: . Acesso em: 19 junho 2007JIANG, L., HE, L., FOUNTOULAKIS, M., Comparison of protein precipitation methods for sample preparation prior to proteomic analysis (2004) Journal of Chromatography A, 1023 (2), pp. 317-320KIM, S.H., KINSELLA, J.E., Surface activity of food proteins: Relationship between surface pressure development, viscoelasticity of interfacial films and foam stability of bovine serum albumin (1985) Journal of Food Science, 50 (6), pp. 1526-1530KUBOTA, N., TATSUMOTO, N., SANO, T., Recovery of serum proteins using cellulosic affinity membranes modified with tannic acid (1999) Carbohydrate Polymers, 40 (2), pp. 107-113LAEMMLI, N.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685MÁRQUEZ, E., Proteins, isoleucine, lysine and methionine content of bovine, porcine and poultry blood and their fractions (2005) Food Chemistry, 93 (3), pp. 503-505MOHANTY, B., MULVIHILL, D.M., FOX, P.F., Emulsifying properties of acidic caseins and sodium caseinate (1988) Food Chemistry, 28 (1), pp. 17-30MORR, C.V., A collaborative study to develop a standartized food protein solubility procedure (1985) Journal of Food Science, 50 (6), pp. 1715-1718MOURE, F., RENDUELES, M., DIAZ, M., Coupling process for plasma protein fractionation using ethanol precipitation and ion exchange chromatography (2003) Meat Science, 64 (4), pp. 391-398NORDE, W.GIACOMELLI, C. E. BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states. Journal of Biotechnology, n. 79, n. 1, p. 259-268, 2000PATEL, P.D., STRIPP, A.M., FRY, J.C., Whipping test for the determination of foaming capacity of protein: A collaborative study (1988) International Journal of Food Science and Technology, 23 (1), pp. 57-63PEARCE, K.N., KINSELLA, J.E., Emulsifying properties of proteins: Evaluation of a turbidimetric technique (1978) Journal of the Agricultural and Food Chemistry, 26 (3), pp. 716-723PENTEADO, M.V.C., LAJOLO, M.F., SANTOS, N.P., Functional and Nutritional Properties of Isolated Bovine Blood Proteins (1979) Journal of the Science of Food and Agriculture, 30 (8), pp. 809-815PHILLIPS, L.G., HAQUE, Z., KINSELLA, J.E., A method for the measurement of foam formation and stability (1987) Journal of Food Science, 52 (4), p. 1077RAEKER, M.O., JOHNSON, L.A., Thermal and functional properties of bovine blood plasma and egg white proteins (1995) Journal of Food Science, 60 (4), pp. 685-690RAMOS-CLAMONT, G., Functional properties of protein fractions isolated from porcine blood (2003) Journal of Food Science, 68 (4), pp. 1196-1200RITO-PALOMARES, M., DALE, C., LYDDIATT, A., Generic application of an aqueous two-phase process for protein recovery from animal blood (2000) Process Biochemistry, 35 (7), pp. 665-673SCHNEIDER, W., WOLTER, D., McCARTY, L.J., Alternatives for plasma fractionation (1976) Vox sanguinius, 31 (2), pp. 141-151SPIES, J.R., Determination of tryptophan in proteins (1967) Analytical Chemistry, 39, pp. 1412-1415TANAKA, K. Fracionamento do plasma bovino para isolamento da albumina e sua liofilização. São Paulo, 1987. Dissertaç ão - (Mestrado em Tecnologia Bioquímico Farmacêutica), Faculdade de Ciências Farmacêuticas, USPTORNBERG, E., EDIRIWEERA, N., Factors that influence the coalescence stability of protein-stabilised emulsions, estimated from the proportion of oil extracted by hexane (1988) Journal of the Science Food and Agriculture, 46 (1), pp. 93-113TYBOR, P.T., DILL, C.W., LANDMAN, W.A., Functional properties of protein isolated from bovine blood by a continuous pilot process (1975) Journal of Food Science, 40 (1), pp. 155-159WALTER, T., Effect of bovine-hemoglobin-fortified cookies on iron status of schoolchildren: A nationwide program in Chile (1993) American Journal Clinical Nutrition, 57, pp. 190-194WISMER-PEDERSEN, J., Utilization of animal blood meat products (1979) Food Technology, 33 (8), pp. 76-80YU, M., DAMODARAN, S., Kinetics of protein foam destabilization: Evaluation of a method using BSA (1991) Journal of Agricultural and Food Chemistry, 39, pp. 1555-156
Influence Of Yeast (saccharomyces Cerevisiae) Cell Wall Fractions On Some Nutritional Parameters Of Growing Rats [influência De Frações Da Parede Celular De Levedura (saccharomyces Cerevisiae) Sobre Alguns Parâmetros Nutricionais De Ratos Em Crescimento]
No full textObjective: The objective of the present work was to assess the nutritional impact of Saccharomyces cerevisiae cell wall fractions on some nutritional parameters in growing Wistar rats. Methods: Yeast (Saccharomyces cerevisiae) biomass collected without undergoing thermolysis came from the mill São José, Zillo Lorenzetti (Macatuba, SP) in a suspension of approximately 20% p/v of cells. Fractionation of the cell wall material was done by differential extraction, centrifugation, and drying in "spray dryer". The importance of the yeast cell components as dietary fibers was assessed in recently weaned Wistar rats by measuring weight gain, diet consumption (28 days), diet efficiency ratio, apparent protein digestibility, total amount of feces and lipids and cholesterol excreted in feces. Results: Rats which were submitted to diets containing glycan plus mannan gained less weight when compared with the other diets. The mannan-containing diet yielded the highest weight gain, followed by the standard AIN diet (S-AIN) and the insoluble glycan diet. Regarding diet efficiency ratio, the diet containing glycan plus mannan produced the lowest values throughout the 28 days. The highest apparent protein digestibility was obtained for the modified standard diet, for the standard AIN diet, as well as for the 10% mannan-containing diet (M). Total lipids and cholesterol excreted in the feces varied substantially among the diets. The diet containing 10% mannan was the one that promoted the greatest excretion of cholesterol. Conclusion: At the end of 28 days, the rats submitted to the glycan plus mannan-containing diets consumed less food and gained less body weight than those submitted to the other diets. Apparent digestibility of all diets was high, 98.6% on average. The amounts of total lipids and cholesterol excreted in the feces varied considerably; however, the mannan-containing diet promoted proportionally more cholesterol excretion than the other diets.212137147São Paulo. Instituto de Eletrotécnica e Energia da Universidade de São Paulo. Cana de açúcar no Brasil. São Paulo. [acesso 2007 maio 5]. Disponível em: 〈http://infoener.iee.usp.br/ scripts/biomassa/br_cana.asp〉Salgado, J.M., Sarruge, J.R., Efeito da lavagem sobre a qualidade do concentrado protéico obtido em destilaria de álcool. (1976) Rev Bras Tecnol, 7, pp. 339-344Benassi, V.T., Camargo, C.R.O., Ciacco, C.F., Caracterização química e redução do conteúdo de ácidos nucléicos das células de levedura (Saccharomyces sp.) provenientes da produção de álcool de cana. (1990) Ciênc e Tecnol Aliment, 10 (2), pp. 249-260Halász, A., Lásztity, R., (1991) Use of yeast biomass in food production, , Boca Raton: CRC Press;Yamada, E.A., Sgarbieri, V.C., Yeast (Saccharomyces cerevisiae) protein concentrate: Preparation, chemical composition and nutritional functional properties (2005) J Agric Food Chem, 53 (10), pp. 3931-3936Otero, M.A., Vasallo, M.C., Verdieira, O., Fernandez, V., Betancourt, D., A process for the complete fracionation of baker's yeast (1996) J Chem Tecnol Biotechnol, 67 (1), pp. 67-71Abreu, J., Millán, N., Effect of addition of brewer's yeast to soy protein and casein on plasma cholesterol levels of rabbits (1994) Arch Latinoam Nutr, 44 (1), pp. 18-22Sgarbieri, V.C., Pacheco, M.T.B., Physiological functional foods (1999) Braz J Food Tech, 2 (1-2), pp. 7-19Bell, P.L., Hectorne, K., Reynolds, H., Balm, L.T., Hunninghake, B.D., Cholesterol-lowering effects of psyllium hydrophilic mucilloid. Adjunct therapy to a prudent diet for patients with mild to moderate hypercholesterolemia (1989) J Am Med Assoc, 261 (23), pp. 3419-3423Robbins, E.A., Seeley, R.D., Cholesterol lowering effect of dietary yeast and yeast fractions (1977) J Food Sci, 42 (3), pp. 694-698Williams, D.L., McNamee, R.B., Jones, E.L., Pretus, H.A., Ensley, H.E., Browder, W.I., A method for the solubilization of α (1→3)-β-D-glucan isolated from Saccharomyces cerevisiae (1991) Carbohyd Res, 219, pp. 203-213Sgarbieri, V.C., Alvim, I.D., Vilela, E.S.D., Baldini, V.L.S., Bragagnolo, N., Produção piloto de derivados de levedura (Saccharomyces sp.) para uso como ingredientes na formulação de alimentos. (1999) Braz J Food Technol, 2 (1-2), pp. 119-125Kollar, R., Sturdik, E., Sajbidor, J., Complete fractionation of Saccharomyces cerevisiae biomass (1992) Food Biotechnol, 6 (3), pp. 225-237(2000) Official methods of analysis, , Association of Official Agricultural Chemists, 17th ed. 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Antiulcerative Properties Of Bovine α-lactalbumin
No full textThe capacity of α-lactalbumin to protect the rat stomach mucosa against ulcerative lesions caused by indomethacin or absolute ethanol was investigated. An α-lactalbumin prepared in the laboratory by anion exchange and molecular exclusion chromatography (Lab.α-La) and a commercial α-lactalbumin (Comm.α-La) were compared with a saline control. Comm.α-La offered 44% protection versus Lab.α-La 12%, in the indomethacin model. For absolute ethanol, no statistical difference was found in the inhibition of the development of ulcerative lesions for the two α-lactalbumins, ranging from 32% to 50%. The content of prostaglandin E2 (PGE2) and mucus increased in the mucosa after α-La intubation, suggesting that the protein protects the mucosa via stimulation of PGE2 and mucus production. Blocking free sulfhydryl groups by in vivo N-ethylmaleimide alkylation caused an increase in mucosal ulcerative lesions, suggesting the importance of sulfhydryl compounds in the gastric mucosa protection. © 2006 Elsevier Ltd. All rights reserved.16910051012Abdel-Salam, D.M.E., Czimmer, J., Debreceni, A., Szolesanyi, J., Mózsik, G., Gastric mucosal integrity: Gastric mucosal blood flow and microcirculation. 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Effects Of A Whey Protein Concentrate And It's Peptides In The Protection Of Ulcerative Lesions At Rat Gastric Mucosa [efeito De Um Hidrolisado De Proteínas De Soro De Leite E De Seus Peptídeos Na Proteção De Lesões Ulcerativas Da Mucosa Gástrica De Ratos]
No full textObjective: To assess the ability of bovine whey protein hydrolysate and its low molecular weight fraction (molecular weight ≤1kDa) to protect the gastric mucosa of rats against ulcerative process induced by three different agents. Methods: Adult Wistar rats were subjected to the indomethacin-induced ulcer (30mg/kg body weigh), absolute ethanol (1ml/animal) and immobilization and cold stress (4°C/2h), models. Results: Whey protein hydrolysate was obtained by treatment with pancreatin to a degree of hydrolysis of 20% and fractionated using a tangential flow membrane with a molecular weight cut-off of 1kDa to obtain the fraction containing low molecular weight peptides (≤1kDa). In the ethanol-induced acute ulcer model (single dose), whey protein hydrolysate inhibited the gastric lesion index by 65.5% and the double dose resulted in a 77.4% inhibition. Conclusion: For the anti-inflammatory model, the cytoprotective effect of low molecular weight peptides was stronger than that of total hydrolysate (53.1 and 71.6%, ulcerative lesion index) for single and double dose, respectively. No mucosa cytoprotective activity was found for whey protein concentrate, whey protein hydrolysate or WPHP in the immobilization and cold stress model.1914755Das, D., Banerjee, R.K., Effect of stress on the antioxidant enzymes and gastric ulceration (1993) Mol Cell Biochem, 125 (2), pp. 115-125Lewis, D.A., Hanson, P.J., Anti-ulcer drugs of plant origin (1991) Prog Med Chem, 28, pp. 201-231Dias, P.C., Flogio, M.A., Possenti, A., Carvalho, J.E., Antiulcerogenic activity of crude hidroalcoholic extract of Rosmarinus officinalis L. (2000) J. 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Utilização de rejeito de dessalinizador como meio de cultura alternativo para cultivo de Arthrospira (Spirulina) platensis
Get PDFDissertação (mestrado) - Universidade Federal de Santa Catarina, Centro de Ciências Agrárias. Programa de Pós-Graduação em Ciência dos Alimentos.Este estudo teve como objetivo a utilização de rejeito de dessalinizador no cultivo de Arthrospira platensis, cultivada em fotobiorreatores de 4 L, sob condições laboratoriais controladas de 30°C, iluminação de 140 µmol.m-2.s-1, fotoperíodo de 12 horas claro/escuro e insuflação constante de ar atmosférico. Utilizaram-se os seguintes meios de cultura: Paoletti (controle), Paoletti suplementado com 1,0 g.L-1 de NaCl (água salinizada) e rejeito de dessalinizador adicionado de 50% dos sais do Paoletti. Foram avaliadas a biomassa produzida, velocidade específica de crescimento, produtividade em células, teor total de proteínas, perfil aminoacídico, lipídios totais e composição de ácidos graxos. Os cultivos foram mantidos até o declínio do crescimento celular. Os maiores valores de biomassa (4,954 g.L-1) e produtividade em células (0,225 g.L-1) foram encontrados no rejeito de dessalinizador, enquanto que a velocidade específica de crescimento máxima (0,393 dia-1) ocorreu no cultivo em meio Paoletti. Os teores de proteína total foram de 56,17% no rejeito e 48,59% na água salinizada e, com exceção de lisina e triptofano, todos os aminoácidos essenciais encontram-se acima dos valores mínimos requeridos pela FAO. Foram obtidos teores de lipídios de 4,54% e 4,69% no rejeito e água salinizada, respectivamente, sendo que destes, 57,69% e 54,79% eram compostos de ácidos graxos saturados
Effect Of Heat Treatment On The Toxicity And Nutritive Value Of Dry Bean (phaseolus Vulgaris Var. Rosinha G2) Proteins
No full textProximate composition, amino acid pattern, and toxicity of an unheated dry bean flour and of six other materials obtained by fractionation of the flour were studied. When fed to weanling rats the flour and all six fractions were toxic. Most of the toxicity was eliminated by heating the soaked beans 2.5 min at 97 °C, but maximum PER was attained after 10 min at the same temperature. Not all trypsin inhibitor and phytohemagglutinin activities had been eliminated by any of these treatments. Autoclaving (121 °C, 15 min) decreased the availability of lysine in the whole flour and in the water-insoluble solids by 36.7 and 29.3%, respectively, whereas it did not affect significantly that of the other fractions. Heating at 121 °C for 7.5 min was deleterious to the nutritive value of the isolated protein fractions. © 1980 American Chemical Society.28593593
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