PERFIL MOLECULAR, PUREZA E ATIVIDADE DO INIBIDOR DE TRIPSINA EM ISOLADOS PROTEICOS DE FEIJÃO-CAUPI
DOI:
https://doi.org/10.1590/1983-21252018v31n123rcPalavras-chave:
Vigna unguiculata. Inibidor de tripsina. Proteína isolada.Resumo
O processo mais utilizado na preparação de isolado proteico (IP) envolve a precipitação isoelétrica da proteína. O aquecimento abrevia o tempo de preparo dos isolados. Entretanto, esse procedimento pode afetar a pureza, rendimento, perfil molecular da proteína e presença do inibidor de tripsina. Este trabalho objetivou investigar o efeito do aquecimento na produção de IP de feijão-caupi. O feijão integral (FI) cru foi moído e desengordurado com hexano e o IP foi obtido por precipitação isoelétrica com aquecimento (IPCA) e sem aquecimento (IPSA). Determinou-se o teor proteico do FI, e dos isolados pelo método de micro-Kjeldahl. Estimou-se o rendimento da extração, pela massa de proteína ao final da extração em relação à existente inicialmente no material seco. Possíveis perdas de frações proteicas foram avaliadas por eletroforese SDS-PAGE. A atividade inibitória da tripsina foi avaliada em ensaio enzimático (BAPNA: benzoil-DLarginina-p-nitroanilida). Obteve-se um IPCA (83,3% de proteína), menos puro que o IPSA (92,2%). O rendimento do IPCA foi menor (40,0%) em relação ao IPSA (42,3%). A eletroforese indicou bandas variando de 13 a 262 kDa no FI, o IPSA apresentou um perfil de frações proteicas mais próximo ao FI que o IPCA. O FI apresentou atividade inibitória, expressa em Unidades Inibitórias de Tripsina (UIT) de 32,5±0,5UIT/mg-proteína, o IPCA apresentou 12,7±0,5UIT/mg-proteína (39% do observado no FI) e, o IPSA, 8,3±0,2 UIT/mg-proteína (25,5%). O aquecimento reduz o rendimento e a pureza da proteína nos isolados. Entretanto, a atividade inibitória da tripsina é mais afetada pelo processo de isolamento.Downloads
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Referências
ASSOCIATION OF OFFICIAL ANALYTICAL CHEMISTS - AOAC. Official methods of analysis of AOAC international. Washington. 2007.
BOYE, J.; ZARE, F.; PLETCH, A. Molecular. functional and processing characteristics of whole pulses and pulse fractions and their emerging food and nutraceutical applications. Food Research International, Amsterdam, v. 43, n. 2, p. 414-431, 2010.
BUTT, M. S.; BATOOL, R. Nutritional and functional properties of some promising legumes protein isolates. Pakistan Journal of Nutrition, Dubai, v. 9, n. 4, p. 373-379, 2010.
DEAK, N. A.; JOHNSON, L. A. Effects of extraction temperature and preservation method on functionality of soy protein. Journal of the American Oil Chemists Society, Chicago, v. 84, n. 3, p. 259-268, 2007.
DUARTE, M. S. L. et al. Determination of the trypsin inhibitor activity in vitro of the black bean (Phaseolus vulgaris L.) albumin and globulin. Alimentos e Nutrição, Araraquara, v. 21, n. 3, p. 373-376, 2010.
ELHARDALLOU, S. et al. Amino acid composition of cowpea (Vigna ungiculata L. Walp.) flour and its protein isolates. Food and Nutrition Sciences, Irvine, v. 6, n. 9, p. 790-797, 2015.
FRIEDMAN, M.; BRANDON, D. L. Nutritional and health benefits of soy proteins. Journal of Agricultural and Food Chemistry, Washington, v. 49, n. 3, p. 1069-1086, 2001.
FROTA, K. M. G. et al. Cholesterol-lowering properties of whole cowpea seed and its protein isolate in hamsters. Journal of Food Science. New Jersey, v. 73, n. 9, p. 235-240, 2008.
FROTA, K. M. et al. Cowpea protein reduces LDL-cholesterol and apolipoprotein B concentrations. but does not improve biomarkers of inflammation or endothelial dysfunction in adults with moderate hypercholesterolemia. Nutrición Hospitalaria, Barcelona, v. 31, n. 4, p. 1611-1619, 2015.
FROTA, K. M. G.; SOARES, R. A. M.; ARÊAS, J. A. G. Composição química do feijão caupi (Vigna unguiculata L. Walp), cultivar BRS-Milênio. Ciência e Tecnologia de Alimentos, Campinas, v. 28, n. 2, p. 470-476, 2008.
HONIG, D. H.; RACKIS, J. J.; WOLF, W. J. Effects of pH and salt on yields. trypsin inhibitor contends. and mineral levels of soybean protein isolate and whey. Journal of Agricultural and Food Chemistry, Washington, v. 35, n. 6, p. 967-971, 1987.
HORAX, R. et al. Functional properties of protein isolate from cowpea (Vigna unguiculata L. Walp.). Journal of Food Science, Oxford, v. 69, n. 2, p. 119–121, 2004.
JOURDAN, G. A.; NOREÑA, C. P. Z.; BRANDELLI, A. Inactivation of trypsin inhibitor activity from Brazilian varieties of beans (Phaseolus vulgaris L.). Food Science and Technology International, London, v. 13, n. 3, p. 195–198, 2007.
KAKADE, M. L.; SIMONS, N.; LIENER, I. E. An evaluation of natural vs synthetic substrates for measuring the antitryptic activity of soybean samples. Cereal Chemistry, Sydney, v. 46, n. 5, p. 518-526, 1969.
KALPANADEVI, V.; MOHAN, V. R. Effect of processing on antinutrients and in vitro protein digestibility of the underutilized legume. Vigna unguiculata (L.) Walp. subsp. unguiculata. LWT-Food Science and Technology, Amsterdam, v. 51, n. 2, p. 455-461, 2013
LAEMMLI, U. K. Cleavage of structural proteins during assembly of the heat of bacteriophage T4. Nature, London, v. 227, n. 5259, p. 680-685, 1970.
LAJOLO, F. M.; GENOVESE, M. Nutritional significance of lectins and enzyme inhibitors from legumes. Journal of Agricultural and Food Chemistry, Washington, v. 50, n. 22, p. 6592-6598, 2002.
LIENER, I. E. Implications of antinutritional components in soybean foods. Critical Reviews in Food Science and Nutrition, Philadelphia, v. 34, n. 1, p. 31-67, 1994.
MARQUES, M. R. et al. Proteolytic hydrolysis of cowpea proteins is able to release peptides with hypocholesterolemic activity. Food Research International, Amsterdam, v. 77, n. 1, p. 43-49, 2015.
PEYRANO, F.; SPERONI, F.; AVANZA, M. V. Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure. Innovative Food Science and Emerging Technologies, Amsterdam, v. 33, n. 1, p. 38-46, 2016.
RANGEL, A. et al. Biological evaluation of a protein isolate from cowpea (Vigna unguiculata) seeds. Food Chemistry, Washington, v. 87, n. 4, p. 491-499, 2004.
RAYAS-DUARTE, P.; BERGERON, D.; NIELSEN, S. Screening of heat-stable trypsin inhibitors in dry beans and their partial purification from great Northern beans (Phaseolus vulgaris) using anhydrotrypsin-sepharose affinity chromatography. Journal of Agricultural and Food Chemistry, Washington, v. 40, n. 1, p. 32-42, 1992.
RIVAS-VEGA, M. E. et al. Nutritional value of cowpea (Vigna unguiculata L. Walp.) meals as ingredients in diets for Pacific white shrimp (Litopenaeus vannamei Boone). Food Chemistry, Washington, v. 97, n. 1, p. 41-49, 2006.
RUSSO, R.; REGGIANI, R. Evaluation of protein concentration. amino acid profile and antinutritional compounds in hempseed meal from dioecious and monoecious varieties. American Journal of Plant Sciences, Irvine, v. 6, n. 1, p. 14-22, 2015.
SARWAR, G.; XIAO, C.; COCKELL, K. A. Impact of antinutritional factors in food proteins on the digestibility of protein and the bioavailability of amino acids and on protein quality. The British Journal of Nutrition, London, v. 108, n. 2, p. 315-332, 2012.
SING, B. B. et al. Cowpea genetics: a review of the recent literature. In: Advances in cowpea research. Ibadan: IITA-JIRCAS. 1997. cap. 2. p. 13-15.
UZZAN, A. Vegetable protein products from seeds: technology and uses in food industry. In: HUDSON. B. J. F. (Ed.). Development in Food Proteins. New York: Elsevier Applied Science. 1988. p. 73-118.
WAGNER, J. R.; SORGENTINI, D. A.; ANÕN, M. C. Relation between Solubility and Surface Hydrophobicity as an Indicator of Modifications during Preparation Processes of Commercial and Laboratory-Prepared Soy Protein Isolates. Journal of Agricultural and Food Chemistry, Washington, v. 48, n. 8, p. 3159-3165, 2000.
WANG, M. Optimization of extraction process of protein isolate from mung bean Procedia Engineering, Amsterdam, v. 15, n. 1, p. 5250-5258, 2011.
WITHANA-GAMAGE, T. S. et al. Physicochemical. thermal and functional characterization of protein isolates from Kabuli and Desi chickpea (Cicer arietinum L.): a comparative study with soy (Glycine max) and pea (Pisum sativum L.). Journal of the Science of Food and Agriculture, New Jersey, v. 91, n. 6, p. 1022-1031, 2011.
WRIGHT, D. J.; BUMSTEAD, M. R. Legume proteins in food technology. Philosophical Transactions of the Royal Society of London, London, v. 304, n. 1120, p. 381-393, 1984.
BOYE, J.; ZARE, F.; PLETCH, A. Molecular. functional and processing characteristics of whole pulses and pulse fractions and their emerging food and nutraceutical applications. Food Research International, Amsterdam, v. 43, n. 2, p. 414-431, 2010.
BUTT, M. S.; BATOOL, R. Nutritional and functional properties of some promising legumes protein isolates. Pakistan Journal of Nutrition, Dubai, v. 9, n. 4, p. 373-379, 2010.
DEAK, N. A.; JOHNSON, L. A. Effects of extraction temperature and preservation method on functionality of soy protein. Journal of the American Oil Chemists Society, Chicago, v. 84, n. 3, p. 259-268, 2007.
DUARTE, M. S. L. et al. Determination of the trypsin inhibitor activity in vitro of the black bean (Phaseolus vulgaris L.) albumin and globulin. Alimentos e Nutrição, Araraquara, v. 21, n. 3, p. 373-376, 2010.
ELHARDALLOU, S. et al. Amino acid composition of cowpea (Vigna ungiculata L. Walp.) flour and its protein isolates. Food and Nutrition Sciences, Irvine, v. 6, n. 9, p. 790-797, 2015.
FRIEDMAN, M.; BRANDON, D. L. Nutritional and health benefits of soy proteins. Journal of Agricultural and Food Chemistry, Washington, v. 49, n. 3, p. 1069-1086, 2001.
FROTA, K. M. G. et al. Cholesterol-lowering properties of whole cowpea seed and its protein isolate in hamsters. Journal of Food Science. New Jersey, v. 73, n. 9, p. 235-240, 2008.
FROTA, K. M. et al. Cowpea protein reduces LDL-cholesterol and apolipoprotein B concentrations. but does not improve biomarkers of inflammation or endothelial dysfunction in adults with moderate hypercholesterolemia. Nutrición Hospitalaria, Barcelona, v. 31, n. 4, p. 1611-1619, 2015.
FROTA, K. M. G.; SOARES, R. A. M.; ARÊAS, J. A. G. Composição química do feijão caupi (Vigna unguiculata L. Walp), cultivar BRS-Milênio. Ciência e Tecnologia de Alimentos, Campinas, v. 28, n. 2, p. 470-476, 2008.
HONIG, D. H.; RACKIS, J. J.; WOLF, W. J. Effects of pH and salt on yields. trypsin inhibitor contends. and mineral levels of soybean protein isolate and whey. Journal of Agricultural and Food Chemistry, Washington, v. 35, n. 6, p. 967-971, 1987.
HORAX, R. et al. Functional properties of protein isolate from cowpea (Vigna unguiculata L. Walp.). Journal of Food Science, Oxford, v. 69, n. 2, p. 119–121, 2004.
JOURDAN, G. A.; NOREÑA, C. P. Z.; BRANDELLI, A. Inactivation of trypsin inhibitor activity from Brazilian varieties of beans (Phaseolus vulgaris L.). Food Science and Technology International, London, v. 13, n. 3, p. 195–198, 2007.
KAKADE, M. L.; SIMONS, N.; LIENER, I. E. An evaluation of natural vs synthetic substrates for measuring the antitryptic activity of soybean samples. Cereal Chemistry, Sydney, v. 46, n. 5, p. 518-526, 1969.
KALPANADEVI, V.; MOHAN, V. R. Effect of processing on antinutrients and in vitro protein digestibility of the underutilized legume. Vigna unguiculata (L.) Walp. subsp. unguiculata. LWT-Food Science and Technology, Amsterdam, v. 51, n. 2, p. 455-461, 2013
LAEMMLI, U. K. Cleavage of structural proteins during assembly of the heat of bacteriophage T4. Nature, London, v. 227, n. 5259, p. 680-685, 1970.
LAJOLO, F. M.; GENOVESE, M. Nutritional significance of lectins and enzyme inhibitors from legumes. Journal of Agricultural and Food Chemistry, Washington, v. 50, n. 22, p. 6592-6598, 2002.
LIENER, I. E. Implications of antinutritional components in soybean foods. Critical Reviews in Food Science and Nutrition, Philadelphia, v. 34, n. 1, p. 31-67, 1994.
MARQUES, M. R. et al. Proteolytic hydrolysis of cowpea proteins is able to release peptides with hypocholesterolemic activity. Food Research International, Amsterdam, v. 77, n. 1, p. 43-49, 2015.
PEYRANO, F.; SPERONI, F.; AVANZA, M. V. Physicochemical and functional properties of cowpea protein isolates treated with temperature or high hydrostatic pressure. Innovative Food Science and Emerging Technologies, Amsterdam, v. 33, n. 1, p. 38-46, 2016.
RANGEL, A. et al. Biological evaluation of a protein isolate from cowpea (Vigna unguiculata) seeds. Food Chemistry, Washington, v. 87, n. 4, p. 491-499, 2004.
RAYAS-DUARTE, P.; BERGERON, D.; NIELSEN, S. Screening of heat-stable trypsin inhibitors in dry beans and their partial purification from great Northern beans (Phaseolus vulgaris) using anhydrotrypsin-sepharose affinity chromatography. Journal of Agricultural and Food Chemistry, Washington, v. 40, n. 1, p. 32-42, 1992.
RIVAS-VEGA, M. E. et al. Nutritional value of cowpea (Vigna unguiculata L. Walp.) meals as ingredients in diets for Pacific white shrimp (Litopenaeus vannamei Boone). Food Chemistry, Washington, v. 97, n. 1, p. 41-49, 2006.
RUSSO, R.; REGGIANI, R. Evaluation of protein concentration. amino acid profile and antinutritional compounds in hempseed meal from dioecious and monoecious varieties. American Journal of Plant Sciences, Irvine, v. 6, n. 1, p. 14-22, 2015.
SARWAR, G.; XIAO, C.; COCKELL, K. A. Impact of antinutritional factors in food proteins on the digestibility of protein and the bioavailability of amino acids and on protein quality. The British Journal of Nutrition, London, v. 108, n. 2, p. 315-332, 2012.
SING, B. B. et al. Cowpea genetics: a review of the recent literature. In: Advances in cowpea research. Ibadan: IITA-JIRCAS. 1997. cap. 2. p. 13-15.
UZZAN, A. Vegetable protein products from seeds: technology and uses in food industry. In: HUDSON. B. J. F. (Ed.). Development in Food Proteins. New York: Elsevier Applied Science. 1988. p. 73-118.
WAGNER, J. R.; SORGENTINI, D. A.; ANÕN, M. C. Relation between Solubility and Surface Hydrophobicity as an Indicator of Modifications during Preparation Processes of Commercial and Laboratory-Prepared Soy Protein Isolates. Journal of Agricultural and Food Chemistry, Washington, v. 48, n. 8, p. 3159-3165, 2000.
WANG, M. Optimization of extraction process of protein isolate from mung bean Procedia Engineering, Amsterdam, v. 15, n. 1, p. 5250-5258, 2011.
WITHANA-GAMAGE, T. S. et al. Physicochemical. thermal and functional characterization of protein isolates from Kabuli and Desi chickpea (Cicer arietinum L.): a comparative study with soy (Glycine max) and pea (Pisum sativum L.). Journal of the Science of Food and Agriculture, New Jersey, v. 91, n. 6, p. 1022-1031, 2011.
WRIGHT, D. J.; BUMSTEAD, M. R. Legume proteins in food technology. Philosophical Transactions of the Royal Society of London, London, v. 304, n. 1120, p. 381-393, 1984.
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Publicado
11-12-2017
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Engenharia de Alimentos
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