Presença de inibidores de proteases em amostras comerciais de “faseolaminas” utilizadas como bloqueadores de carboidratos e os riscos à saúde
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Palavras-chave

faseolamina
inibidores de proteases
inibidores de tripsina
bloqueadores de carboidratos
inibidores de amilase
pâncreas

Como Citar

1.
Murra M dos S, Pessato TB, Tavano OL. Presença de inibidores de proteases em amostras comerciais de “faseolaminas” utilizadas como bloqueadores de carboidratos e os riscos à saúde. Rev Inst Adolfo Lutz [Internet]. 22º de março de 2013 [citado 26º de dezembro de 2024];72(3):198-205. Disponível em: https://periodicos.saude.sp.gov.br/RIAL/article/view/32918

Resumo

Foi investigada a veiculação de inibidores de proteases, concomitante ao consumo de “faseolamina”, cuja ingestão diária e de maneira prolongada poderia estar associada ao risco no desenvolvimento de alterações morfológicas e metabólicas de pâncreas. Dez amostras foram obtidas em farmácias de manipulação no município de Uberaba – MG, as quais são comercializadas na forma de cápsulas como “faseolamina” e uma como “farinha de feijão branco”, além de amostra de farinha preparada a partir da trituração de feijões brancos (Phaseolus vulgaris) obtidos comercialmente, sem qualquer processamento. Estas amostras foram analisadas efetuando-se a determinação de atividade de inibidores de tripsina, a determinação de proteínas totais e de atividade de inibição de amilase. Todas as amostras estudadas apresentaram atividades de
inibição de tripsina, porém com baixa ou mesmo inexistente inibição de amilase; e em algumas amostras foi detectada concentração de proteínas muito inferior ao esperado. Uma vez observada a presença de atividade de inibição de tripsina em todas as amostras estudadas, e pela inexistência de níveis seguros de consumo estabelecidos para o ser humano, e ainda baseando-se nos trabalhos sobre associação de ingestão prolongada destes inibidores com alterações de atividade pancreática, o consumo destes “bloqueadores de carboidratos” deveria ser melhor controlado.

https://doi.org/10.18241/0073-98552013721564
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Referências

1. Ferreira VA, Magalhães, R. Obesidade no Brasil: tendências atuais. Rev Port Saúde Publ. 2006; 24(2):71-81.

2. Ryan DH, Kushner R. The State of Obesity and Obesity Research. JAMA. 2010;304(16):1835-6.

3. Steyer TE, Ables A. Complementary and alternative therapies forweight loss. Prim Care Clin Office Pract. 2009; 36: 395-406.

4. Udani JK, Singh BB, Barrett ML, Preuss HG. Lowering the glycemic index of white bread using a white bean extract. Nutr J. 2009;8(52):1-5.

5. Chokshi D. Subchronic oral toxicity of a standardized white kidney bean (Phaseolus vulgaris) extract in rats. Food Chem Toxicol. 2007;45:32-40.

6. Marshall JJ, Lauda CM. Purification and Properties of Phaseolamin, an Inhibitor of α-Amylase, from the Kidney Bean (Phaseolus vulgaris). J Biol Chem.1975;250(20):8030-7.

7. Carlson GL, Li BUK, Bass P, Olsen WA. A Bean α-Amylase Inhibitor Formulation (Starch Blocker) Is Ineffective in Man. Science.1983;219:393-5.

8. Liener, IE. Toxic constituents of plants foods. 2ª ed. New York: Academic Press; 1980.

9. Liener IE, Donatucci DA, Tarcza JC. Starch blockers: a potential source of trypsin inhibitors and lectin. Am J Clin Nutr.1984; 39:196-200.

10. Deglaire A, Moughan PJ, Bos C, Tome D. Commercial Phaseolus vulgaris Extract (Starch Stopper) Increases Ileal Endogenous Amino Acid and Crude Protein Losses in the Growing Rat. J Agric Food Chem.2006;54:5197-202.

11. Holm H, Krogdahl A, Hansen LE. High and Low Inhibitor Soybean Meals Affect Human Duodenal Proteinase Activity Differently: In Vitro Comparison of Proteinase Inhibition. J Nutr.1998;118:521-5.

12. Reseland JE, Holm H, Jacobsen MB, Jenssen TG, Hanssen LE. Proteinase inhibitors induce selective stimulation of human trypsin and chymotrypsin secretion. J Nutr.1996;126(3):634-42.

13. Liener IE. Possible adverse effects of soybean anticarcinogens. J Nutr.1995;125(3):S:744-9.

14. Liener IE. Soybean protease inhibitors and pancreatic carcinogenesis. J Nutr.1996;126(2):582-3.

15. Liener IE. Trypsin inhibitors: concern of human nutrition or not? J Nutr.1986; 116(5):920-3.

16. Roebuck BD. Trypsin inhibitors: potential concern for humans?. J Nutr.1987;117(2):398-400.

17. Friess H, Kleeff J, Isenmann R, Malfertheiner P, Büchler MW. Adaptation of the Human Pancreas to Inhibition of Luminal Proteolytic Activity. Gastroenterol.1998;115(2):388-96.

18. Durigan JF, Sgarbieri,VC, Bulisani EA. Protein value of dry bean cultivars; factors interfering with biological utilization. J Agric Food Chem.1987;2(35):694-8.

19. Silva MR, Silva MAAP. Fatores antinutricionais: inibidores de proteases e lectinas. Rev Nutr.2000;13(1):3-9.

20. Al-Wesali M, Lambert N, Welham T, Domoney C. The influence of pea seed trypsin inhibitors on the in vitro digestibility of casein. J Sci Food Agric.1995;68(4):431-7.

21. Antunes PL, Sgarbieri VC. Effect of heat treatment on the toxicity value of dry bean (Phaseolus vulgaris var. Rosinha G2) proteins. J Agric Food Chem.1980;28(5):935-8.

22. Egbe IA, Akinyele IO. Effect of cooking on the antinutritional factors of lima beans (Phaseolus lunatus). Food Chem.1990;35:81-7.

23. Khattab RY, Arntfield SD. Nutritional quality of legume seeds as affected by some physical treatments 2. Antinutritional factors. Food Sci Technol.2009;42:1113-8.

24. Mulimani VH, Paramjyothi S. Effect of heat and u.v. on trypsin and chymotrypsin inhibitor activities in redgram (Cajanus cajan NCAL.). J Food Sci Technol.1993;30(1):62-3.

25. Shimelis EA, Rakshit SK. Effect of processing on antinutrients and in vitro protein digestibility of kidney bean (Phaseolus vulgaris L.) varieties grown in East África. Food Chem.2007;103:161-72.

26. Wang N, Hatcher DW, Tyler RT, Toews R, Gawalko EJ. Effect of cooking on the composition of beans (Phaseolus vulgaris L.) and chickpeas (Cicer arietinum L.). Food Res Int.2010;43:589–94.

27. Kakade ML, Rackis JJ, Mcghee JE, Puski G. Determination of trypsin inhibitor activity of soy products: a collaborative analysis of an improved procedure. Am Assoc Cereal Chem.1974;51:376-82.

28. Mosca M, Boniglia C, Carrat B, Giammarioli S, Nera V, Sanzini E. Determination of a-amylase inhibitor activity of phaseolamin from kidney bean (Phaseolus vulgaris) in dietary supplements by HPAEC-PAD. Anal Chim Acta.2008;617:192–5.

29. Association of Analytical Communities - AOAC. Official Methods of Analysis. 15th ed. Arlington, VA, 1990

30. Pires CV, Oliveira MGA, Cruz GADR, Mendes FQ, Rezende ST, Moreira MA. Composição físico-química de diferentes cultivares de feijão (Phaseolus vulgaris L.). Alim Nutr.2005;16(2):157-62.

31. Tavano OL, Silva Junior SI, Demonte A, Neves VA. Pancreatic hypertrophy in rats caused by chickpea (Cicer arietinum L.) protein intake. Alim Nutr.2005;16(1):5-10.

32. Gumbmann MR, Dugan GM, Spangler WL, Baker EC, Rackis JJ Pancreatic response in rats and mice to trypsin inhibitors from soy and potato after short- and long-term dietary exposure. J Nutr.1989;119(11):1598-607.

33. Mills PK, Beeson WL, Abbey DE, Fraser GE, Phillips RL. Dietary Habits and Past Medical History as Related to Fatal Pancreas Cancer Risk Among Adventists. Cancer.1988;61:2578-85.

34. Roebuck BD, Kaplita PV, Edwards BR, Praissman M. Effects of Dietary Fats and Soybean Protein on Azaserine-induced Pancreatic Carcinogenesis and Plasma Cholecystokinin in the Rat. Cancer Res.1987;1(47):1333-8.

35. Green GM, Lyman RL. Feedback regulation of pancreatic enzyme secretion as a mechanism for trypsin induced hypersecretion in the rat. Proc Soc Exp Biol Med.1972;140:6-12.

36. Fushiki T, Iwai K. Two hypotheses on the feedback regulation of pancreatic enzyme secretion. Faseb J.1989;3:121-6.

37. Gride JR. Role of Cholecystokinin in the Regulation of Gastrointestinal Motility. J Nutr.1994;124(8):S:1334-9.

38. Owyang C. Negative Feedback Control of Exocrine Pancreatic Secretion: Role of Cholecystokinin and Cholinergic Pathway. J Nutr.1994;124(8):S:1321-6.

39. Reidelberger RD. Cholecystokinin and Control of Food Intake. J Nutr.1994;124(8):S:1327-33.

40. Liddle RA. Regulation of Cholecystokinin Synthesis and Secretion in Rat Intestine. J Nutr.1994;124(8):S:1308-14.

41. Shrikhande SV, Barreto G, Koliopanos A. Pancreatic carcinogenesis: The impact of chronic pancreatitis and its clinical relevance. Indian J Cancer.2009;46(4):288-96.

42. Weder JK, Kahleyss R. Reaction of lentil trypsin-chymotrypsin inhibitors with human and bovine proteinases. J Agric Food Chem.2003;51(27):8045-50.

43. Nit, CA, Plahar WA. Cowpea Inhibition of human and bovine protease activities and the effects of processing. Food Control.1996;7(3):129-33.

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Este trabalho está licenciado sob uma licença Creative Commons Attribution 4.0 International License.

Copyright (c) 2013 Mariana dos Santos Murra, Tassia Batista Pessato, Olga Luisa Tavano

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