Protein quality of soy lines lacking Kunitz’s Trypsin Inhibitor and Lipoxygenase isozymes
Keywords:
soybeans, Trypsin inhibitors, protein quality, Trypsin inhibitor, Kunitz soybeanAbstract
Objective
The objective of this work was to evaluate the protein quality of soybean flours that differs from each other in relation to the presence of lypoxigenases and/or Kunitz’s Trypsin Inhibitor.
Methods
Biological assays with rats were carried out to evaluate Protein Efficiency Ratio, Net Protein Ratio, Net Protein Utilization and the digestibility. The determination of the aminoacid composition of the flours and the estimation of Chemical Score Corrected by Digestibility were carried out.
Results
The Protein Efficiency Ratio, Net Protein Ratio, Net Protein Utilization values for the soybean varieties were inferior to the values obtained for casein. Higher digestibility values were obtained for the flours lacking Kunitz’s Trypsin Inhibitor than for the flours with Kunitz’s Trypsin Inhibitor present, and those were very close to the values of casein. About the determination the aminoacid composition it was verified that the restraining amino acid of this soybean is lysine, not methionine, differently from what literature indicates.
Conclusions
The genetic removal of Kunitz’s Trypsin Inhibitor improves soybean protein digestibility considerably. Chemical Score Corrected by Digestibility results did not indicate difference between the flours lacking Kunitz’s Trypsin Inhibitor and those derived from flours of lines with Kunitz’s Trypsin Inhibitor present, as it was observed by the results of in vivo digestibility.
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References
Miura EMY, Binotti MAR, Camargo DS, Mizubuti IY, Ida EI. Avaliação biológica de soja com baixas atividades de inibidores de tripsina e ausência do inibidor Kunitz. Arch Latinoam Nutr 2001; 51(2):1-8.
Sant’ana LFR, Costa NMB, Oliveira MGA, Gomes MRA. Valor nutritivo e fatores antinutricionais de multimisturas utilizadas como alternativa alimentar. Braz J Food Technol 2000; 3:129-35.
Vasconcelos IM, Maia AAB, Siebra EA, Oliveira JTA, Carvalho AFFU, Melo VMM, et al. Nutritional study of two Brazilian soybean (Glycine max) cultivars differing in the contents of antinutritional and toxic proteins. J Nutr Biochem 2001; 12:55-62.
Association of Official Analytical Chemists. Official methods of analysis of the Association of Official Analytical Chemists. 14th ed. Washington, DC; 1984. 1141p.
Reeves PG, Nielsen FH, Fahey GC. AIN-93 purified diets for laboratory rodents: final report of the american institute of nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet. J Nutr 1993; 123(11):1939-51.
Bender AE, Doell BH. Note on the determination of net protein utilization by carcass analysis. Br J Nutr 1957; 11:138-43.
Miller DS, Bender AE. The determination of the net utilization of proteins by a shortened method. Br J Nutr 1955; 9:382-8.
Food and Agriculture Organization. Protein quality evaluation. Rome; 1991. 66p. (FAO Food and Nutrition Paper, 51).
Sarwar G. The protein digestibility-corrected amino acid score method overestimates quality of proteinscontaining antinutritional factors and of poorly digestible proteins supplemented with limiting amino acids in rats. J Nutr 1997; 127:758-64.
Food and Agriculture Organization. Energy and protein requirements. Geneva; 1985. 724p.
Henley EC, Kuster JM. Protein quality evaluation by protein digestibility corrected amino acid scoring. Food Technol 1994; 48:74-7.
Association of Official Analytical Chemists. Official methods of analysis of the Association of Official Analytical Chemists. 15th ed. Washington, DC; 1990. p.1105-6.
Lima GJMM. Importância da qualidade nutricional da soja e de seus subprodutos no mercado de rações: situação atual e perspectivas futuras. In: Congresso Brasileiro de Soja; 1999; Londrina. Londrina: Embrapa; 1999. 533p.
McLaugaulan JM, Keith OM. Biossays for protein quality. In: Frieedman M, editor. Protein nutritional quality of foods and feeds. New York: Marcel Dekker; 1975. p.79-85.
Rackis JJ, Gunbmann MR, Liener IE. The USDA trypsin inhibitor study. I. background, objectives and procedural details. Qual Plant Food Hum Nutr 1985; 35:213-42.
Morales de León JC, Rodrigues HB, Zardain MI. Cooking procedures fordirect consumption of whole soybeans. Arch Latinoam Nutr 1985; 35(2):326-36.
Gutierrez RR, Romano MA, Gomez MH. Evaluación nutricional y de estabilidad durante el almacenamiento de mezclas extruidas com sorgo. Arch Latinoam Nutr 1987; 37(3):503-14.
Stipanuk MH. Biochemical and physiological aspects of human nutrition. Philadelphia: Saunders Company; 2000.
Friedman M, Gumbmann MR. Nutritional improvement of soy flour through inactivation of trypsin inhibitors by sodium sulfite. J Food Sci 1986; 51:1239-41.
Herkelman KL, Cromwell GL, Pfeiffer TW, Knabe DA. Apparent digestibility of amino acids in raw and heated conventional and low trypsin inhibitor soybeans for pigs. J Anim Sci 1992; 70(3): 818-26.
Blanco A, Bressani R. Biodisponibilidad de aminoácidos in el frijol (Plhaseolus vulgaris). Arch Latinoam Nutr 1991; 41(1):38-51.
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Copyright (c) 2023 Márcia Regina Pereira MONTEIRO, Neuza Maria Brunoro COSTA, Maria Goreti de Almeida OLIVEIRA, Christiano Vieira PIRES, Maurílio Alves MOREIRA
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