Bowman-Birk inhibitor (BBI) is a protease inhibitor that affects protein digestibility; however, it is increasingly being recognised as anutraceutical and cosmeceutical molecule. In the present study, BBI concentration during soybean seed development, its loss during processing treatments, and the level in commercial soy products were determined. Significant differences for BBI concentration were observed across the genotypes and seed development stages. Genotype × seed development stage interaction was also found to be significant (P<0.05) for BBI concentration. Boiling, autoclaving, microwave irradiation, and sprouting resulted in significant (P<0.05) loss of BBI. Minimum loss was observed in sprouting, while autoclaving for 5 min completely deactivated BBI. Microwave irradiation of the soaked seeds resulted in higher BBI loss than of dry seeds. Among the commercial soy products, BBI concentration was high in soy flour brands, minuscule in ready-to-cook miso soup and undetectable in extruded soy products and roasted soy nuts.
Armstrong, W.B., Taylor, T.H., Kennedy, A.R., Melrose, R.J., Messadi, D.V. & Meyskens, F.L. (2013): Bowman-Birk inhibitor concentrate and oral leukoplakia: A random phase IIb trial. Cancer Prev. Res., 6(5), 410-418.
AICRPS (2018): Proceedings of varietal identifi cation committee meeting held on 15th March during 48th Annual Group meeting of the All India Coordinated Research Project on Soybean (AICRPS) held from March 15th to March 18th, 2018 at Raipur. p. 40.
Barac, M.B. & Stanojevic, S. (2005): The effect of microwave roasting on soybean protein composition and components with trypsin inhibitor activity. Acta Alimentaria, 34, 23-31.
Chen, Y., Xu Z., Zhang, C., Kong, X. & Hua, Y. (2014): Heat induced inactivation mechanism of Kunitz trypsin inhibitor and Bowman-Birk inhibitor in soymilk processing. Food Chem., 15 ,108-116.
Clarke, E. & Wiseman, J. (2007): Effects of extrusion conditions on trypsin inhibitor activity of full fat soybeans subsequent effects on their nutritional value for young broilers. Brit. Poultry Sci., 48, 703-712.
Clemente,A., Moreno, F.J., Marín-Manzano Mdel, C., Jiménez, E. & Domonex C. (2010): The cytotoxic effect of Bowman-Birk isoinhibitors, IBB1 and IBBD2, from soybean (Glycine max) on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases. Mol. Food Nutr. Res., 5(3), 396-405.
Clemente, A. & Arques, M.C. (2014): Bowman Birk inhibitors from legumes as colorectal chemopreventive agents. World J. Gastroentero., 20(30), 10305-10315.
Dai, H., Ciric, B., Zhang, G.X. & Rostami, A.M. (2011): Bowman-Birk inhibitor attenuates experimental autoimmune encephalomyelitis by delaying infiltration of inflammatory cell into CNS. Immunol. Res., 51, 145-152.
Dia, V.P., Gomez, T., Vernaza, G., Berhow, M., Chang, Y.K. & de Mejia, G.E. (2012): Bowman-Birk and Kunitz protease inhibitors among antinutrients and bio-actives modified by germination and hydrolysis in Brazilian soybean cultivar BRS133. J. Agr. Food Chem., 60, 7886-7894.
Fehr, W.R., Caviness, C.E., Burmood, D.T. & Pennington. J.S. (1971): Stage of development descriptions for soybeans, Glycine max (L.). Merrill. Crop Sci., 11, 929-931.
Friedman, M., Brandon, D.L., Bates, A.H. & Hymowitz, T. (1991): Comparison of a commercial soybean cultivar and an isoline lacking the Kunitz trypsin Inhibitor: Composition, nutritional value, and effects of heating. J. Agr. Food Chem., 39, 327-335.
Hernández-Ledesma, B., Hsieh, C.C. & de Lumen, B.O. (2009): Lunasin and Bowman-Birk protease inhibitor (BBI) in US commercial soy foods. Food Chem., 115, 574-580.
Kennedy A.R. (2005): The status of human trials utilizing Bowman-Birk inhibitor concentrate from soybean. -in: Sugano, M. (Ed.): Soy in health and disease prevention .CRC Press, Taylor & Francis, pp. 207-223.
Kim, J.E., Kang, Y.G., Park, J.S., Lim, T.G. & Lee, K.W. (2017): Review of soybean phytochemicals and their bioactive properties relevant for skin health. J. Food Nutr. Res., 5 ,852-858.
Kumar, V., Rani, A. & Chauhan, G.S. (2010): Nutritional value of soybean. -in: Singh, G. (Ed.) Soybean: The botany, production and uses .CAB International, pp. 375-403.
Kumar, V., Rani, A., Mittal, P. & Shuaib, M. (2019): Kunitz trypsin inhibitor in soybean: Contribution to total trypsin inhibitor activity as a function of genotype and fate during processing. J. Food Meas. Charact., 13, 1583-1590.
Kumar, V., Rani, A., Shuaib, M. & Mittal, P. (2018): Comparative assessment of trypsin inhibitor vis-à-vis Kunitz trypsin inhibitor and Bowman-Birk inhibitor activities in soybean, Food Anal. Method., 11, 2431-2437.
Lasso, J.N. (2010): The biochemical and functional food properties of Bowman Birk inhibitor. Crit. Rev. Food Sci., 48(1), 94-118.
Malkowicz, S.B., McKenna, W.G., Vaughn, D.J., Wan, X.S., Propert, K.J. & Kennedy, A.R. (2001): Effects of Bowman-Birk inhibitor concentrate in patients with benign prostatic hyperplasia. Prostate, 48(1), 16-18.
Messina, M. (2016): Soy and health update: Evaluation of the clinical and epidemiological literature. Nutrition, 8, 754.
Papastoitsis, G. & Wilson, K.A. (1991): Initiation of the degradation of the soybean Kunitz and Bowman-Birk trypsin inhibitors by a cysteine protease. J. Plant Physiol., 96, 1086-1092.
Sarkar, R., Chugh, S. & Garg, V.K. (2012): Newer and upcoming therapies for melasma. Indian J. Dermatol Ve., 78(4),417-428.
Szmigielski, M., Wesolowska-Janczarek, M. & Szczepanik, M. (2010): Determination of trypsin activity of microwave heated bean seeds using bromocresole purple index (BCPI). Pol. J. Food Nutr. Sci., 60, 329-333.