Methods and procedures for reducing soy trypsin inhibitor activity by means of heat treatment combined with chemical methods

J. Csapó; Cs. Albert

doi:10.2478/ausal-2018-0004

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Methods and procedures for reducing soy trypsin inhibitor activity by means of heat treatment combined with chemical methods

Acta Universitatis Sapientiae, Alimentaria

Volume 11 (2018): Issue 1 (December 2018)

By: J. Csapó and Cs. Albert

Open Access

|Dec 2018

Abstract

We have developed a new procedure for reducing soy trypsin inhibitor activity by means of heat treatment combined with chemical methods, through which soy trypsin inhibitor activity decreases to the tenth or twentieth part of the original value. We determined the optimal concentration of the applied chemicals (hydrogen-peroxide, ammonium-hydroxide) as well as the optimal temperature and duration of the treatment. The chemical procedure combined with heat treatment results in lower energy consumption as compared to the original heat treatment methods.

References

[1] H. M. Abu-Tarboush, Irradiation inactivation of some antinutritional factors in plant seeds. Journal of Agricultural and Food Chemistry, 46. (1998) 2698–2702.10.1021/jf980102x
Search in Google Scholar Back to article
[2] D. Agrahar-Murugkar, K. Jha, Effect of drying on nutritional and functional quality and electrophoretic pattern of soyflour from sprouted soybean (Glycine max). Journal of Food Science and Technology, 47. (2010) 482–487.10.1007/s13197-010-0082-5
Search in Google Scholar Back to article
[3] Cs. Albert, J. Csapó, Módszer és eljárás a szója tripszininhibítor tartalmának és ureáz enzim aktivitásának csökkentésére hőkezeléssel kombinált kémiai módszerekkel [Method and procedure for decreasing the trypsin inhibitor content and urease activity of soy-bean by chemical methods combined with heat treatment]. XXI. Nemzetközi Vegyészkonferencia [21^st International Conference of Chemistry). Csíksomlyó (Şumuleu Ciuc), 23–27 September 2015. 24.
Search in Google Scholar Back to article
[4] J. D. Astwood, J. N. Leach, R. L. Fuchs, Stability of food allergens to digestion in vitro. Nature Biotechnology, 14. (1996) 1269–1273.10.1038/nbt1096-1269
Search in Google Scholar Back to article
[5] K. Baintner, J. Csapó, Lack of acid-resistant trypsin inhibitor in mare’s colostrum: short communication. Acta Veterinarica Hungarica, 44. 1. (1996) 95–97.
Search in Google Scholar Back to article
[6] M. Bayram, A. Kaya, M. D. Öner, Changes in properties of soaking water during production of soy-bulgur. Journal of Food Engineering, 61. (2004) 221–230.10.1016/S0260-8774(03)00094-3
Search in Google Scholar Back to article
[7] S. Begum, A. Saito, X. Xu, A. Kato, Improved functional properties of the ovoinhibitor by conjugating with galactomannan. Bioscience, Biotechnology and Biochemistry, 67. (2003) 1897–1902.10.1271/bbb.67.1897
Search in Google Scholar Back to article
[8] Y. Birk, The Bowman-Birk Inhibitor. Trypsin- and chymotrypsin-inhibitor from soybeans. International Journal of Peptide and Protein Research, 2. (1985) 113–131.10.1111/j.1399-3011.1985.tb02155.x
Search in Google Scholar Back to article
[9] M. R. B. Carvalho, V. C. Sgarbieri, Heat treatment and inactivation of trypsin-chymotrypsin inhibitors and lectins from beans (Phaseolus vulgaris L.). Journal of Food Biochemistry, 21. (1997) 219–233.10.1111/j.1745-4514.1997.tb00216.x
Search in Google Scholar Back to article
[10] S. K. Cooke, H. A. Sampson, Allergenic properties of ovomucoid in man. Journal of Immunology, 159. (1997) 2026–2032.10.4049/jimmunol.159.4.2026
Search in Google Scholar Back to article
[11] J. Csapó, Zs. Csapóné Kiss (eds.),Élelmiszerés takarmányfehérjék minősítése. Mezőgazda Kiadó, Budapest, (2006).
Search in Google Scholar Back to article
[12] J. Csapó, Z. Henics, A teljesértékű szójabab aminosav összetételének alakulása a nyersfehérje-tartalom függvényében. Állattenyésztés és Takarmányozás, 2. (1990) 173–176.
Search in Google Scholar Back to article
[13] J. Csapó, Zs. Csapóné Kiss, A szója hőkezeltségének megállapítása krezolvörös festékkötési próbával. In: Takarmányanalitika. Kaposvári Egyetem,Állattudományi Kar, Kaposvár, (2010) 137.
Search in Google Scholar Back to article
[14] J. Csapó, Zs. Csapóné Kiss, A szója ureázaktivitásának meghatározása. In: Takarmányanalitika. Kaposvári Egyetem,Állattudományi Kar, Kaposvár, (2010) 136.
Search in Google Scholar Back to article
[15] U. De Vonis Bidlingmeyer, T. R. Leary, M. Laskowski, Identity of the tryptic and alpha-chymotryptic reactive sites on soybean trypsin inhibitor (Kunitz). Biochemistry, 11. (1972) 3303–3310.10.1021/bi00767a028
Search in Google Scholar Back to article
[16] C. M. DiPietro, I. E. Liener, Heat inactivation of the Kunitz and Bowman-Birk soybean protease inhibitors. Journal of Agricultural and Food Chemistry, 37. (1989) 39–44.10.1021/jf00085a010
Search in Google Scholar Back to article
[17] W. R. Finkenstadt, M. Laskowski, Resynthesis by trypsin of the cleaved peptide bond in modified soybean trypsin inhibitor. Journal of Biological Chemistry, 242. (1967) 771–773.10.1016/S0021-9258(18)96272-1
Search in Google Scholar Back to article
[18] M. Friedman, D. L. Brandon, Nutritional and health benefits of soy proteins. Journal of Agricultural and Food Chemistry, 49. (2001) 1069–1086.10.1021/jf0009246
Search in Google Scholar Back to article
[19] A. Gertler, I. Ben-Valid, Stoichiometry of interaction of chicken ovoinhibitor with pancreatic trypsin, chymotrypsin and elastase I. European Journal of Biochemistry, 110. (1980) 571–577.10.1111/j.1432-1033.1980.tb04900.x
Search in Google Scholar Back to article
[20] M. Hernandez-Infante, V. Sousa, I. Montalvo, E. Tena, Impact of microwave heating on hemagglutinins, trypsin inhibitors and protein quality of selected legume seeds. Plant Food for Human Nutrition, 52. (1998) 199–208.10.1023/A:1008033610737
Search in Google Scholar Back to article
[21] H. Huang, K. C. Kwok, H. H. Liang, Inhibitory activity and conformation changes of soybean trypsin inhibitor induced by ultrasound. Ultrasonics Sonochemistry, 15. (2008) 724–730.10.1016/j.ultsonch.2007.10.007
Search in Google Scholar Back to article
[22] R. Huber, D. Kukla, A. Rühlmann, W. Steigemenn, Pancreatic trypsin inhibitor (Kunitz) Part 1: Structure and function. Cold Spring Harbor Symposia on Quantitative Biology, 36. (1971) 141.10.1101/SQB.1972.036.01.019
Search in Google Scholar Back to article
[23] L. A. Johnson, C. W. Deyoe, W. J. Hoover, J. R. Schwenke, Inactivation of trypsin inhibitor sin aqueous soybean extracts by direct steam infusion. Cereal Chemistry, 57. (1980) 376–379.
Search in Google Scholar Back to article
[24] B. Kassell, Trypsin inhibitors from other legumes. Methods of Enzymology, 19. (1970) 862–871.10.1016/0076-6879(70)19076-8
Search in Google Scholar Back to article
[25] S. Kaur, S. Sharma, B. Dar, B. Singh, Optimization of process for reduction of antinutritional factors in edible cereal brans. Food Science and Technology International, 18. (2012) 445–454.10.1177/1082013211428236
Search in Google Scholar Back to article
[26] E. Kay, Structure-function relationships of proteinase inhibitors from soybean (Bowman-Birk) and lima bean. The Journal of Biological Chemistry, 254. (1979) 7648–7650.10.1016/S0021-9258(18)35995-7
Search in Google Scholar Back to article
[27] E. Kayitesi, K. G. Duodu, A. Minnaar, H. L. Kock, Effect of micronisation of pre-conditioned cowpeas on cooking time and sensory properties of cooked cowpeas. Journal of the Science and Food of Agriculture, 93. (2013) 838–845.10.1002/jsfa.580523080034
Search in Google Scholar Back to article
[28] A. R. Kennedy, The Bowman-Birk Inhibitor from soybeans as an anti-carcinogenic agent. American Journal of Clinical Nutrition, 68. (1998) 1406S–1412S.10.1093/ajcn/68.6.1406S9848508
Search in Google Scholar Back to article
[29] K. Kinoshita, T. Shimogiri, S. Okamoto, K. Yoshizawa, H. Mannen, H. R. Ibrahim, H. H. Cheng, Y. Maeda, Linkage mapping of chicken ovoinhibitor and ovomucoid genes to chromosome 13. Animal Genetics, 35. (2004) 356–358.10.1111/j.1365-2052.2004.01159.x
Search in Google Scholar Back to article
[30] T. Koide, T. Ikenaka, Studies on soybean trypsin inhibitors. 1. Fragmentation of soybean trypsin inhibitor (Kunitz) by limited proteolysis and by chemical cleavage. European Journal of Biochemistry, 32. (1973) 401–407.10.1111/j.1432-1033.1973.tb02622.x
Search in Google Scholar Back to article
[31] H. Kozlowska, K. Elkowicz, A. Rutkowski, Thermal inactivation of trypsin inhibitors of soybean preparations added to meat. Meat Science, 4. (1980) 95–102.10.1016/0309-1740(80)90035-2
Search in Google Scholar Back to article
[32] V. Kumar, A. Rani, V. Pandey, G. S. Chauhan, Changes in lipoxygenase isozymes and trypsin inhibitor activity in soybean during germination at different temperatures. Food Chemistry, 99. (2006) 563–568.10.1016/j.foodchem.2005.08.024
Search in Google Scholar Back to article
[33] M. Kunitz, Crystalline soybean trypsin inhibitor II. General properties. The Journal of General Physiology, 30. (1947) 291–310.10.1085/jgp.30.4.291
Search in Google Scholar Back to article
[34] M. Kunitz, Crystalline soybean trypsin inhibitor. Science, 101. (1945) 668–669.10.1126/science.101.2635.668
Search in Google Scholar Back to article
[35] K. C. Kwok, W. H. Qin, J. C. Tsang, Heat inactivation of trypsin inhibitors in soymilk at ultrahigh temperature. Journal of Food Science, 58. (1993) 859–862.10.1111/j.1365-2621.1993.tb09377.x
Search in Google Scholar Back to article
[36] MSZ EN ISO 14902:2002: Takarmányok. A tripszininhibitor aktivitásának meghatározása szójatermékekben (ISO 14902:2001) [Animal feeding stuffs. Determination of trypsin inhibitor activity of soya products (ISO 14902:2001)]. 01.06.2002.
Search in Google Scholar Back to article
[37] L. B. Naninga, M. M. Guest, On the interaction of fibrinolysine (plasmin) with the inhibitors antifibrinolysine and soybean trypsin inhibitor. Archives of Biochemistry and Biophysics, 108. (1964) 542–551.10.1016/0003-9861(64)90440-0
Search in Google Scholar Back to article
[38] M. A. Osman, P. M. Reid, C. W. Weber, Thermal inactivation of tepary bean (Phaseolus acutifolius), soybean and lima bean protease inhibitors: effect of acidic and basic pH. Food Chemistry, 78. (2002) 419–423.10.1016/S0308-8146(02)00144-9
Search in Google Scholar Back to article
[39] K. Ozawa, M. Laskowski, The reactive site of trypsin inhibitors. Journal of Biological Chemistry, 241. (1966) 3955–3961.10.1016/S0021-9258(18)99798-X
Search in Google Scholar Back to article
[40] J. Petres, Z. Márkus,É. Gelencsér, Z. Bogár, I. Gajzágó, B. Czukor, Effect of dielectric heat treatment on protein nutritional values and some antinutritional factors in soya bean. Journal of the Science of Food and Agriculture, 53. (1990) 35–41.10.1002/jsfa.2740530105
Search in Google Scholar Back to article
[41] N. D. Rawlings, D. P. Tolle, A. J. Barrett, Evolutionary families of peptidase inhibitors. Biochemical Journal, 378. (2004) 705–716.10.1042/bj20031825
Search in Google Scholar Back to article
[42] A. Salahuddin, M. A. Baig Sibghatullah, Homologous structural domains in chicken egg-white ovomucoid: characterization and acid denaturation. Proc. Int. Symp. Biomol. Struct. Interactions – Supplement Journal of Biosciences, 8. (1985) 67–87.10.1007/BF02703968
Search in Google Scholar Back to article
[43] D. J. Sessa, E. C. Baker, J. P. Friedrich, Inactivation of trypsin inhibitors in whole and cracked soybeans with sodium metabisulfite. Lebensmittel-Wissenschaft & Technologie, 21. (1988) 163–168.
Search in Google Scholar Back to article
[44] D. J. Sessa, P. E. Ghantous, Chemical inactivation of soybean trypsin inhibitors. Journal of the American Oil Chemistry Society, 64. (1987) 1682–1887.10.1007/BF02542503
Search in Google Scholar Back to article
[45] D. J. Sessa, J. K. Honey, T. C. Nelsen, Inactivation of soybean trypsin inhibitor with ascorbic acid and copper. Journal of Agricultural and Food Chemistry, 38. (1990) 1469–1474.10.1021/jf00097a008
Search in Google Scholar Back to article
[46] G. A. Silverman, P. I. Bird, R. W. Carrell, F. C. Church, P. B. Cough-lin, P. G. W. Gettins, J. A. Irwing, D. A. Lomas, C. J. Luke, R. W. Moyer, P. A. Pemberton, E. R. O’Donell, G. S. Salvesen, J. Travis, J. C. Whisstock, The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Journal of Biological Chemistry, 276. (2001) 33293–33296.10.1074/jbc.R100016200
Search in Google Scholar Back to article
[47] W. Stadelman, C. Owen. Technology and Engineering. Haworth Press, (1995).
Search in Google Scholar Back to article
[48] R. F. Steiner, The reduction and reoxidation of the disulfide bonds of soy-bean trypsin inhibitor. Biochimica and Biophysica Acta, 100. (1965) 111–121.10.1016/0304-4165(65)90433-2
Search in Google Scholar Back to article
[49] B. H. Vagadia, S. K. Vanga, V. Raghavan, Inactivation methods of soybean trypsin inhibitor – A review. Trends in Food Science and Technology, 64. (2017) 115–125.10.1016/j.tifs.2017.02.003
Search in Google Scholar Back to article
[50] C. Van der Ven, A. M. Matser, R. W. Van den Berg, Inactivation of soybean trypsin inhibitors and lipoxygenase by high-pressure processing. Journal of Agricultural and Food Chemistry, 53. (2005) 1087–1092.10.1021/jf048577d15713024
Search in Google Scholar Back to article
[51] S. K. Vanga, A. Singh, V. Raghavan, Review of conventional and novel food processing methods on food allergens. Critical Reviews of Food Science and Nutrition, 57. (2017) 2077–2094.10.1080/10408398.2015.104596526558955
Search in Google Scholar Back to article
[52] É. Vargáné Visi, J. Csapó, A száraz termikus kezelés hatása a fullfat szója D-aminosav-tartalmára. Műszaki Kémiai Napok ‘05, 26–28 April. Veszprém, (2005) 236–240.
Search in Google Scholar Back to article
[53] É. Varga-Visi, Cs. Albert, K. Lóki, J. Csapó, Evaluation of the inactivation of heat sensitive antinutritive factors in fullfat soybean. Krmiva, 48. 4. (2006) 201–205.
Search in Google Scholar Back to article
[54] É. Varga-Visi, Cs. Albert, K. Lóki, J. Csapó, Evaluation of the inactivation of heat sensitive antinutritive factors in fullfat soybean. Acta Universitatis Sapientiae, Alimentaria, 2. (2009a) 111–117.
Search in Google Scholar Back to article
[55]É. Varga-Visi, Cs. Albert, Zs. Mándoki, J. Csapó, The effect of thermic treatment conditions on the amino acid composition of soybean and maize. Acta Universitatis Sapientiae, Alimentaria, 2. (2009c) 166–173.
Search in Google Scholar Back to article
[56] É. Varga-Visi, G. Pohn, Cs. Albert, Zs. Mándoki, J. Csapó, The effect of thermic treatment conditions on the amino acid composition of soybean and maize. Krmiva, 51. (2009b) 139–144.
Search in Google Scholar Back to article
[57] T. Vearasilp, W. Laenoi, S. Vearasilp, N. Krittigamas, W. Lücke, E. Pawelzik, U. Ter Meulen, Effect of radio frequency technique on nutrient quality and destruction of trypsin inhibitor in soybean. In: E. Tielkes, C. Hülsebusch, I. Hauser (eds), The Global Food and Product Chain – Dynamics, Innovations, Conflicts, Strategies. Book of Abstracts, (2005) 384.
Search in Google Scholar Back to article
[58] L. J. Wang, D. Li, E. Tatsumi, Z. S. Liu, X. D. Chen, L. T. Li, Application of two stage ohmic heating to tofu processing. Chemical Engineering and Processing: Process Intensification, 46. (2007) 486–490.10.1016/j.cep.2006.06.017
Search in Google Scholar Back to article
[59] S. H. Yuan, S. K. C. Chang, Trypsin inhibitor activity in laboratory produced and commercial soymilk. ACS Symposium Series, 1059. (2010) 23–43.10.1021/bk-2010-1059.ch002
Search in Google Scholar Back to article
[60] Y. Zhong, Z. Wang, Y. Zhao, Impact of radio frequency, microwaving, and high hydrostatic pressure at elevated temperature on the nutritional and antinutritional components in black soybeans. Journal of Food Science, 80. (2015) C2732–C2739.10.1111/1750-3841.1313126579996
Search in Google Scholar Back to article
[61] J. M. Zhou, C. Liu, C. L. Tsou, Kinetics of trypsin inhibition by its specific inhibitors. Biochemistry, 3. (1989) 1070–1076.10.1021/bi00429a0222713358
Search in Google Scholar Back to article

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DOI: https://doi.org/10.2478/ausal-2018-0004 | Journal eISSN: 2066-7744

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Language: English

Page range: 58 - 80

Published on: Dec 24, 2018

Published by: Sapientia Hungarian University of Transylvania

In partnership with: Paradigm Publishing Services

Publication frequency: 1 issue per year

Keywords:

trypsin inhibitor,

inactivation by heat treatment,

chemical methods,

hydrogen-peroxide,

ammonium-hydroxide

Related subjects:

Business and economics,

Business management,

Industries,

Agribusiness, food industry,

Industrial chemistry,

Food science and technology

© 2018 J. Csapó, Cs. Albert, published by Sapientia Hungarian University of Transylvania
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Volume 11 (2018): Issue 1 (December 2018)