Source: https://content.sciendo.com/abstract/journals/ausal/11/1/article-p58.xml?rskey=9Y9hFJ&amp;result=5
Timestamp: 2019-04-19 09:07:01+00:00

Document:
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.
 H. M. Abu-Tarboush, Irradiation inactivation of some antinutritional factors in plant seeds. Journal of Agricultural and Food Chemistry, 46. (1998) 2698–2702.
 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.
 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 [21st International Conference of Chemistry). Csíksomlyó (Şumuleu Ciuc), 23–27 September 2015. 24.
 J. D. Astwood, J. N. Leach, R. L. Fuchs, Stability of food allergens to digestion in vitro. Nature Biotechnology, 14. (1996) 1269–1273.
 K. Baintner, J. Csapó, Lack of acid-resistant trypsin inhibitor in mare’s colostrum: short communication. Acta Veterinarica Hungarica, 44. 1. (1996) 95–97.
 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.
 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.
 Y. Birk, The Bowman-Birk Inhibitor. Trypsin- and chymotrypsin-inhibitor from soybeans. International Journal of Peptide and Protein Research, 2. (1985) 113–131.
 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.
 S. K. Cooke, H. A. Sampson, Allergenic properties of ovomucoid in man. Journal of Immunology, 159. (1997) 2026–2032.
 J. Csapó, Zs. Csapóné Kiss (eds.),Élelmiszerés takarmányfehérjék minősítése. Mezőgazda Kiadó, Budapest, (2006).
 J. Csapó, Z. Henics, A teljesértékű szójabab aminosav összetételének alakulása a nyersfehérje-tartalom függvényében. Állattenyésztés és Takarmányozás, 2. (1990) 173–176.
 J. Csapó, Zs. Csapóné Kiss, A szója hőkezeltségének megállapítása krezolvörös festékkötési próbával. In: Takarmányanalitika. Kaposvári Egyetem,Állattudományi Kar, Kaposvár, (2010) 137.
 J. Csapó, Zs. Csapóné Kiss, A szója ureázaktivitásának meghatározása. In: Takarmányanalitika. Kaposvári Egyetem,Állattudományi Kar, Kaposvár, (2010) 136.
 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.
 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.
 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.
 M. Friedman, D. L. Brandon, Nutritional and health benefits of soy proteins. Journal of Agricultural and Food Chemistry, 49. (2001) 1069–1086.
 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.
 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.
 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.
 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.
 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.
 B. Kassell, Trypsin inhibitors from other legumes. Methods of Enzymology, 19. (1970) 862–871.
 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.
 E. Kay, Structure-function relationships of proteinase inhibitors from soybean (Bowman-Birk) and lima bean. The Journal of Biological Chemistry, 254. (1979) 7648–7650.
 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.
 A. R. Kennedy, The Bowman-Birk Inhibitor from soybeans as an anti-carcinogenic agent. American Journal of Clinical Nutrition, 68. (1998) 1406S–1412S.
 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.
 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.
 H. Kozlowska, K. Elkowicz, A. Rutkowski, Thermal inactivation of trypsin inhibitors of soybean preparations added to meat. Meat Science, 4. (1980) 95–102.
 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.
 M. Kunitz, Crystalline soybean trypsin inhibitor II. General properties. The Journal of General Physiology, 30. (1947) 291–310.
 M. Kunitz, Crystalline soybean trypsin inhibitor. Science, 101. (1945) 668–669.
 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.
 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.
 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.
 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.
 K. Ozawa, M. Laskowski, The reactive site of trypsin inhibitors. Journal of Biological Chemistry, 241. (1966) 3955–3961.
 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.
 N. D. Rawlings, D. P. Tolle, A. J. Barrett, Evolutionary families of peptidase inhibitors. Biochemical Journal, 378. (2004) 705–716.
 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.
 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.
 D. J. Sessa, P. E. Ghantous, Chemical inactivation of soybean trypsin inhibitors. Journal of the American Oil Chemistry Society, 64. (1987) 1682–1887.
 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.
 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.
 W. Stadelman, C. Owen. Technology and Engineering. Haworth Press, (1995).
 R. F. Steiner, The reduction and reoxidation of the disulfide bonds of soy-bean trypsin inhibitor. Biochimica and Biophysica Acta, 100. (1965) 111–121.
 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.
 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.
 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.
 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.
 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.
 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.
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.
 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.
 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.
 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.
 S. H. Yuan, S. K. C. Chang, Trypsin inhibitor activity in laboratory produced and commercial soymilk. ACS Symposium Series, 1059. (2010) 23–43.
 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.
 J. M. Zhou, C. Liu, C. L. Tsou, Kinetics of trypsin inhibition by its specific inhibitors. Biochemistry, 3. (1989) 1070–1076.

References: V. 
 V. 
 V. 
 V. 
 V. 
 V.