Abstract
The inhibition of bovine trypsin by ordinary Western foods was estimated and the daily intake of trypsin inhibitor activity (TIA) from the average British diet was calculated and shown to be 330 mg per person per day. Examination of some traditional Oriental soya foods showed that most of the TIA had been removed or inactivated during processing and the remainder was further reduced during cooking. The Japanese food, miso, was an exception and showed heat-stable inhibition of unknown biological significance, associated with the presence of free fatty acids rather than the specific soya bean trypsin inhibitors which are proteins.
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References
Bollman IA, Bassler A (1960) Qualitätsprüfung von getoastetem sojaschrot. Vorschlag einer einheitlichen untersuchen methode auf urease-activität und eiweiss löslichkeit. Kraftfutter 43:104–105
British Standards Institution, London (1958) Methods of analysis of oils and fats. BS 684, p 43
Buck FF, Bier M, Nord FF (1962) Some properties of human trypsin. Arch Biochem Biophys 98:528–530
Coan MH, Travis J (1971) Interaction of human pancreatic proteinases with naturally occurring proteinase inhibitors. In: Fritz H, Tschesche H (eds) Proceedings of the International Research Conference on Proteinase Inhibitors, Munich, 4–6 November 1970. Berlin: Walter de Gruyter, pp 294–298
FAO (1971) Food balance sheets 1964–66 average. Rome: FAO, p 731
Feeney RE (1971) Comparative biochemistry of avian egg white ovomucoids and ovoinhibitors. In: Fritz H, Tschesche H (eds) Proceedings of the International Research Conference on Proteinase Inhibitors, Munich, 4–6 November 1970. Berlin: Walter de Gruyter, pp 189–195
Feeney RE, Means GE, Bigler JC (1969) Inhibition of human trypsin, plasmin and thrombin by naturally occurring inhibitors of proteolytic enzymes. J Biol Chem 244:1957–1960
Horii M, Miyazarki M (1973) Changes in soybean trypsin inhibitor during processing. I. Trypsin inhibitor contents of soybeans, other beans and soybean products. Report of the National Food Research Institute (Sokuryo Kenkyusho Kenky Hokoku) no. 28:52–58: Abstract 12J 1833 in Food Science and Technology Abstracts (1975) 7:91
Huang DY, Swanson BG, Ryan CA (1981) Stability of proteinase inhibitors in potato tubers during cooking. J Food Sci 46:287–290
Kakade ML, Rackis JJ, McGhee JE, Puski G (1974) Determination of trypsin inhibitor activity of soy products: a collaborative analysis of an improved procedure. Cereal Chem 51:376–382
Kakade ML, Simons N, Liener IE (1970) Nutritional effects induced in rats by feeding natural and synthetic trypsin inhibitors. J Nutr 100:1003–1008
Kiuchi K, Teruo O, Ebine H (1976) Accumulation of diglycerides and monoglycerides and decrease in unsaturated free fatty acids in miso. Nippon Shokuhin Kogyo Gakkaishi 23:455–459
Krogdahl A, Holm H (1979) Inhibition of human and rat pancreatic proteases by crude and purified soybean protease inhibitors. J Nutr 109:551–558
Ministere de L'Agriculture, Service de la Repression des Fraudes et du Controle de la Qualite (1975) Définition et utilisation des protéines végétals dans les devées alimentaires. Circulaire DGAF/SRF/C-1375, Paris
Ministry of Agriculture, Fisheries and Food (1975) Household food consumption and expenditure: 1973. London: Her Majesty's Stationery Office, Table 25, pp 105–108
Orr E, Adair D (1967) The production of protein foods and concentrates. London: Tropical Products Institute, Ministry of Overseas Development, pp 65–67
Platt BS (1956) The soya bean in human nutrition. Chem Ind (London):834–837
Rackis JJ (1965) Physiological properties of soybean trypsin inhibitors and their relationship to pancreatic hypertrophy and growth inhibition of rats. Fed Proc 24:1488–1493
Rackis JJ (1974) Biological and physiological factors in soybeans. J Am Oil Chem Soc 51:161A-174A
Smith C, Megen van W, Twaalhoven L, Hitchcock C (1980) The determination of trypsin inhibitor levels in foodstuffs. J Sci Food Agric 31:341–350
Wang HL, Vespa JB, Hesseltine CW (1972) Release of bound trypsin inhibitors in soybeans byRhizopus oligosporus. J Nutr 102:1495–1500
Wang HL, Swann EW, Wallen LL, Hesseltine CW (1975) Free fatty acids identified as antitryptic factor in soybeans fermented byRhizopus oligosporus. J Nutr 105:1351–1355
Watanabe T, Ebine H, Okadu M (1974) New protein food technologies in Japan. In: Altschul AM (ed) New protein foods, vol 1A: Technology. New York: Academic Press, pp 415–454
Yanatori Y, Fujita T (1976) Hypertrophy and hyperplasia in the endocrine and exocrine pancreas of rats fed soybean trypsin inhibitor or repeatedly injected with pancreozymin. Arch Histol Jpn 39:67–78
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Doell, B.H., Ebden, C.J. & Smith, C.A. Trypsin inhibitor activity of conventional foods which are part of the British diet and some soya products. Plant Food Hum Nutr 31, 139–150 (1981). https://doi.org/10.1007/BF01094038
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DOI: https://doi.org/10.1007/BF01094038