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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 289))

Abstract

Trypsin inhibitor (TI) occurs naturally in many foods from plants, notably soybean protein products. Heat treatment inactivates TI and improves nutritional quality, but residual TI activity of 5 to 20% remains after typical commercial treatments. Chronic feeding of TI or products that contain TI can inhibit trypsin and chymotrypsin, stimulate their secretion, cause hypertrophy and hyperplasia of the pancreas, and lead to adenomas and carcinomas of the exocrine pancreas. In the rat, TI promotes pancreatic carcinogenesis initiated by azaserine. Data needed for possible risk assessment on TI would include 2-year bioassays from animals treated with TI find fed diets carefully controlled for type and amount of fat (which also promotes pancreatic carcinogenesis). The effects of TI on protein nutrition would have to be considered when identifying the maximum tolerated dose. Major reductions in human dietary TI exposure may not be feasible because of the multiple sources of TI, the substantial promotion by other factors such as fat, and the adverse effects of excessive heat on food products. For risk assessment of TI in a particular food, other promotora and the feasibility of decreasing TI intake must be considered.

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© 1991 Springer Science+Business Media New York

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Hathcock, J.N. (1991). Residue Trypsin Inhibitor: Data Needs for Risk Assessment. In: Friedman, M. (eds) Nutritional and Toxicological Consequences of Food Processing. Advances in Experimental Medicine and Biology, vol 289. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2626-5_20

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  • DOI: https://doi.org/10.1007/978-1-4899-2626-5_20

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4899-2628-9

  • Online ISBN: 978-1-4899-2626-5

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