Trypsin and chymotrypsin inhibitors activities

Authors: Liu, Keshun

Submitted to: Book Chapter
Publication Type: Book / Chapter
Publication Acceptance Date: 5/15/2024
Publication Date: 1/20/2025
Citation: Liu, K. 2025. Trypsin and chymotrypsin inhibitors activities. Book Chapter. Chapter 13. https://doi.org/10.1007/978-1-0716-4272-6_13.
DOI: https://doi.org/10.1007/978-1-0716-4272-6_13

Interpretive Summary: "Plant-Based Proteins, Production, Physiochemical, Functional, and Sensory Properties" is a series of books on Methods and Protocols in Food Science. It was edited by Y. Li. The book consists of four parts, with a total of 33 chapters on methods and protocols for plant-based proteins. It was published in January 2025, by Humana Press, an imprint of Springer Science.

Technical Abstract: Trypsin inhibitors and chymotrypsin inhibitors are protease inhibitors of protein nature. Occurring naturally in legumes, cereals, and many other species, they are considered key antinutritional factors, since they can interfere with protein digestions, induce hypersecretion of trypsin and chymotrypsin in animal digestive tracts, and lead to pancreatic enlargement and growth suppression of animals. Thermal treatments and genetic manipulation can reduce activities of the inhibitors, but complete elimination is hard to achieve. Paradoxically, during the past few decades, some protease inhibitors have been found to be beneficial in humans and animals by exerting therapeutic effects. Therefore, protease inhibitor activities remaining in food and feed products have been an important parameter, due to their significant effects on animal nutrition and human health. Historically, trypsin inhibitor activity has been a priority parameter for measurement, but lately determination of chymotrypsin inhibitor activity has also gained attention. This chapter (Chapter 13) covers the latest method for measuring trypsin inhibitor activity and the latest method for measuring chymotrypsin inhibitory activity, after a brief overview of the method development over the past half century. The latest methods feature improved sensitivity and accuracy and can express inhibitory activities in both arbitrary units and absolute amounts of trypsin or chymotrypsin inhibited for easy comparison among studies. A detailed description of the latest method for determining chymotrypsin inhibitor activity is also provided.