Abstract
Among the many factors that have been implicated as having an adverse effect on the nutritional value of proteins is a class of proteins, known as protease inhibitors, that has the ability to inhibit the proteolytic activity of proteases of diverse origin. The protease inhibitors that have been isolated from soybeans and other legumes fall biochemically into two main categories: (1) those that have a molecular weight of 20,000 to 25,000 Da with relatively few disulfi de bonds and a specifi city directed primarily toward trypsin (Kunitz inhibitor), and (2) those that have a molecular weight of only 6000 to 10,000 Da with a high proportion of cystine residues and are capable of inhibiting chymotrypsin as well as trypsin at independent binding sites (Bowman-Birk inhibitor).
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Kakade, M. L., Rackis, J. J., McGhee, J. E., and Puski, G. (1974) Determination of trypsin inhibitor activity of soy products: a collaborative analysis of an improved procedure. Cereal Chem. 51, 376–382.
Kakade, M. L., Simons, N., and Liener, I. E. (1969) An evaluation of natural vs synthetic substrates for measuring the antitryptic activity of soybean samples. Cereal Chem. 46, 518–526.
Smith, C., Megen, W. V., Twaalfhoven, L., and Hitchcock, C. (1980) The determination of trypsin inhibitor levels in foodstuffs. J. Sci. Food Agric. 31, 341–350.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 2007 Humana Press Inc., Totowa, NJ
About this protocol
Cite this protocol
Makkar, H.P.S., Siddhuraju, P., Becker, K. (2007). Trypsin Inhibitor. In: Plant Secondary Metabolites. Methods in Molecular Biology™, vol 393. Humana Press. https://doi.org/10.1007/978-1-59745-425-4_1
Download citation
DOI: https://doi.org/10.1007/978-1-59745-425-4_1
Publisher Name: Humana Press
Print ISBN: 978-1-58829-993-2
Online ISBN: 978-1-59745-425-4
eBook Packages: Springer Protocols