Quantitative Determination of Trypsin Inhibitory Activity in Complex Matrices
Robin E.J. Spelbrink*, Pieter Jan Gerrits, Carina Mooij, Marco L.F. Giuseppin
Identifiers and Pagination:Year: 2011
First Page: 42
Last Page: 46
Publisher Id: TOFSJ-5-42
Article History:Received Date: 2/8/2011
Revision Received Date: 25/9/2011
Acceptance Date: 28/9/2011
Electronic publication date: 18/11/2011
Collection year: 2011
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
A quantitative assay using azocasein was developed to measure trypsin inhibitory activity in emulsions and other complex systems that are refractory to analysis. The method was tested for reproducibility on pure protein solutions as well as protein-containing material rich in fats and sugars, with special attention to emulsions. In the clean situation, the overall relative standard deviation was less than 6% while for the more complex systems it was less than 16%. The procedure proved robust against deliberate variations of temperature, incubation time and substrate concentration.