The protein inhibitors of amylases and peptidases isolated from cereal grains
- 1 January 1986
- journal article
- Published by Wiley in Molecular Nutrition & Food Research
- Vol. 30 (3-4) , 275-279
- https://doi.org/10.1002/food.19860300316
Abstract
The peptidase and amylase inhibitors were isolated from rye and preliminarily purified to investigate some of their properties. It was shown, that both are of albumin character despite the acetic acid solubility of the former. They are not active against the native cereal grain peptidases or amylases (rye, wheat, triticale) but the latter inhibited the animal (hog pancreas, man salivary) and bacterial (Thermamyl, NOVO) α‐amylases. In the long‐term experiments on various rye genotypes there was shown, that the peptidase inhibitor level was rather differentiated between them, but more stable as concerns particular ones. On the other hand the level differentiation of α‐amylase inhibitor between the genotypes was rather small, but that of climate much more significant.Keywords
This publication has 7 references indexed in Scilit:
- The preparation and properties of two new chromogenic substrates of trypsinPublished by Elsevier ,2004
- Wheat protein inhibitors of α-amylasePhytochemistry, 1977
- Comparison of wheat albumin inhibitors of α-amylase and trypsinPhytochemistry, 1974
- Isolation of isoinhibitors from cow colostrum by affinity chromatography on column of trypsin-Sepharose 4BCollection of Czechoslovak Chemical Communications, 1974
- A Proposition for a Unified Method of Glucoamylase Activity Determination in Microbial MaterialStarch ‐ Stärke, 1974
- Differences between Endospermal and Embryonal Trypsin Inhibitors in Barley, Wheat, and Rye.Acta Chemica Scandinavica, 1972
- [17] Amylases, α and βPublished by Elsevier ,1955