Back to Search
Start Over
Expression of α-amylase inhibitors in diploid Triticum species
- Source :
- Food Chemistry. 135:2643-2649
- Publication Year :
- 2012
- Publisher :
- Elsevier BV, 2012.
-
Abstract
- The aim of the work was to characterize the expression of various α-amylase inhibitors (αAIs), well known anti-nutritional compounds, for the development of healthier diploid wheat-based functional foods. The salt-soluble protein fractions from the seeds of 53 accessions among Triticum monococcum subsp. monococcum (T.m.), T. monococcum subsp. boeoticum (T.b.) and Triticum urartu (T.u.) were analyzed by immunoblotting after SDS-PAGE and Urea-PAGE using polyclonal antibodies (PABs) raised against 0.19 and 0.28 αAIs expressed in bread-wheat. Reverse zymography with human saliva and Tenebrio molitor α-amylases was used to assay inhibition activity. A great variability of the expression of αAI-related proteins was observed among T.b. and T.u. PABs, and reverse zymography revealed different bands, often not correlating with those present in bread-wheat. Two-dimensional electrophoresis followed by immunoblotting and mass spectrometric analysis identified these proteins as αAIs. Interestingly, no signal was observed within T.m. accessions. This makes T.m. an important candidate for the production of novel functional foods.
- Subjects :
- Triticum monococcum
Saliva
Gene Expression
Alpha amylase inhibitor
Biology
Anti-nutritional compound
Analytical Chemistry
Gene expression
Humans
Triticum
Plant Proteins
Functional food
food and beverages
General Medicine
Einkorn
Diploidy
alpha-Amylase inhibitor
Triticum urartu
Biochemistry
Polyclonal antibodies
Seeds
biology.protein
Electrophoresis, Polyacrylamide Gel
alpha-Amylases
Ploidy
Alpha-amylase
Amylase inhibitors
Food Science
Subjects
Details
- ISSN :
- 03088146
- Volume :
- 135
- Database :
- OpenAIRE
- Journal :
- Food Chemistry
- Accession number :
- edsair.doi.dedup.....932102794ca99ae5046ccff04d000148
- Full Text :
- https://doi.org/10.1016/j.foodchem.2012.06.123