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Biochemical analysis and rheological properties of gluten modified by transglutaminase

Authors :
Jacques Lefebvre
Sandra Denery-Papini
Yves Popineau
Colette Larré
G. Deshayes
C. Desserme
ProdInra, Migration
UR 0724 Unité de recherche Biochimie et technologie des protéines
Institut National de la Recherche Agronomique (INRA)-Transformation des Produits Végétaux (T.P.V.)-Unité de recherche Biochimie et technologie des protéines (NANT LBTP)
PhysicoChimie des Macromolécules (LPCM)
Institut National de la Recherche Agronomique (INRA)
Source :
Cereal Chemistry, Cereal Chemistry, American Association of Cereal Chemists, 1999, 77 (1), pp.32-38, Cereal Chemistry, American Association of Cereal Chemists, 2000, 77 (2), pp.121-127
Publication Year :
1999
Publisher :
HAL CCSD, 1999.

Abstract

A transglutaminase from Streptoverticillium sp. was used to create new covalent intermolecular cross-links between proteins in gluten. This modification induced drastic changes in its physicochemical properties as well as in its rheological behavior. To understand these changes, we characterized the gluten extractability in acetic acid and identified the proteins of supernatant and pellet by immunoblotting using antibodies specific for each prolamin class. The proportion of soluble proteins decreased drastically after transglutaminase treatment due to the formation of large insoluble polymers as shown by SDS-PAGE. Among the constitutive proteins of gluten, the high molecular weight glutenin subunits were the most affected in the transglutaminase reaction. The rheological behavior of gluten after 18 hr of incubation with transglutaminase was studied in shear by dynamic measurements over 10-3 – 101 Hz frequency range and by creep and recovery tests. The behavior of treated glutens remained that of ...

Details

Language :
English
ISSN :
00090352
Database :
OpenAIRE
Journal :
Cereal Chemistry, Cereal Chemistry, American Association of Cereal Chemists, 1999, 77 (1), pp.32-38, Cereal Chemistry, American Association of Cereal Chemists, 2000, 77 (2), pp.121-127
Accession number :
edsair.doi.dedup.....b25aa0680f6efbf36cae86bff0c10cc2