Results 231 to 240 of about 26,994 (292)
Recent Advances in Heat-Induced Wheat Protein Modifications. [PDF]
Food Chem XHe HJ, Li G, Obadi M, Ou X.
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Gliadin Characterization by Sans and Gliadin Nanoparticle Growth Modelization
Journal of Nanoscience and Nanotechnology, 2006Nanosized colloidal carriers can ensure a controlled and targeted therapeutic substances delivery. The original contribution of this work was to use biopolymers of vegetable source, which are an interesting alternative to synthetic polymers. The aim of this study was to prepare submicronic particles from wheat proteins: Gliadins extracted from gluten.
Orecchioni, Anne-Marie +3 more
openaire +5 more sources
An accurate fluorometric method to measure the breakdown of gliadin and gliadin peptides
Clinica Chimica Acta, 1981A simple and accurate method is described to measure the breakdown of gliadin and gliadin peptides. It involves measuring the release of the predominant amino acids glutamine and glutamic acid using a fluorometric double enzyme assay and contains none of the problems normally associated with previously used techniques.
John F. Woodley, Gordon Bruce
openaire +3 more sources
Quantification of Gliadin by Flow Cytometry
Cereal Chemistry, 2004Gliadin is a heterogeneous group of alcohol-soluble wheat storage proteins, comprising ≈50% of the gluten proteins (Campbell et al 1987; Fido et al 1997). Gliadin influences important baking properties of wheat, in particular loaf volume (Weegels et al 1994; Khatkar et al 2002) and water absorption (Dong et al 1992).
CAPPARELLI, ROSANNA +6 more
openaire +4 more sources
Lysosomal damage by gliadin and gliadin peptides; An activity not related to coeliac disease
Clinica Chimica Acta, 1979Rat-liver lysosomes have been used to determine the toxicity of gliadin fractions in relation to coeliac disease. In this study we compared the activity in acid phosphatase release from rat-liver lysosomes by casein, gliadin and by their peptic-tryptic digests. The release of acid phosphatase is not specific for gliadin.
W. T. J. M. Hekkens +2 more
openaire +3 more sources
Surface Films of Gliadin [PDF]
Nature, 1938 MITCHELL1 has reported that under suitable conditions proteins can be spread from a solution to give films the force-area curves of which show a sharp transition point in the region of 1–2 dynes/cm., the extrapolated areas of the two distinct portions of the curve being approximately 0.3 and 0.7 × 10−7gm. /sq. cm. respectively.
T. W. J. Taylor, G. I. Jenkins
openaire +1 more source