Gliadin ELISA Kit (DEIA292)

Regulatory status: For research use only, not for use in diagnostic procedures.

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Size
96T
Sample
food
Species Reactivity
N/A
Intended Use
Enzyme Immunoassay for the Quantitative Determination of Gliadin/Gluten in Food.
Contents of Kit
1. Microtiter plate
2. Gliadin Standards(0, 2, 6, 20, 60 ppm Gliadin)
3. Conjugate(anti-gliadin-Peroxidase)
4. Substrate Solution (TMB)
5. Stop Solution(0.5 M H2SO4)
6. Sample dilution buffer (Tris)
7. Washing Solution(PBS + Tween 20)
8. plastic foils
Storage
For more detailed information, please download the following document on our website.

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References


Fabrication of OSA Starch/Chitosan Polysaccharide-Based High Internal Phase Emulsion via Altering Interfacial Behaviors

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY

Authors: Yan, Chi; McClements, David Julian; Zhu, Yuqing; Zou, Liqiang; Zhou, Wei; Liu, Wei

This paper attempted to construct a high internal phase emulsion (HIPE) through altering interfacial behaviors using the electrostatic interaction between positive chitosan and negative octenyl succinic anhydride (OSA) starch. The partial polysaccharide complex of OSA starch/chitosan was used to stabilize HIPE, which was able to adsorb at the oil droplet interface and prevent the coalescence of oil droplets. The wettability of OSA starch was enhanced with the addition of positively charged chitosan, leading to the formation of partial complexes. The impact of pH and concentration of chitosan on the droplet size, surface charge, and interface behavior were investigated, and the formation of the polysaccharide complex was further confirmed by atomic force microscopy. The presence of the OSA starch/chitosan complex facilitated the formation of stable HIPE with a gel-like structure and satisfactory centrifugal and oxidative stability. These results are useful to provide information for fabricating polysaccharide-based HIPE delivery systems, which may help expand their application in the food industry.

Impact of aqualysin 1 peptidase from Thermus aquaticus on molecular scale changes in the wheat gluten network during bread baking

FOOD CHEMISTRY

Authors: Verbauwhede, Annelien E.; Lambrecht, Marlies A.; Fierens, Ellen; Shegay, Oksana; Brijs, Kristof; Delcour, Jan A.

The impact of Aqualysin 1 (Aq1), the thermo-active peptidase of Thermus aquaticus, on wheat albumin, globulin, gliadin and glutenin proteins during heat treatment of wheat dough and bread baking was examined. The level of protein extractable in sodium dodecyl sulfate containing medium under non-reducing conditions (SDS-EP-NR) from wheat dough decreases upon heating to a lesser extent when Aq1 is used than in control experiments. The higher SDS-EP-NR level is caused by the release by Aq1 of peptides from the repetitive gluten protein domains during baking. These peptides are also extractable from bread crumb with salt solution. The resultant thermoset gluten network in bread crumb is mainly made up by protein from non-repetitive gluten domains.

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