Effect of heat, pH and shear on digestibility and antigenic characteristics of wheat gluten
| Autor: | Lata Ramchandran, Todor Vasiljevic, Toheder Rahaman |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
chemistry.chemical_classification
Antigenicity Chromatography biology Chemistry 010401 analytical chemistry 04 agricultural and veterinary sciences General Chemistry Protein aggregation 040401 food science 01 natural sciences Biochemistry Gluten Industrial and Manufacturing Engineering Hydrolysate 0104 chemical sciences Electrophoresis 0404 agricultural biotechnology biology.protein Gliadin Deamidation Digestion Food Science Biotechnology |
| Zdroj: | European Food Research and Technology. 242:1829-1836 |
| ISSN: | 1438-2385 1438-2377 |
| Popis: | Processing-induced conformational changes may affect digestibility and antigenic potential of food proteins. In vitro gastrointestinal digestibility of gluten proteins was established after treatment at various pH (3 or 7), temperature (room temperature or 100 °C) and shear (0 or 1500 s−1). Electrophoretic patterns (SDS-PAGE) of the resulting hydrolysates and antigenicity (ELISA and immunoblotting) of gliadin fraction of the proteins were also studied. Digestibility was positively correlated with α-helix/β-sheet ratio. Lower antigenic reaction shown by digested hydrolysate of gluten samples treated at pH 3 and room temperature was ascribed to its acidic deamidation and improved digestibility. Further heating to 100 °C slightly increased antigenicity. In contrast, hydrolysate of gluten at pH 7 and room temperature exhibited highest antigenicity, attributed to partial resistance of α-/β-gliadin to digestion and appearance of some new potentially antigenic polypeptides. However, heating at 100 °C caused heat-induced protein aggregation, consequently lowered digestibility and availability of antigenic components resulting in a minimum (60 % reduction) antigenicity. Overall, shear had no effect on digestibility and antigenicity irrespective of pH and temperature. Thus, antigenic potential of gliadins can be minimized by selecting appropriate parameters during processing. |
| Databáze: | OpenAIRE |
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