Changes in Hydrophobic Interactions among Gluten Proteins during Dough Formation

نویسندگان

چکیده

In this study, changes in hydrophobic interactions among gluten proteins were analyzed during dough mixing. Size-exclusion high-performance chromatography and two-dimensional fluorescence difference gel electrophoresis performed on extracted with 1-propanol by weakening the interaction. The amount of 30% increased from start mixing to peak consistency, suggesting that strongly aggregated weakened resulted disaggregation. 10% decreased hydration, indicating these through relatively weak interactions. extractability mainly low molecular weight glutenin, α-gliadin, γ-gliadin. monomeric after consistency. protein was ω-gliadin, ω-gliadin other A front-face analysis addition 8-anilino-1-naphthalenesulfonic acid or thioflavin T. intensity as a result exposure groups formation aggregates These results indicate importance formation.

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ژورنال

عنوان ژورنال: Processes

سال: 2021

ISSN: ['2227-9717']

DOI: https://doi.org/10.3390/pr9071244