it was demonstrated the unfolding of the protein structure by acetylation of faba bean protein isolate. The corresponding changes with regard to the flow, emulsifying and gelifying behaviour of aqueous protein solutions are described. Acetylation of proteins causes modifications of functional prope
Nutritional and functional properties of Vicia faba protein isolates and related fractions
✍ Scribed by Javier Vioque; Manuel Alaiz; Julio Girón-Calle
- Book ID
- 113626297
- Publisher
- Elsevier Science
- Year
- 2012
- Tongue
- English
- Weight
- 363 KB
- Volume
- 132
- Category
- Article
- ISSN
- 0308-8146
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The flow behaviour of unmodified and succinylated protein isolates from faba beans (FBPI) was studied in dependence on the degree of succinylation, temperature and protein concentration. The dispersions of exhaustively \uccinvl:ilcd I BPI which represent unfolded proteins show structura! viscosity a
## Abstract By acetylation of __Vicia faba__ protein it becomes in aqueous solution compatible with gelatine up to a substitution degree of about 50%. The swellability and brittleness of foils and the viscosity of aqueous solution of __Vicia faba__ protein are increased by its acetylation and these