Table 1 Influence of acetylation degree on gelling properties of solutions of broad bean protein isolates Product Gel firmness Short characterization of the gel WaI Unmodified protein isolate 0.9 No gel, viscous pulp Acetylated protein isolate; acetylation degree z 68% 7.4 Soft gel, brittle structur
Foaming properties of modified faba bean protein isolates
β Scribed by F.A. Husband; P.J. Wilde; D.C. Clark; H.M. Rawel; G. Muschiolik
- Book ID
- 114200280
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 945 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0268-005X
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The foaming ability (foam capacity and stability) of protein isolates from faba beans (Viciafaba L.) depends closely on the manner of isolation and treatment of the isolates. Unmodified isolates possess a moderate foaming ability with a maximum foam capacity of 210 %in alkaline solution (pH 10.0) a
Succinylation causes a step-by-step dissociation of oligomeric 11 S storage proteins into subunits (1, 2). In previous papers it was shown that with the 11 S proteins from peanuts [l], sunflower seeds [2] and rapeseeds [3] a 'critical step' of.succinylation occurs at which the dissociation into mono
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
An ultrastructural comparison is given for dispersions of a protein isolate (FBPI) from faba beans (Viciu fubu L.) and its highly acetylated derivative (AFBPI) as well as for various o/w emulsions stabilized by FBPI and AFBPI. Both protein isolates contain substantial amounts of surface-active phosp