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Functional properties of plant proteins Part 7. Rheological properties of succinylated protein isolates from faba beans (Vicia faba L.)

✍ Scribed by Prahl, L. ;Schwenke, K. D.

Publisher: John Wiley and Sons
Year: 1986
Tongue: English
Weight: 323 KB
Volume: 30
Category: Article
ISSN: 0027-769X
DOI: 10.1002/food.19860300329

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✦ Synopsis

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 and high yield values at room temper,iiure and tend to jellify without heating. There exists a critical degree of succinylation (between 50 and 80"") at which the unfolding of the proteins begins. In the unmodified and moderately succinylated proteins this unfolding is characterized by a minimum of viscosity at a transition temperature and a sharp viscosity increase by further heating in the cyclic heatingcooling diagram. The "transition" temperature of unmodified FBPI is identical with the "critical" temperature of aggregation in dilute solution. Flow curves of 10% dispersions of FBPI show a decrease of shear stress r with increasing succinylation up to a moderate degree of modification. The 49% succinylated sample shows the lowest value of T and nearly Newtonian fluid behaviour.

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