Selected physico-chemical properties of a faba bean protein isolate before and after being acetylated have been investigated using analytical ultracentrifugation, SE-and RP-HPLC, viscometry and hydrophobicity measurements using fluorescence probe techniques. The time course of relative chymotryptic
Off-flavour reduction in Vicia faba bean protein isolate
β Scribed by M. Schultz; K. Hoppe; H. Schmandke
- Book ID
- 103709829
- Publisher
- Elsevier Science
- Year
- 1988
- Tongue
- English
- Weight
- 604 KB
- Volume
- 30
- 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
2.06 . 10 ' 10 5.35 . g/ml with progressive acetylation. The depen- dence of thc CAC on the degree of acetylation was found to be significant. For FBPI stabilized n-decane/water emulsions with varying volume fraction of oil (rp) the emulsifying activity index increased from 166 to 593 m2/g whereas t
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