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
‘Continuous’ conformational change in succinylated faba bean protein isolates
✍ Scribed by Schwenke, K. D. ;Prahl, L. ;Danilenko, A. N. ;Grinberg, V. J. ;Tolstoguzov, V. B.
- Book ID
- 102213980
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 144 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0027-769X
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✦ Synopsis
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 monomeric subunits takes place and the unfolding of proteins begins. This 'critical step' has been found to correspond to adegree of 60-70 % succinyla-
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