Proteins from faba beans (Vicia faba L.) - Acetylation and functional properties

✍ Scribed by Schmandke, H.

• Publisher: John Wiley and Sons
• Year: 1986
• Tongue: English
• Weight: 220 KB
• Volume: 30
• Category: Article
• ISSN: 0027-769X
• DOI: 10.1002/food.19860300326

✦ Synopsis

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 properties which are changed characteristically in comparison with the initial protein [I, 21. The blocking of basic residues by acylation r a s h i l i c i i c p i i \ c net charge and disturbs the electrostatic equilibrium between the polypeptide chains of a protein. An acylation consequently facilitates the decomposition of the structure of the native protein [3-81. This is also valid for faba bean protein in case of acetylation [9, 101.

The existing results are underlined exemplary. As stated in Table I , Table 2 and Fig. 1 the increase of reactive disulfide groups [9], small subunits [ 11, 121, shifting of endothems to lower temperatures and the decrease of endothermic heat flow [I21 in the protein, and that with an increasing acetylation degree, points also to