Immunoreactivity of acetylated and succinylated pea proteins

Szymkiewicz, A. and Jędrychowski, L. (2009) Immunoreactivity of acetylated and succinylated pea proteins. Acta Alimentaria, 38 (3). pp. 329-339. ISSN 0139-3006

Text aalim.2009.0002.pdf Restricted to Repository staff only until 30 September 2029. Download (397kB)

Abstract

Proteins of pea variety Kwestor, grown in Poland, were modified with acetic or succinic anhydride (0.01–1.0 g/g anhydride/protein). Degree of acylation, electrophoretic properties (SDS-PAGE) and immunoreactivity (by ELISA) were studied. The study indicates that not only the degree of acylation but also the type of anhydrides affected the extent of changes in the immunoreactivity of individual pea proteins. The greatest reductions in the immunoreactivity of albumins and legumin were observed during acylation with 0.2 g anhydrides (by 91–99% and 79–97% during succinylation and acetylation, respectively). The lowest immunoreactivity of vicilin fraction was found when 1.0 g of anhydride was used (about 6% during succinylation and 14.7% during acetylation as compared to the immunoreactivity of vicilin in native pea proteins).

Actions (login required)

Edit Item