Influence of Alcalase and transglutaminase on immunoreactivity of cow milk whey proteins
2008
Barbara WRÓBLEWSKA | Lucjan JĘDRYCHOWSKI | Gyongyi HAJÓS | Erzsebet SZABÓ
The aim of the research was to determine the changes in the immunoreactivity of whey protein concentrate (WPC) modified by two enzymes: proteinase, Alcalase 2.4L FG (Novo Nordisk), and cross-linked transglutaminase (EC 2.3.2.13, ActivaTM P, m-TG, Ajinomoto). The new products were characterised by 2D electrophoresis, immunoblotting, and ELISA methods. The WPC hydrolysate obtained with Alcalase contained proteins and peptides characterised mostly by low molecular weight peptides (MW < 14.4 kDa) in the pH range of 3-10. Immunoblotting showed strong immunoreactive properties of the hydrolysate with α-la and β-lg polyclonal rabbit antibodies. The 2D electrophoretic patterns of WPC and its modified product obtained with m-TG did no differ significantly. However, the immunoblot analysis demonstrated that WPC showed a stronger reactivity towards IgE of allergic patients as compared to WPC with m-TG. ELISA methods showed that two-step hydrolysis with Alcalase followed by m-TG significantly reduced the immunoreactive properties of whey proteins. No cross reactions were observed with α-la and only about 0.6% cross-reactivity with β-lg.
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