Czech J. Food Sci., 2008, 26(1):15-23 | DOI: 10.17221/1141-CJFS

Influence of Alcalase and transglutaminase on immunoreactivity of cow milk whey proteins

Barbara WRÓBLEWSKA1, Lucjan JĘDRYCHOWSKI1, Gyongyi HAJÓS2, Erzsebet SZABÓ2
1 Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences, Olsztyn, Poland
2 Central Food Research Institute, Budapest, Hungary

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.

Keywords: whey proteins; immunoreactivity; Alcalase; transglutaminase

Published: February 29, 2008  Show citation

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WRÓBLEWSKA B, JĘDRYCHOWSKI L, HAJÓS G, SZABÓ E. Influence of Alcalase and transglutaminase on immunoreactivity of cow milk whey proteins. Czech J. Food Sci. 2008;26(1):15-23. doi: 10.17221/1141-CJFS.
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