Author
Listed:
- Barbara WRÓBLEWSKA
(Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences, Olsztyn, Poland)
- Lucjan JĘDRYCHOWSKI
(Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences, Olsztyn, Poland)
- Gyongyi HAJÓS
(Central Food Research Institute, Budapest, Hungary)
- Erzsebet SZABÓ
(Central Food Research Institute, Budapest, Hungary)
Abstract
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.
Suggested Citation
Barbara WRÓBLEWSKA & Lucjan JĘDRYCHOWSKI & Gyongyi HAJÓS & Erzsebet SZABÓ, 2008.
"Influence of Alcalase and transglutaminase on immunoreactivity of cow milk whey proteins,"
Czech Journal of Food Sciences, Czech Academy of Agricultural Sciences, vol. 26(1), pages 15-23.
Handle:
RePEc:caa:jnlcjf:v:26:y:2008:i:1:id:1141-cjfs
DOI: 10.17221/1141-CJFS
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