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Proteolysis by Lactobacillus fermentum IFO3956 isolated from Egyptian milk products decreases immuno-reactivity of αS1-casein

Published online by Cambridge University Press:  09 March 2011

Shady El-Ghaish ,
Hanitra Rabesona ,
Yvan Choiset ,
Mahmoud Sitohy ,
Thomas Haertlé  and
Jean-Marc Chobert
Shady El-Ghaish
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, F-44300 Nantes
Hanitra Rabesona
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, F-44300 Nantes
Yvan Choiset
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, F-44300 Nantes
Mahmoud Sitohy
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, F-44300 Nantes Zagazig University, Biochemistry Department, Faculty of Agriculture, Zagazig, Egypt
Thomas Haertlé
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, F-44300 Nantes
Jean-Marc Chobert*
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, F-44300 Nantes
*
*For correspondence; e-mail: chobert@nantes.inra.fr
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Abstract

Proteinase activity of Lactobacillus fermentum IFO3956 cells was higher when they were grown on milk-based media than on 10% reconstituted skim milk. The lowest protease activity was observed when cells were grown on milk-free media. The extraction of milk-induced cell-bound proteases from Lb. fermentum IFO3956 was most efficient using 1% Tween 80 while the use of 1% SDS inhibited all proteolytic activity. Two bands of ∼35 and >100 kDa were observed by zymogram, indicating that proteolytic activity corresponded to the presence of at least two types of enzymes or two molecular forms of one enzyme. Mass spectrometry analyses of αS1-casein hydrolysates detected 24 peptides with sizes ranging from 5 to 36 amino acids, including 9 phosphorylated peptides, resulting from the fermentation of Lb. fermentum IFO3956 of αS1-casein. Most of the identified peptides originated from the N-terminal portion of αS1-casein. The studied bacterial strain could hydrolyze αS1-casein in many sites including the epitopes triggering the allergic reactions against αS1-casein e.g. at the positions 23, 30, 41, 71, 91, 98, 126, 179. After hydrolysis of αS1-casein with Lb. fermentum IFO3956 the recognition and the binding of this casein to IgE from the pooled sera of 18 patients with cow's milk allergy was significantly reduced.

Keywords

Egyptian dairy productsLactobacillus fermentumproteolytic activityallergy
Type
Research Article
Information
Journal of Dairy Research , Volume 78 , Issue 2 , May 2011 , pp. 203 - 210
Copyright
Copyright © Proprietors of Journal of Dairy Research 2011

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