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Proteolysis by Lactobacillus fermentum IFO3956 isolated from Egyptian milk products decreases immuno-reactivity of αS1-casein.
MedLine Citation:
PMID:  21385515     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
Shady El-Ghaish; Hanitra Rabesona; Yvan Choiset; Mahmoud Sitohy; Thomas Haertlé; Jean-Marc Chobert
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-3-9
Journal Detail:
Title:  The Journal of dairy research     Volume:  -     ISSN:  1469-7629     ISO Abbreviation:  -     Publication Date:  2011 Mar 
Date Detail:
Created Date:  2011-3-9     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985125R     Medline TA:  J Dairy Res     Country:  -    
Other Details:
Languages:  ENG     Pagination:  1-8     Citation Subset:  -    
Affiliation:
UR 1268 Biopolymères Interactions Assemblages, INRA, F-44300 Nantes.
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