MODIFICATION OF IgE BINDING TO β- AND αS1-CASEINS BY PROTEOLYTIC ACTIVITY OF LACTOBACILLUS HELVETICUS A75
AYNUR AHMADOVA
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
Department of Biotechnology and Biochemistry, Baku State University, 370602 Baku, Azerbaijan
Search for more papers by this authorSHADY EL-GHAISH
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
Search for more papers by this authorYVAN CHOISET
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
Search for more papers by this authorHANITRA RABESONA
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
Search for more papers by this authorMARTINE DROUET
CHU d'Angers, Unité Allergologie Générale et Pneumologie, Angers Cedex 9, France
Search for more papers by this authorJEAN-MARC CHOBERT
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
Search for more papers by this authorAKIF A. KULIEV
Department of Biotechnology and Biochemistry, Baku State University, 370602 Baku, Azerbaijan
Search for more papers by this authorCorresponding Author
THOMAS HAERTLE
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
TEL: +332-40-67-50-91; FAX: +332-40-67-50-84; EMAIL: [email protected]Search for more papers by this authorAYNUR AHMADOVA
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
Department of Biotechnology and Biochemistry, Baku State University, 370602 Baku, Azerbaijan
Search for more papers by this authorSHADY EL-GHAISH
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
Search for more papers by this authorYVAN CHOISET
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
Search for more papers by this authorHANITRA RABESONA
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
Search for more papers by this authorMARTINE DROUET
CHU d'Angers, Unité Allergologie Générale et Pneumologie, Angers Cedex 9, France
Search for more papers by this authorJEAN-MARC CHOBERT
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
Search for more papers by this authorAKIF A. KULIEV
Department of Biotechnology and Biochemistry, Baku State University, 370602 Baku, Azerbaijan
Search for more papers by this authorCorresponding Author
THOMAS HAERTLE
UR 1268, INRA Biopolymères Interactions Assemblages – Equipe FIP, B.P. 71627, 44316 Nantes Cedex 03, France
TEL: +332-40-67-50-91; FAX: +332-40-67-50-84; EMAIL: [email protected]Search for more papers by this authorAbstract
ABSTRACT
Proteolytic activity of Lactobacillus helveticus A75 and effects of caseins hydrolysis by this strain on their immuno-reactivity were studied. Proteases of L. helveticus A75 hydrolyzed both αS1- and β-caseins and were inhibited by serine- and metallo-proteases inhibitors. Polymerase chain reaction amplification revealed the presence of prtH gene, which was 99% identical to prtH gene of L. helveticus CNRZ 32. Effect of proteolysis of αS1- and β-caseins by L. helveticus A75 on their immunoglobulin E (IgE) binding ability was studied by an enzyme-linked immunosorbent assay with the pool of eight sera from cow milk allergy patients. The IgE binding ability of hydrolyzed proteins was lower than that of intact proteins, which indicates that hydrolysis of αS1- and β-caseins by proteases of L. helveticus A75 decreases their recognition by specific IgE. Half maximal inhibitory concentration values were 2.01 and 2.28 µg/mL for αS1- and β-casein, respectively, and increased until 9.08 and 13.65 µg/mL, respectively, after their hydrolysis by L. helveticus A75.
PRACTICAL APPLICATIONS
The obtained results yield new information about proteolytic activity and potential application of lactobacilli isolated from traditional Azerbaijani cheeses. Isolated strain could represent new adjunct cultures for the dairy industry.
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