Lactic Acid Bacteria for Coeliac Disease

a technology of lactobacillus and coeliac disease, which is applied in the field of lactobacilli or streptococci, can solve the problems of affecting the absorption of nutrients and causing achycardia

Inactive Publication Date: 2013-05-16
DANONE
View PDF3 Cites 9 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0009]Surprisingly it was found that the 33-mer peptide was slowly degraded under conditions mimicking the human digestive tract and that a 18-mer peptide breakdown product PQLPYPQPQLPYPQPQPF (SEQ ID NO: 4) emerged which was com

Problems solved by technology

The inflammation subsequently leads to villous atrophy and interferes with

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Examples

Experimental program
Comparison scheme
Effect test

example 1

Screening of Supernatants of Lactic Acid Bacteria for the Ability to Degrade the 33 -Mer of SEQ ID No: 1

[0058]34 Lactobacillus, 10 Streptococcus and 3 Bifidobacterium strains were selected and their capacity to produce a proteolytic activity with capacity to degrade the 33-mer peptide LQLQPFPQPQLPYPQPQLPYPQPQLPYPQPQPF (SEQ ID NO: 1) from α2-gliadin (which is assumed to be responsible of celiac disease) was evaluated.

[0059]All of the included micro-organisms were grown both in a general and specific medium.

[0060]For Lactobacillus strains, the general medium MRS (20 g / l dextrose, 10 g / l peptone, 8 g / l meat extract, 5 g / l sodium acetate, 2 g / l dipotassium phosphate, 2 g / l ammonium citrate, 1 ml Tween 80, 0.2 g / l magnesium sulphate, 0.05 g / l manganese sulphate) was used and the specific medium YGBLP (10 g / l peptone, 8 g / l meat extract, 3 g / l yeast extract, 2.5 g / l monopotassium sulphate, 2.5 g / l dipotassium phosphate, 0.2 g / l magnesium sulphate, 0.05 g / l manganese sulphate, 5 g / l glucos...

example 2

Screening of Selected Cells and Supernatants of Lactic Acid for Resistance Against the Gastro-Intestinal Tract

[0067]The strains most efficient in 33-mer degradation, strain P02503 A1, P02503 A3, P02431 C1, P02445 H7, P02638 H7, P 02646 A9 were selected and also a mixture of P 02638 F9 / P02523 A4, was selected as a typical yogurt symbiosis. They were identified on the basis of both PCR typing and biochemical activity on API 50 CHL kit (Biomerieux, France).

[0068]P02503 A1 is strain DN—114001, Lactobacillus casei, deposited at CNCM under number I-1518 on January 23th 1995.

[0069]P02431 C1 is strain DN—1190118, Lactobacillus helveticus deposited at CNCM under number I-4279 on February 25th, 2010.

[0070]P02445 H7 is strain DN—1110272, Lactobacillus delbrueckii subsp lactis deposited at CNCM under number I-4280 on February 25th, 2010.

[0071]P02638 F9 is strain DN—001343, Streptococcus thermophilus, deposited at CNCM under number I-2776 at January 24th 2002.

[0072]P02523 A4 is strain Lactobacil...

example 3

Screening of Supernatants of Selected Strains for the Ability to Degrade the 20-Mer of SEQ ID No: 2 and 13-Mer of SEQ ID No: 3

[0077]Subsequently a screening was performed to determine the ability to degrade other peptides involved with coeliac disease, namely the 20-mer and the 13-mer.

[0078]In the same way as in Example 1, the capacity of different supernatants (P02503 A1, P02431 C1, P02445 H7 and the mixture P02523 A4 -P02638 F9 to degrade other peptides involved in celiac disease as 20-mer from α-gliadin (QQLPQPQQPQQSPFQQQRPF) and 13-mer from A-gliadin (LGQQQPFPPQQPY) were assayed. A high degradation of both samples with the selected strains was detected (Table 3). These data underline the important role of the proteolytic activity of the culture supernatants of the selected strains not only the principal peptide related with celiac disease but also other peptides involves in this disorder.

TABLE 3Percentage of 13-mer and 20-mer peptide degradationby the selected strainsStrain13-m...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

PropertyMeasurementUnit
Fractionaaaaaaaaaa
Fractionaaaaaaaaaa
Acidityaaaaaaaaaa
Login to view more

Abstract

The present invention discloses strains of Lactobacillus and Streptococcus which have a capacity to degrade gliadin peptides involved in coeliac disease and which peptide degrading activity is stable under low pH and in the presence of mammalian digestive enzymes. These strains are suitable in a product for use in prevention and/or treatment of celiac disease.

Description

FIELD[0001]The invention relates to lactobacilli or streptococci in the treatment or prevention of coeliac disease.BACKGROUND ART[0002]Coeliac disease is an autoimmune disorder of the small intestine that occurs in genetically predisposed people of all ages from infancy on up. Coeliac disease is caused by a reaction to gliadins, a family of related proline and glutamine rich protein in gluten protein, which are found in wheat (and similar proteins of the tribe Triticeae, such as barley and rye). Upon exposure to gliadin, the enzyme tissue transglutaminase modifies the protein, and the immune system of subjects prone to celiac disease reacts and cross-reacts with the small-bowel tissue, causing an inflammatory reaction. The inflammation subsequently leads to villous atrophy and interferes with the absorption of nutrients, including minerals and fat soluble vitamins. Classic symptoms of coeliac disease include abdominal distension, vomiting, diarrhoea, weight loss (or stunted growth i...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
IPC IPC(8): A61K35/74A61K35/744
CPCA61K35/744C12N1/20A61K35/74C12R1/245C12R1/46C12R1/225A61P1/12C12R2001/245C12N1/205C12R2001/225C12R2001/46A61K35/747C12N1/18C12Q1/02
Inventor MONTSERRAT CARRERAS, AGUSTIANDREU COROMINAS, MONTSERRATRAMON VIDAL, DANIELGENOVES MARTINEZ, SALVADORBATALLER LEIVA, ESTHER
Owner DANONE
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products