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Use of proline specific endoproteases to hydrolyse peptides and proteins

a technology of proline and endoprotease, which is applied in the direction of peptide/protein ingredients, immunological disorders, metabolism disorders, etc., and can solve the problems of unsatisfactory effects in specific groups of individuals, the presence of such molecules in protein hydrolysates, and the use of proline specific endoproteases,

Inactive Publication Date: 2011-06-16
DSM IP ASSETS BV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

The present invention provides a process for the proteolytic hydrolysis of a peptide or polypeptide using a proline specific endo protease. This enzyme is able to hydrolyze peptides or polypeptides that have specific amino acid residues, such as proline or glutamine residues, at certain positions in the peptide or polypeptide. The process can be used to hydrolyze peptides or polypeptides with a tripeptide motif of Glu-Xxx-Pro or Gln-Xxx-Pro, wherein X is any amino acid residue. The hydrolysis can occur at pH 6 or lower, preferably 5.5 or lower, and more preferably 5.0 or lower. The percentage of hydrolysis can be at least 70%, preferably at least 80%, and most preferably at least 90%. The invention also provides a process for the proteolytic hydrolysis of peptides or polypeptides that contain at least 4 amino acid residues. The proline specific endo protease can be used to produce food or medicament that is free of certain epitopes associated with certain disorders, such as psychiatric disorders, celiac disease, and type 1 diabetes. The invention also provides a proline specific endo protease for use in manufacturing a dietary supplement or medicament for the treatment or prevention of these disorders.

Problems solved by technology

As a result proline rich peptides can build up and may lead to undesirable effects in specific groups of individuals.
As the BCM-7 peptide fragment and its related molecules have been linked with certain diseases, the presence of such molecules in protein hydrolysates, quite often used in the diet of vulnerable groups like infants, elderly and patients, is an undesirable situation.
Although in normal individuals the peptidases in the intestinal epithelial layer and in the blood can cope with the beta-casomorphins, this seems not to be always the case for patients suffering from schizophrenia, autism, ADHD or other mood disorders.
IBS usually begins around the age of 20 and causes a great deal of discomfort and distress.

Method used

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  • Use of proline specific endoproteases to hydrolyse peptides and proteins
  • Use of proline specific endoproteases to hydrolyse peptides and proteins
  • Use of proline specific endoproteases to hydrolyse peptides and proteins

Examples

Experimental program
Comparison scheme
Effect test

example 2

The Enzyme as Obtained from A. Niger Represents a New Class of Proline Specific Enzymes

[0098]From the entire coding sequence of the A. niger derived proline specific endoprotease as provided in WO 02 / 45524 a protein sequence of 526 amino acids can be determined. The novelty of the enzyme was confirmed by BLAST searches of databases such as SwissProt, PIR and trEMBL. To our surprise, no clear homology could be detected between the A. niger enzyme and the known prolyl oligopeptidases. Closer inspection of the amino acid sequence, however, revealed low but significant homology to Pro-X carboxypeptidases (EC3.4.16.2), dipeptidyl aminopeptidases I (EC3.4.14.2), and thymus specific serine protease. All of these enzymes have been assigned to family S28 of serine peptidases. Also the GxSYxG configuration around the active site serine is conserved between these enzymes and the A. niger derived endoprotease. Additionally, members of family S28 have an acidic pH optimum, have specificity for c...

example 3

The A. Niger Derived Proline Specific Endoprotease can Hydrolyse Large Proteins as Well as Small Peptides and is Thus a True Endoprotease

[0100]Owing to a specific structural feature, prolyl oligopeptidases belonging to the S9 family cannot digest peptides larger than 30 amino acids. This limitation is an obvious disadvantage for an enzyme, which is meant to hydrolyse as quickly and as efficiently as possible all potential proline rich toxic proline rich peptides. To see if the A. niger derived proline specific endoprotease exhibits the same limitations with respect to the size of the substrate molecule, we have incubated the chromatographically purified prolyl endopeptidase from A. niger with a small synthetic peptide and with the large ovalbumine molecule and have analysed the hydrolysis products formed by SDS-PAGE. The synthetic peptide used was a 27-mer of the sequence NH2-FRASDNDRVIDPGKVETLTIRRLHIPR-COOH and was a gift of the Pepscan company (Lelystad, The Netherlands). As shown...

example 4

Beta-Casomorphins in Hydrolysates Formed After Incubation with Alcalase and a Combination of Alcalase Plus Proline Specific Endoprotease from A. Niger

[0108]In analogy with the formation of protease-resistant beta-casomorphins during gastro-intestinal proteolysis, we wondered whether during the industrial production of milk protein hydrolysates a similar accumulation of BCM-7 related peptide fragments would occur. To that end we incubated A2 beta-casein isolated from bovine milk with the industrially frequently used subtilisin Alcalase and with Alcalase plus the proline specific endoprotease from A. niger. Using LC / MS / MS analysis the peptides thus formed were analysed.

[0109]Bovine milk contains almost 10 grams of beta-caseine per kg of milk representing 28% of all protein present. To facilitate the analysis of BCM-7 related amino acid. sequences, in this experiment we used a concentrated preparation (from Sigma) containing a minimum of 90% (A2) beta-casein. The latter product was di...

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Abstract

The present invention relates to a process for the proteolytic hydrolysis of a peptide or a polypeptide, said peptide or polypeptide comprising 4 to 40, preferably 5 to 35, amino acid residues and said peptide or polypeptide is not hydrolysable by subtilisin whereby said peptide or polypeptide is hydrolysed by a proline specific endo protease at a pH of 6.5 or lower, preferably 5.5 or lower and more preferably 5.0 or lower to hydrolyse said peptide or polypeptide.

Description

FIELD OF THE INVENTION[0001]The present invention relates to the proteolytic :hydrolysis of, a peptide or polypeptide.BACKGROUND OF THE INVENTION[0002]Proline rich dietary proteins such as caseins in bovine milk or glutens in cereals are known to resist proteolytic degradation in the human gastrointestinal tract. As a result proline rich peptides can build up and may lead to undesirable effects in specific groups of individuals. Some of these effects have been ascribed to the fact that the proline rich peptides act as opioids that bind to receptors in peripheral tissues and the central nervous system. For example, syndromes shown by autistic and schizophrenic patients have been linked with the consumption of proline rich dietary proteins. Other effects are the result of an intolerance for proline rich peptides. For example specific proline rich sequences are responsible for the observed toxicity of gluten in celiac disease. Celiac disease is a widely prevalent autoimmune disease of ...

Claims

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Application Information

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Patent Type & Authority Applications(United States)
IPC IPC(8): A23L1/305C12C11/00A21D8/04A21D13/00A23J3/34A61K38/48
CPCA23J3/346C12P21/06A61K38/482A61P1/12A61P1/14A61P1/16A61P19/04A61P25/18A61P25/24A61P3/02A61P3/10A61P37/06A61P5/14A61P9/00
Inventor EDENS, LUPPOHOEVEN, ROBERTUS ANTONIUS MIJNDERT VAN DERDE ROOS, ANDRE LEONARDUSHARVEY, MELISSA
Owner DSM IP ASSETS BV
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