US2005256057A1PendingUtilityA1

Protein hydrolysate rich in tripeptides

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Assignee: EDENS LUPPOPriority: Jun 4, 2002Filed: Jun 3, 2003Published: Nov 17, 2005
Est. expiryJun 4, 2022(expired)· nominal 20-yr term from priority
C12N 9/48
54
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Claims

Abstract

The present invention describes a protein hydrolysate which is rich in tripeptides whereby the tripeptides are rich in proline at one end of the peptide.

Claims

exact text as granted — not AI-modified
1 . A protein hydrolysate which is rich in tripeptides whereby the tripeptides are rich in proline at one end thereof.  
     
     
         2 . The protein hydrolysate of  claim 1  wherein at least 20 molar % of peptides having a molecular weight of 200 to 2000 Da is present in the hydrolysate as tripeptides.  
     
     
         3 . The protein hydrolysate of  claim 1  wherein at least 20% of the proline present in a starting protein that forms the protein hydrolysate is present in the tripeptides.  
     
     
         4 . The protein hydrolysate of  claim 1  wherein at least 30% of the tripeptides have a carboxy terminal proline.  
     
     
         5 . The protein hydrolysate according to an) one of  claim 1  wherein at least 70 molar % of peptides present in the hydrolysate contain 2 to 7 amino acid residues (dipeptide to heptapeptide).  
     
     
         6 . A method of producing a protein hydrolysate comprising 
 contacting a protein substrate with:    a) endoprotease; and    b) tripeptidase (TPAP).    
     
     
         7 . The method of  claim 6  wherein the endoprotease is a proline specific endoprotease (PSE), a serine protease, an aspartic protease or a metalloendoprotease.  
     
     
         8 . The method of  claim 6  wherein the protein substrate is first contacted with serine protease, aspartic protease or metalloendoprotease and subsequently the TPAP and optionally PSE is added.  
     
     
         9 . A method of using the protein hydrolysate of  claim 1  comprising 
 consuming the hydrolysate wherein a mammal performs the consuming step.    
     
     
         10 . An enzyme composition comprising 
 (a) an endoprotease and    (b) a tripeptidase (TPAP).    
     
     
         11 . The enzyme composition of  claim 10  wherein the endoprotease is a serine protease, an aspartic protease, a metalloendoprotease or a proline specific endoprotease (PSE).  
     
     
         12 . The enzyme composition of  claim 10  whereby this composition when added to a suitable protein is able to produce a protein hydrolysate of which is rich in tripeptides whereby the tripeptides are rich in proline at one end thereof.  
     
     
         13 . A food or feed product comprising a hydrolysate of  claim 1 .  
     
     
         14 . A method of reducing the intolerance to proline rich food stuffs comprising incubating a protein substrate found in proline rich food stuffs with the enzyme composition of  claim 10  wherein the intolerance of the incubated protein substrate is reduced in comparison to the protein substrate that has not been incubated.  
     
     
         15 . A method of producing food or feed comprising 
 incubating a protein substrate with the enzyme composition of  claim 10;  and    producing food or feed from the incubated protein substrate.    
     
     
         16 . The protein hydrolysate of  claim 2  wherein at least 25 molar % of the peptides having a molecular weight of 200 to 2000 Da is present in the hydrolysate as tripeptides.  
     
     
         17 . The protein hydrolysate of  claim 16  wherein at least 30 molar % of the peptides having a molecular weight of 200 to 2000 Da is present in the hydrolysate as tripeptides.  
     
     
         18 . The protein hydrolysate of  claim 3  wherein at least 30% of the proline present in the starting protein is present in the tripeptides.  
     
     
         19 . The protein hydrolysate of  claim 18  wherein at least 40% of the proline present in the starting protein is present in the tripeptides.  
     
     
         20 . The protein hydrolysate of  claim 4  wherein at least 35% of the tripeptides have a carboxy terminal proline.  
     
     
         21 . The protein hydrolysate of  claim 5  wherein at least 75 molar % of the peptides contain 2 to 7 amino acid residues (dipeptide to heptapeptide).  
     
     
         22 . The method of  claim 7  wherein the endoprotease is PSE.  
     
     
         23 . The method of  claim 9  wherein the mammal is a human.  
     
     
         24 . The enzyme composition of  claim 11  wherein the endoprotease is PSE.

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