US2006147581A1PendingUtilityA1

Hybrid enzymes

Assignee: NOVOZYMES ASPriority: Dec 22, 2004Filed: Dec 22, 2005Published: Jul 6, 2006
Est. expiryDec 22, 2024(expired)· nominal 20-yr term from priority
A21D 8/042Y02E50/10
66
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Claims

Abstract

The present invention relates to a polypeptide and the use thereof.

Claims

exact text as granted — not AI-modified
1 . polypeptide which polypeptide is a hybrid comprising; 
 a) a first amino acid sequence having endo-amylase activity and    b) a second amino acid sequence comprising a carbohydrate-binding module.    
     
     
         2 . The polypeptide of  claim 1 , wherein said first amino acid sequence and/or said second amino is derived from a bacterium  
     
     
         3 . The polypeptide according to  claim 1 , wherein said second amino acid sequence has at least 60% identity to the amino acid sequence shown as amino acid residues 485 to 586 in SEQ ID NO:2.  
     
     
         4 . The polypeptide according to  claim 1 , wherein said first amino acid sequence has at least 60% identity to any amino acid sequence selected from the group consisting of SEQ ID NO:35, SEQ ID NO:36, SEQ ID NO:37, SEQ ID NO:38, SEQ ID NO:39, SEQ ID NO:40, SEQ ID NO:41 and SEQ ID NO:42.  
     
     
         5 . The polypeptide according to  claim 1 , having at least 60% identity to any amino acid sequence selected from the group consisting of SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14.  
     
     
         6 . The polypeptide according to  claim 1 , comprising a) the catalytic domain shown in SEQ ID NO:40 or a homologous catalytic domain, wherein one or more, or preferably all, of the following substitutions have been introduced: R118K, D183*, G184*, N195F, R320K, R458K, N33S, D36N, K37L, E391I, Q394R, K395D, T452Y and N484P, using the numbering of SEQ ID NO: 40 and b) the CBM shown as residue 485 to 585 of SEQ ID NO:2.  
     
     
         7 . The polypeptide according to  claim 1  comprising a) the catalytic domain shown in SEQ.ID: 37 or a homologous catalytic domain and comprising one or more, e.g. such as all of the following alterations: S31A, D32N, 133L, E178*, G179*, N190F, K3891, K392R, E393D, V508A and b) the CBM having the amino acid sequence shown as amino acid residues 485 to 586 in SEQ ID NO:2.  
     
     
         8 . The polypeptide according to  claim 1  comprising a) the catalytic domain shown in SEQ ID NO:40 or a homologous catalytic domain, wherein one or more, or preferably all, of the following substitutions have been introduced: R118K, D183*, G184*, N195F, R320K, R458K and N484P, using the numbering of SEQ ID NO: and b) the CBM shown as residue 485 to 585 of SEQ ID NO:2.  
     
     
         9 . The polypeptide according to  claim 1 , wherein said polypeptide has; 
 a) an EIF1 larger than 1.0 at the test conditions given in the specification, or    b) an EIF2 larger than 1.0 at the test conditions given in the specification.    
     
     
         10 . The polypeptide according to  claim 1 , wherein said polypeptide has at least 25% residual activity at 70° C. at the test conditions given in the specification.  
     
     
         11 . The polypeptide according to  claim 1 , wherein the addition of 2 times the effective dosage of said polypeptide to a dough results in an ELR of less than 15%.  
     
     
         12 . The polypeptide according to  claim 1 , wherein the addition of 2 times the effective dosage of said polypeptide to a dough results in an ELR N  of less than 15%.  
     
     
         13 . A process for preparing a dough or an edible product made from a dough, which process comprises adding the polypeptide according to  claim 1  to the dough.  
     
     
         14 . The process of  claim 13  wherein the edible product is a baked product.  
     
     
         15 . The process of  claim 13  wherein the addition of 2 times the effective dosage of said polypeptide results in an ELR of less than 15%.  
     
     
         16 . The process according to  claim 13  wherein the addition of 2 times the effective dosage of said polypeptide results in an ELR N  of less than 15%.  
     
     
         17 . The process according to  claim 13  wherein the polypeptide gives a cohesiveness reduction of less than 5% when dosed to give a dHardness of at least 85 units at the test conditions given in the specification.  
     
     
         18 . The process according to  claim 13  wherein the polypeptide when added together with 300 MANU Novamyl/kg flour gives a cohesiveness reduction of less than 5% when dosed to give a dHardness of at least 15 units at the test conditions given in the specification  
     
     
         19 . The process according to  claim 13  wherein the polypeptide gives a cohesiveness reduction of less than 5% when dosed to give a dMobility of at least 400 units at the test conditions given in the specification  
     
     
         20 . The process according to  claim 13  wherein the polypeptide when added together with 300 MANU Novamyl/kg flour gives a cohesiveness reduction of less than 5% when dosed to give a dMobility of at least 1100 units at the test conditions given in the specification  
     
     
         21 - 52 . (canceled)

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