US2010069512A1PendingUtilityA1

Process for preparing an oil-in-water emulsion stabilised with recombinant collagen-like material and products prepared

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Assignee: FUJI FILM MFG EUROP B VPriority: Jun 24, 1999Filed: May 21, 2007Published: Mar 18, 2010
Est. expiryJun 24, 2019(expired)· nominal 20-yr term from priority
G03C 1/005
65
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Claims

Abstract

The invention provides oil-in-water emulsions comprising recombinant collagen-like polymer in an amount sufficient to act as stabiliser of the emulsion. The polymer is especially a polypeptide which is free of helix structure, has an isoelectric point at least 0.5 pH units removed from the pH of the oil-in-water emulsion. Furthermore, bipolar recombinant collagen-like polymers are provided for use in oil-in-water emulsions. The bipolar polymers are polar at one end as a result of a relative abundance of polar amino acids, and apolar at the other end as a result of a relative abundance of apolar amino acids.

Claims

exact text as granted — not AI-modified
1 - 22 . (canceled) 
     
     
         23 . A process for preparing an oil-in-water-emulsion comprising mixing a hydrophilic phase and a hydrophobic phase, wherein the hydrophilic phase comprises a collagen-like recombinant peptide in an amount sufficient to stabilize the emulsion, the collagen-like recombinant peptide comprising at least one GXY domain having a length of at least 5 consecutive GXY triplets, wherein each X and each Y represents an amino acid residue, and wherein at least 20 percent of the amino acid residues of the recombinant collagen-like peptide are constituents of consecutive GXY triplets, and the hydrophobic phase comprises an additive selected from the group consisting of a pharmaceutical agent, a nutritional agent and a photographic agent. 
     
     
         24 . Process according to  claim 23 , wherein the recombinant collagen-like peptide is free of helix structure. 
     
     
         25 . Process according to  claim 23 , wherein the recombinant collagen-like polymer is free of hydroxyproline residues. 
     
     
         26 . Process according to  claim 23 , wherein the recombinant collagen-like peptide has an isoelectric point at least 0.5 pH units removed from the pH of the oil-in-water emulsion. 
     
     
         27 . Process according to  claim 23 , wherein the recombinant collagen-like peptide has an isoelectric point of 4 or 10 or in the range between 4 and 10. 
     
     
         28 . Process according to  claim 23 , wherein the recombinant collagen-like peptide has a molecular weight in the range of from 2.5 kDa to 100 kDa. 
     
     
         29 . Process according to  claim 23 , wherein the recombinant collagen-like peptide is homodisperse with regard to the molecular weight of the peptide. 
     
     
         30 . Process according to  claim 23 , wherein the hydrophilic phase further comprises non-recombinant collagen. 
     
     
         31 . Process according to  claim 23 , wherein the recombinant collagen-like peptide exhibits an amphiphilic structure and comprises at least one polar part containing at least 10 polar amino acid residues and at least one apolar part containing at least 10 apolar amino acid residues. 
     
     
         32 . Process according to  claim 31 , wherein the lengths of the at least one polar part and of the at least one apolar part are each at least 10 percent of the length of the peptide backbone. 
     
     
         33 . Process according to  claim 31 , wherein the average transfer free energy per amino acid residue of the at least one polar part is at least 0.3 kcal/mole lower than the average transfer free energy per amino acid of the at least one apolar part. 
     
     
         34 . Process according to  claim 23 , wherein the oil-in-water emulsion exhibits an initial droplet size of less than 500 nm at a temperature of 40° C. or lower and at a pH of 5. 
     
     
         35 . Process according to  claim 33 , wherein the oil-in-water emulsion exhibits an increase in droplet size of less than 400 nm after 4 hours at a temperature of 40° C. or lower and at a pH of 5. 
     
     
         36 . Process according to  claim 23 , wherein the recombinant collagen-like peptide is present in a solvent in a concentration in the range from about 2 g/l to about 100 g/l of solvent. 
     
     
         37 . Process according to  claim 23 , wherein the recombinant collagen-like peptide exhibits a viscosity in the range of from 0.005 mP to 8 mP when dissolved at a concentration of 6.6 percent in water at a temperature of 40° C. 
     
     
         38 . Process according to  claim 23 , wherein the recombinant collagen-like peptide does not exhibit gelation at a temperature below 30° C. 
     
     
         39 . Process according to  claim 23 , wherein the hydrophobic phase additive is selected from the group consisting of trihexyl-, trioctyl-, tridecyl-, tris(butoxyethyl)-, tris(haloalkyl)-, trixylenyl- and tricresyl-phosphates. 
     
     
         40 . Process according to  claim 23 , wherein the hydrophobic phase additive comprises edible triglycerides derived from vegetable or animal fats. 
     
     
         41 . Process according to  claim 23 , wherein the hydrophobic phase additive comprises sodium dodecylbenzenesulphonate.

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