# US 11,028,147 B2 · Hydrolyzed collagen compositions and methods of making thereof

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- Number: US 11,028,147 B2
- Document ID: US11028147B2
- Status: Granted
- Kind: B2
- Application number: 16/356,030
- Filed: 2019-03-18
- Published: 2019-07-11
- Granted: 2021-06-08
- Earliest claimed: 2016-03-22
- Assignees: Avicenna Nutraceutical, LLC
- Applicants: Avicenna Nutraceutical, LLC
- Inventors: Ali Elnajjar; Ali Mourad; Mark Ernst Brandt; Christopher Lippelt
- Web page: https://patentgrep.com/patent/US11028147B2

## CPC

- C07K 14/78: Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
- A23J 1/00: Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23L 5/00: Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
- A23L 29/284: {Gelatin; Collagen}
- A23L 33/18: Peptides; Protein hydrolysates
- C08H 1/06: derived from horn, hoofs, hair, skin or leather
- C08L 89/06: derived from leather or skin {, e.g. gelatin}
- C07K: PEPTIDES (peptides in foodstuffs A23; obtaining protein compositions for foodstuffs, working-up proteins for foodstuffs A23J; preparations for medicinal purposes A61K; peptides containing beta-lactam rings C07D; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, C07D; ergot alkaloids of the cyclic peptide type C07D519/02; macromolecular compounds having statistically distributed amino acid units in their molecules, i.e. when the preparation does not provide for a specific; but for a random sequence of the amino acid units, homopolyamides and block copolyamides derived from amino acids C08G69/00; macromolecular products derived from proteins C08H1/00; preparation of glue or gelatine C09H; single cell proteins, enzymes C12N; genetic engineering processes for obtaining peptides C12N15/00; compositions for measuring or testing processes involving enzymes C12Q; investigation or analysis of biological material G01N33/00)
- A23J: PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23L: FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF (preservation thereof A23B)
- C08H: DERIVATIVES OF NATURAL MACROMOLECULAR COMPOUNDS (polysaccharides C08B; natural rubber C08C; natural resins or their derivatives C09F; bituminous materials C10)
- C08L: COMPOSITIONS OF MACROMOLECULAR COMPOUNDS (compositions based on polymerisable monomers C08F, C08G; artificial filaments or fibres D01F; textile treating compositions D06)

## Abstract

Disclosed herein are hydrolyzed collagen compositions. The compositions are inexpensive to make and can be produced without the use of proteolytic enzymes, decolorizing agents, antibacterial and antifungal agents, and the like. Further, the compositions are substantially free of odors and are white to light yellow in color and are suitable to be used as dietary supplements. Also disclosed are methods for producing the compositions.

## Claims

### Claim 1

A method for producing hydrolyzed collagen, the method comprising
(a) heating avian cartilage in the presence of an aqueous acid to at a temperature of from 50° C. to 100° C. for 8 to 48 hours to produce a first composition, wherein the avian cartilage comprises the ribcage and sternum;
(b) optionally filtering the first composition to remove the supernatant;
(c) neutralizing the acid present in the supernatant to produce a neutralized supernatant; and
(d) removing the water in the neutralized supernatant to produce the hydrolyzed collagen,
wherein the process does not use an enzyme.

### Claim 2 (depends on 1)

The method of claim 1, wherein the avian cartilage comprises chicken cartilage.

### Claim 3 (depends on 1)

The method of claim 1, wherein the avian cartilage comprises chicken sternum.

### Claim 4 (depends on 3)

The method of claim 3, wherein chicken sternum is removed from the chicken skeleton prior to step (a).

### Claim 5 (depends on 1)

The method of claim 1, wherein avian cartilage is treated with an anti-bacterial agent prior to step (a).

### Claim 6 (depends on 1)

The method of claim 1, wherein the acid comprises hydrochloric acid.

### Claim 7 (depends on 1)

The method of claim 1, wherein the ratio of chicken sternum per mole of acid is from 500 g chicken sternum/mole of acid to 5,000 g chicken sternum/mole of acid.

### Claim 8 (depends on 1)

The method of claim 1, wherein the ratio of avian cartilage per mole of acid is from 500 g avian cartilage/mole of acid to 1,000 g avian cartilage/mole of acid.

### Claim 9 (depends on 1)

The method of claim 1, wherein the supernatant is neutralized with an alkali metal base or an alkaline earth metal base.

### Claim 10 (depends on 1)

The method of claim 1, wherein the supernatant is neutralized with sodium hydroxide or sodium carbonate.

### Claim 11 (depends on 1)

The method of claim 1, wherein the supernatant is neutralized with calcium hydroxide or calcium carbonate.

### Claim 12 (depends on 1)

The method of claim 1, wherein the water in step (d) is removed by lyophilization or spray drying.

### Claim 13 (depends on 1)

The method of claim 1, wherein the avian cartilage is heated in the presence of aqueous hydrochloric acid at a temperature of from 58° C. to 62° C. for 16 to 18 hours, wherein the ratio of avian cartilage per mole of acid is from 500 g avian cartilage/mole of acid to 1,000 g avian cartilage/mole of acid.

### Claim 14 (depends on 13)

The method of claim 13, wherein the supernatant is neutralized with calcium hydroxide or calcium carbonate.

### Claim 15 (depends on 1)

The method of claim 1, wherein the avian cartilage is heated in the presence of an aqueous acid at a temperature of from 55° C. to 100° C. for 8 to 48 hours, wherein the ratio of avian cartilage per mole of acid is from 250 g avian cartilage/mole of acid to 5,000 g avian cartilage/mole of acid to produce a first composition.