GB2274458A - Production of soluble collagen by hydrolysis and spray-drying - Google Patents
Production of soluble collagen by hydrolysis and spray-drying Download PDFInfo
- Publication number
- GB2274458A GB2274458A GB9301086A GB9301086A GB2274458A GB 2274458 A GB2274458 A GB 2274458A GB 9301086 A GB9301086 A GB 9301086A GB 9301086 A GB9301086 A GB 9301086A GB 2274458 A GB2274458 A GB 2274458A
- Authority
- GB
- United Kingdom
- Prior art keywords
- collagen
- spray
- solution
- dried
- drying
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 102000008186 Collagen Human genes 0.000 title claims abstract description 58
- 108010035532 Collagen Proteins 0.000 title claims abstract description 58
- 229920001436 collagen Polymers 0.000 title claims abstract description 58
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 9
- 238000001694 spray drying Methods 0.000 title claims abstract description 4
- 230000007062 hydrolysis Effects 0.000 title description 2
- 238000006460 hydrolysis reaction Methods 0.000 title description 2
- 238000000034 method Methods 0.000 claims abstract description 13
- 239000000463 material Substances 0.000 claims abstract description 7
- 230000003301 hydrolyzing effect Effects 0.000 claims abstract description 3
- 241000206672 Gelidium Species 0.000 claims description 7
- 108010059642 isinglass Proteins 0.000 claims description 7
- 229910052627 muscovite Inorganic materials 0.000 claims description 7
- 238000005352 clarification Methods 0.000 abstract description 4
- 239000000243 solution Substances 0.000 description 19
- 235000013405 beer Nutrition 0.000 description 7
- 239000000843 powder Substances 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 238000004925 denaturation Methods 0.000 description 3
- 230000036425 denaturation Effects 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 239000007921 spray Substances 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 241000252335 Acipenser Species 0.000 description 2
- 241000251468 Actinopterygii Species 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- HRZFUMHJMZEROT-UHFFFAOYSA-L sodium disulfite Chemical compound [Na+].[Na+].[O-]S(=O)S([O-])(=O)=O HRZFUMHJMZEROT-UHFFFAOYSA-L 0.000 description 2
- 235000010262 sodium metabisulphite Nutrition 0.000 description 2
- 239000004296 sodium metabisulphite Substances 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 210000004712 air sac Anatomy 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 102000034240 fibrous proteins Human genes 0.000 description 1
- 108091005899 fibrous proteins Proteins 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000006260 foam Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 235000011007 phosphoric acid Nutrition 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08H—DERIVATIVES OF NATURAL MACROMOLECULAR COMPOUNDS
- C08H1/00—Macromolecular products derived from proteins
- C08H1/06—Macromolecular products derived from proteins derived from horn, hoofs, hair, skin or leather
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Engineering & Computer Science (AREA)
- Materials Engineering (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Polymers & Plastics (AREA)
- Peptides Or Proteins (AREA)
Abstract
A process for the manufacture of solubilised collagen, comprising hydrolysing collagenous tissue material to produce a collagen solution and spray-drying the collagen solution at a temperature below 150 DEG C. The spray-dried collagen may be rehydrated and used as finings for the clarification of fermented liquors.
Description
PROCESS FOR THE MANUFACTURE OF COLLAGEN
The present invention relates to a process for the manufacture of collagen, more specifically to a process for the manufacture of solubilised collagen. The collagen is suitable for use in the clarification of liquids, in particular fermentation products such as beer.
Collagen is a fibrous protein which comprises most of the white fibre in the connective tissues of animals; particularly in the skin and muscles. The collagen molecule is in the form of a triple helix, each strand of the helix being a polypeptide chain. Collagen has a molecular weight of approximately 300,000, each strand of the triple helix having a molecular weight of approximately 100,000. Collagen has an unusual amino acid composition in that it contains an unusually high proportion of glycine, (approx. 30%). Also, proline is present to a much greater extent than in most other proteins. In so-called 'soluble' collagen, the intermolecular bonds have been cleaved, but leaving the triple helices intact. As the collagen becomes increasingly cross-linked it also becomes less hygroscopic.
Special forms of collagen have been developed for use in medical membranes, e.g. for use in dialysis. Regenerated collagen is used in the manufacture of edible food casingsand is manufactured by neutralising with acid collagen that has been purified by alkaline treatment.
Collagen is also useful in the clarification of liquids, in particular fermented liquids such as beer and wine.
This process, known as fining, brings suspended matter to the bottom of the treatment vessel. Collagen finings may be added to the liquor as an aqueous solution containing from about 0.25 to 1.5 weight percent collagen to produce a concentration of from 10 to 150 parts per million in the liquor, most preferably 30-50 ppm. In beer, yeasts and other proteins are removed from suspension to produce a clarified product. It has also been found that fining can improve foam stability and long term haze stability. The treatment is particularly important in the manufacture of traditional draught beer and is also widely used in bulk beer production to remove suspended solids prior to filtration to reduce storage time and improve filter efficiency.
The most preferred form of collagen for use in finings is isinglass collagen. This is a semi-transparent substance originally prepared from the air-bladders of sturgeons from the rivers of Western Russia but which is now largely made from those of sturgeons of other areas and of various other fishes. The isinglass is extracted from the fish and then partially hydrolysed by a dilute acid solution.
Other forms of collagenous tissue material may be used to extract pure collagen. Animal skin is rich in collagen in which the triple helices are highly cross-linked and which must be treated with alkaline agents to cleave the crosslinks to render it soluble in acids.
Solubilised collagen has few cross-links between the helical members. It is generally produced at a very lot strength in water (about 1-1.5 weight percent). This increases the bulk of matter which must be transported with resulting increased costs and storage problems. It is known to further concentrate the soluble collagen by the addition of certain salts to separate collagen fibres from aqueous solution. However, at higher concentrations the collagen solutions become highly viscous. This is a disadvantage when using the system in fining.
GB 2 147 299 (Isinglass Manufacturers Limited) describes that concentrated collagen in solubilised form is particularly susceptible to denaturing at temperatures of about 250C and above. This creates problems in unregulated storage and transport, particularly in shipping collagen to tropical countries. Accordingly, this document describes the discovery that collagen can be prepared in a dried form whereby collagenous tissue material is hydrolysed under acid or alkaline conditions to produce collagen having a moisture content of from 40-99 weight percent. The collagen is then freeze-dried and comminuted.
In contrast, it has now been found that a collagen solution may be spray-dried at temperatures up to about 12 OOC to produce a dry powder with very little denaturation. The resulting dried form of collagen is much less susceptible to denaturation than solubilised collagen, particularly at temperatures of 250C and above.
This enables easier transportation and it creates less problems in long-distance transport.
According to the present invention there is provided a process for the manufacturer of solubilised collagen which comprises hydrolysing collagenous tissue material and spray-drying the resulting collagen solution at temperatures below 1500C, preferably below 1200C.
Hydrolysis may occur either at a pH of from 1.4 to 5.0 or from 8.0 to 13.0.
The dried powder which results has low or minimal denaturation and no or minimal deleterious effect on performance.
Isinglass is preferred as the basic collagen material.
The resulting spray-dried collagen may be rehydrated for use in clarification processes.
The spray-dried collagen is found to give a good result when used in fining.
The present invention further relates to spray-dried collagen produced in accordance with the present invention.
The invention will now be further described with reference to the following non-limiting examples.
Example 1 75 kg of granulated isinglass purchased in bulk was made into a collagen finings solution:
To a vessel containing the isinglass was added:
19 L orthophosphoric acid
1.5 kg sodium metabisulphite (preservative)
3000 L water.
The solution was stirred slowly at ambient temperature (10-180C) for 24 hours.
The solution volume was increased to 6500 L by the addition of further water, and a further 5.0 kg sodium metabisulphite added. Stirring continued for a further 24 hours. The solution, containing 1% collagen by weight was stored at ambient temperature for a further 24 hours, then filtered to remove insolubles.
The filtered solution was spray-dried using a direct gasfired spray drier with a 2.5m chamber and a cyclone dis harge. Air inlet temperature was 1200C. Air outlet temperature was 68-700C.
The resulting product is an off-white, free flowing powder. Moisture content is below 15 weight percent.
5.0 grams of the powder was added to 1 litre of water at 150C and stirred. Dissolution occurred in under 30 minutes.
The solution was analysed. A comparison was made with a standard 'Ready For Use' (RFU) collagen solution known in the art. This is a 1% collagen solution diluted to 0.35% with water.
Spray-Dried Powder RFU
Solution pH 2.95 2.6-2.9
Total Nitrogen 536 ppm 530-560 ppm
Total Soluble Nitrogen 495 ppm > 504 ppm
Soluble Collagen 385 ppm ? 398 ppm
Example 2
The performance of the spray-dried powder solution was compared to 'RFU' collagen finings solution.- The beer was chilled to -10C, collagen solution added and the temperature held at -1 C. Haze was measured in EBC formazin haze units using a Radiometer haze meter. (EBC stands for European Brewery Convention).
Beer Collagen Addition Haze after solution rate (milL) 1 day 4 day 6 day Lager A RFU 1.7 4.2 2.0 2.1 Solution 1.7 4.7 2.0 2.1 of spray dried Lager B RFU 3.5 2.8 1.5 1.8 Solution 3.5 3.6 1.8 1.9 of spray dried
Claims (6)
- CLAIMS 1. A process for the manufacture of solubilised collagen, comprising hydrolysing collagenous tissue material to produce a collagen solution and spray-drying the collagen solution at a temperature below 120"C.
- 2. A process according to Claim 1, wherein the tissue material is isinglass.
- 3. A process according to Claim 1 or Claim 2, wherein the spray-dried collagen is re-hydrated to produce collagen finings.
- 4. A process according to Claim 1, substantially as described in Example 1.
- 5. Dried particulate collagen produced by a process according to any one of Claims 1 to 4.
- 6. Collagen finings produced by a method according to Claim 3.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9301086A GB2274458A (en) | 1993-01-20 | 1993-01-20 | Production of soluble collagen by hydrolysis and spray-drying |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9301086A GB2274458A (en) | 1993-01-20 | 1993-01-20 | Production of soluble collagen by hydrolysis and spray-drying |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| GB9301086D0 GB9301086D0 (en) | 1993-03-10 |
| GB2274458A true GB2274458A (en) | 1994-07-27 |
Family
ID=10729019
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| GB9301086A Withdrawn GB2274458A (en) | 1993-01-20 | 1993-01-20 | Production of soluble collagen by hydrolysis and spray-drying |
Country Status (1)
| Country | Link |
|---|---|
| GB (1) | GB2274458A (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001060922A1 (en) * | 2000-02-15 | 2001-08-23 | Euroresearch Srl | Process for the preparation of micronised collagen, and its therapeutic applications |
| WO2016146954A1 (en) | 2015-03-17 | 2016-09-22 | Universite Pierre Et Marie Curie (Paris 6) | Injectable collagen suspensions, the preparation method thereof, and the uses thereof, particularly for forming dense collagen matrices |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB903975A (en) * | 1960-01-26 | 1962-08-22 | Nihon Hikaku Kabushiki Kaisha | Improvements in and relating to the solubilization of collagen and reconstitution thereof |
| RO64884A2 (en) * | 1972-01-25 | 1978-12-15 | Piele Si Incaltaminte Flacara | PROCESS FOR THE PREPARATION OF COLLAGEN HYDROSCOPIC POWDERS |
| GB2147299A (en) * | 1983-03-14 | 1985-05-09 | Isinglass Manufacturers Limite | A process for treating collagen, and dried collagen produced by that process |
-
1993
- 1993-01-20 GB GB9301086A patent/GB2274458A/en not_active Withdrawn
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB903975A (en) * | 1960-01-26 | 1962-08-22 | Nihon Hikaku Kabushiki Kaisha | Improvements in and relating to the solubilization of collagen and reconstitution thereof |
| RO64884A2 (en) * | 1972-01-25 | 1978-12-15 | Piele Si Incaltaminte Flacara | PROCESS FOR THE PREPARATION OF COLLAGEN HYDROSCOPIC POWDERS |
| GB2147299A (en) * | 1983-03-14 | 1985-05-09 | Isinglass Manufacturers Limite | A process for treating collagen, and dried collagen produced by that process |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001060922A1 (en) * | 2000-02-15 | 2001-08-23 | Euroresearch Srl | Process for the preparation of micronised collagen, and its therapeutic applications |
| US20070253912A1 (en) * | 2000-02-15 | 2007-11-01 | Euroresearch Srl | Process for the preparation of micronised collagen, and its therapeutic applications |
| WO2016146954A1 (en) | 2015-03-17 | 2016-09-22 | Universite Pierre Et Marie Curie (Paris 6) | Injectable collagen suspensions, the preparation method thereof, and the uses thereof, particularly for forming dense collagen matrices |
| US11654212B2 (en) | 2015-03-17 | 2023-05-23 | Universite Pierre Et Marie Curie (Paris 6) | Injectable collagen suspensions, the preparation method thereof, and the uses thereof, particularly for forming dense collagen matrices |
Also Published As
| Publication number | Publication date |
|---|---|
| GB9301086D0 (en) | 1993-03-10 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| WAP | Application withdrawn, taken to be withdrawn or refused ** after publication under section 16(1) |