US4185011A
Expired / Lapsed
US
⏱️ 0.0 years remaining
Process for the production of collagen fibers
Assignee: Henkel AG and Co KGaA
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Filing: 1978-10-16
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Granted: 1980-01-22
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Expires: 1998-10-16
Abstract
Abstract A process for the preparation of collagen fibers, especially suited for medicinal use, comprising subjecting animal skin, hide or tendons to digestion with a strong alkali until the material has an amide nitrogen content of approximately 0.20 to 0.40 mole per gram, swelling the mass by thorough intermixing with acid, mechanically separating collagen fibers from the mass, de-swelling the collagen fibers with salts or organic solvents, and dehydrating the collagen fibers to approximately 20 to 40 weight % moisture based on the dry weight of the fibers. A plasticizer may be applied to the fibrous mass before dehydration.
Inventors
- 👤 Zdenek Eckmayer
- 👤 Alexander Berg
- 👤 Joachim Kuhn
Bibliographic Details
Application Number
—
Jurisdiction
US
Data Source
google_patents
Last Synchronized
2026-10-22 23:22
CPC Classifications
D; D01; D01C; D01C3/00
Claims Analysis
Total Claims: 9
Claim 1
Independent Claim
87 words
A process for the preparation of collagen fibers, especially suited for medicinal use, comprising subjecting animal skin, hide or tendons to digestion with a strong alkali until the material has an amide nitrogen content of approximately 0.20 to 0.40 mole per gram, swelling the mass by thorough intermixing with acid, mechanically separating collagen fibers from the mass, de-swelling the collagen fibers with salts or organic solvents, and dehydrating the collagen fibers to approximately 20 to 40 weight % moisture based on the dry weight of the fibers.
Claim 2
Dependent Claim
87 words
A process for the preparation of collagen fibers, especially suited for medicinal use, comprising subjecting animal skin, hide or tendons to digestion with a strong alkali until the material has an amide nitrogen content of approximately 0.20 to 0.40 mole per gram, swelling the mass by thorough intermixing with acid, mechanically separating collagen fibers from the mass, de-swelling the collagen fibers with salts or organic solvents, and dehydrating the collagen fibers to approximately 20 to 40 weight % moisture based on the dry weight of the fibers.
Claim 3
Dependent Claim
41 words
The process according to claim 1, wherein the alkaline digestion is continued to an amide nitrogen content of approximately 0.30 to 0.40 mole per gram and the acid treatment is continued until the mass looks glassy, a strong swelling taking place.
Claim 4
Dependent Claim
44 words
The process according to claim 1, wherein the acid treatment is carried out by the addition of phosphoric acid, formic acid, sulfuric acid or hydrochloric acid and is continued until the pH throughout the cross-section of the material is from about 0.5 to 1.5.
Claim 5
Dependent Claim
42 words
The process according to claim 1, wherein the acid treatment is carried out by the addition of acetic acid, citric acid or lactic acid and is continued until the pH throughout the cross-section of the material is from about 2.5 to 3.5.
Claim 6
Dependent Claim
36 words
The process according to claim 1, wherein different sources of starting materials are separately digested with strong alkali until each achieves substantially the same amide nitrogen value, and then the materials are combined for further processing.
Claim 7
Dependent Claim
31 words
The process according to claim 1, wherein the mechanical separation of fibers from the de-swelled material is effected by means of a high pressure water jet of at least 5 atmospheres.
Claim 8
Dependent Claim
30 words
The process according to claim 1, wherein de-swelling after the mechanical separation of fibers is effected with about 5 to 20 weight % of salt based on the fiber weight.
Claim 9
Dependent Claim
48 words
The process according to claim 1, wherein prior to dehydration there is supplied to the collagen mass an approximately 5% solution of oleic acid in acetone or of glycerin in ethyl alcohol, whereby upon dehydration the oleic acid or glycerin is left in the collagen as a plasticizer.
References Cited (Backward Citations)
DE1619288U
Cited
DE1494740C3
Cited
US3435117A
Cited
US3637642A
Cited
US3579358A
Cited
US4097234A
Cited
USPTO Annuity & Maintenance Windows
| Annuity Stage | Window Opens | Payment Deadline | Surcharge Period Until | Estimated Fee | Status |
|---|---|---|---|---|---|
| 3.5 Years (Year 4) | 1983-01-21 | 1983-07-23 | 1984-01-22 | $2000.00 | Window Closed / Lapsed |
| 7.5 Years (Year 8) | 1987-01-21 | 1987-07-23 | 1988-01-22 | $3760.00 | Window Closed / Lapsed |
| 11.5 Years (Year 12) | 1991-01-21 | 1991-07-23 | 1992-01-22 | $7700.00 | Window Closed / Lapsed |