CN1133652C - Process for preparing collagen - Google Patents
Process for preparing collagen Download PDFInfo
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- CN1133652C CN1133652C CNB001205315A CN00120531A CN1133652C CN 1133652 C CN1133652 C CN 1133652C CN B001205315 A CNB001205315 A CN B001205315A CN 00120531 A CN00120531 A CN 00120531A CN 1133652 C CN1133652 C CN 1133652C
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- collagen
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Abstract
The present invention relates to a method for preparing collagen, which is characterized in that chrome leather shavings or chrome leather blocks are used as raw materials and are processed in an alkaline medium; the raw materials are purified by cation exchange resin as a collagen protein source and then are degraded by activity biologic enzyme for 0.5 to 4 hours at a temperature of 30 to 60 DEG C; furthermore, degraded materials are raised to 80 to 85 DEG C, keep a temperature for 15 to 30 minutes, are sterilized, and are concentrated by decompression at the vacuum degree of 0.06 to 0.10MPa at a temperature of 70 to 85 DEG C; therefore, a liquid state product of which the solid content is from 20 to 50% is obtained. Furthermore, the liquid state product is sprayed, is dried, and is packaged without bacilus, and a solid state collagen protein powder and polypeptide powder product is obtained. The product can be used for industry such as food, beverage, medicine, cosmetics, etc., and has obvious economical and social benefit.
Description
The present invention relates to a kind ofly utilize that the secondary refuse of process hides---chrome shavinge (piece) extracts the method for collagen protein and polypeptide, belongs to field of biological product.
In the at present commercially available food and medical gelatin, edible, medical collagen and polypeptide are with the by product in fresh skin of mammal, bone or the tanning production---rawhide corner, alkali skin bit are that raw material is made, and the cost height, use range is restricted; Mainly near mouth, the import collagen protein is a raw material with fresh animal skin all also with collagen protein for China's medicine, makeup etc., adopts alkaline process or acid system to make, as Japanese Patent JP8027035A.Acid-hydrolysis method rapidly and thoroughly, but tryptophane all destroys, Serine and tyrosine part are destroyed, the product yield is low, equipment corrosion is serious, and produces secondary pollution; Alkali hydrolysis method is also very rapid thoroughly, but hydroxyl and mercaptoamino-acid are all destroyed, and produces racemization (structure variation).Therefore, the collagen protein that acid, alkali hydrolysis method are produced reduces its biological activity, nutritive health-care, beauty functions because of the partial amino-acid structure variation.Chinese patent CN 1155549 and reported in literature thereof are raw material with the Mammals reticular tissue, and it is medical to adopt enzyme or organic acid to extract, the used for cosmetic collagen protein, raw materials used costliness, technology is loaded down with trivial details, production cycle is long, cost is high, the product yield is low, and product application is restricted.
The objective of the invention is to provide a kind of manufacture method of collagen protein at the deficiencies in the prior art, adopting cheap process hides, secondary refuse---chrome shavinge, chrome leather limit piece are raw material, make edible, medical, used for cosmetic collagen protein and polypeptide products under biotechnology and chemical physical action.
Purpose of the present invention is realized by following technical measures.
The manufacture method of collagen protein:
1. choose 100 parts of chrome shavinge or chrome leather pieces, add 100～150 parts in tap water, 1～5 part of nonionogenic tenside in 15～55 ℃ of temperature, stirred 60-180 minute, and venting liquid cleans 2～3 times for 200～600 parts with flowing water, squeezes (getting rid of) and does standby.
2. with 100 parts of standby raw materials, add 150～600 parts of deionized waters, transfer pH10-11 to separate filtration in 0.5～5.5 hour in 80～90 ℃ of glue of temperature with 2.0～10 parts in alkali, filter cake reclaims separately and contains chrome protein.Filtrate feeds CO
2Or adding Na
2CO
3, NaHCO
3, Na
2HPO
4Or NaH
2PO
46～12 parts, left standstill 5～15 hours, clear liquid is handled by Zeo-karb, makes highly purified collagen protein source.
3. through the collagen liquid of plastic resin treatment, add 0.01～0.2 part of biological enzyme with high activity, be warmed up to 30～60 ℃, degraded 0.5～4 hour, under mild conditions, be degraded to the collagen protein and the polypeptide of desired molecule amount.Be warmed up to 80～85 ℃ then, be incubated 15～30 minutes, after the sterilization, in vacuum tightness 0.06～0.10MPa, 70～85 ℃ of concentrating under reduced pressure of temperature, acquisition solid content are 20～50% liquid product, with the liquid product spraying drying, sterile packed promptly gets solid state collagen protein powder and polypeptide powder product again.
Active biological enzyme is a trypsinase, pancreas galactase, stomach en-, and microbial enzyme is or/and papoid is at least a.
Regulating pH value alkali is NH
3Water, NaOH, KOH, Na
2CO
3, NaHCO
3, GaO, Ca (OH)
2Or milk of lime is at least a.
Collagen protein and polypeptide products good quality that the present invention makes are in anhydrous (over dry) solids, ash content (Ash)≤0.5%, its Ca
2+, Mg
2+Content＜0.2%, Cr (III)≤0.2mg/kg, total amino acid content reaches 95%.And United States Patent (USP) U.S.P5271912 claims Chrome-free in gelatin and the hydrolytic collagen, but the patent inventor studies show that recently (gelatin and the protolysate ash oontent 5.23～15.09% of JALCA Vol 92,200 (1997) preparations, chromium content is up to 3.4 * 10
4～5.01 * 10
5Mg/kg, (JALCA Vol 93 40 (1998) reaches 7.38% with the gelatin ash content of top condition preparation to another report, and chromium content reaches 2.5 * 10
4Mg/kg, the protolysate of preparation after mixture iron exchange resin is handled, ash content＜1.0%, chromium content is up to 5.0～10
3Mg/kg (all in over dry)
The present invention has following advantage
1. chrome shavinge, chrome leather piece have been realized that high value efficiently transforms, opened up new collagen protein resource.
2. for chrome shavinge and chrome leather piece have found good outlet, further fully reclaimed chromium, reduced the pollution of chromic salts environment.
3. remarkable in economical benefits.Chrome shavinge and chrome leather piece are commonly used to processing industry gelatin or animal-feed protein powder, abroad have as fertilizer etc.But chromium content height in, the feedstuff protein low because of the technical gelatine quality is substantially without chrome shavinge (piece) glue and feedstuff protein.Chrome shavinge (piece) gets nowhere.The leather bits that pile up like a mountain around the tannery, leather limit piece are seriously threatening the existence of tannery.Technical gelatine or animal-feed protein powder can only be sold 0.5～0.8 ten thousand yuan/ton usually.The collagen protein of the present invention's preparation and polypeptide (edible, medical) price usually reach 4.5～6.0 ten thousand yuan/ton: used for cosmetic polypeptide, Collagen Hydrolysate can be sold 20～40.0 ten thousand yuan/ton; Have up to 700～1000 yuan/kilogram, the height of its added value really is " turning waste into wealth ".
4. social environment benefit is outstanding.China's year leather processing amount accounts for 1/5 of the world at present.Rank first in the world.The annual generation contains about 30～400,000 tons of chromium solid waste (wherein containing the collagen egg from about 60%).Because suitably utilized, not only cause billions of first financial losses, and rotten rot to cause great environmental pollution, seriously have influence on the Sustainable development of tanning industry.Utilize the present invention that chrome shavinge and chrome leather limit piece are converted into the collagen protein and the polypeptide of high added value, not only can create remarkable economic efficiency, do not produce secondary pollution in the production process substantially, also can reduce environmental pollution, belong to eco-friendly green chemical industry.This benign development, leading position and Sustainable development in the processing of world's leather industry, trade of maintenance development of China leather industry to promoting China's husbandry, leather industry; and create technology and protection of home industries, resource and market with independent intellectual property rights, have the important strategic contribution.
5. the present invention has significant Atom economy, meets the 21 century development strategy.
Embodiment
Below by embodiment the present invention is specifically described; be necessary to be pointed out that at this following examples only are used for the present invention is further specified; can not be interpreted as limiting the scope of the invention, the person skilled in the art in this field can make some nonessential improvement and adjustment to the present invention according to the invention described above content.
1. choose chrome shavinge or chrome leather piece 100g, add 15～55 ℃ of tap water 200g nonionogenic tenside 2g, stirred 80 minutes, venting liquid cleans 2～3 times with the 300g flowing water again, squeezes (getting rid of) and does standby.Get standby raw material 100g, add deionized water 300g, with CaO 2.5～3.0 grams, regulate pH10-11, separate 3～4 hours after-filtration in 80～90 ℃ of glue of temperature, filter cake reclaims separately and contains chrome protein, and filtrate feeds CO
2Become muddy to clear liquid, leave standstill deliming in 8～10 hours; Clear liquid feeds 731 or 732 resin columns, liquid after treatment adds ammoniacal liquor and regulates pH7.5～8.0, adds 0.02～0.1 part in trypsinase, is warmed up to 30-40 ℃ of degraded 2-5 hour, be warmed up to 80-85 ℃ then, be incubated sterilization in 15～30 minutes, in vacuum tightness 0.06～0.10MPa, temperature 70-85 ℃ of concentrating under reduced pressure, the acquisition solid content is 20～25% liquid product, with the liquid product spraying drying, sterile packed promptly gets solid state collagen protein powder and polypeptide powder product again.
2. choose chrome shavinge or chrome leather piece 100g, add 15～55 ℃ of tap water 300g, nonionogenic tenside 3g, stirred 120 minutes, venting liquid cleans 2～3 times with the 500g flowing water again, squeezes (getting rid of) and does standby.Get standby raw material 100g, add deionized water 400g, with Ca (OH)
23.5～5.0g regulates pH10-11, separates 3～6 hours after-filtration in temperature 80-90 ℃ glue, filter cake reclaims separately and contains chrome protein, and solution adds Na
2CO
35-8g left standstill 10-12 hour, clear liquid is by 731 or 732 resin columns, liquid after treatment, add 0.1～0.5 part of 0.05～0.01 part in microbial enzyme 0.1～0.2g trypsinase and stomach en-, be warmed up to 35～50 ℃ of degradeds 3～3.5 hours, be warmed up to 80～85 ℃ then, be incubated sterilization in 15～30 minutes, in vacuum tightness 0.06～0.1MPa, 70～85 ℃ of concentrating under reduced pressure of temperature, the acquisition solid content is 20～50% liquid product, again with the liquid product spraying drying, sterilising packaging promptly gets solid-state polypeptide powder product.
3. choose chrome shavinge or chrome leather piece 100g, add 15～55 ℃ of tap water 400g, nonionogenic tenside 4g stirred 150 minutes, and venting liquid cleans 2-3 time with the 600g flowing water again, extracts standby.Get standby raw material 130g, add deionized water 600g, regulate pH10-11 with milk of lime 10～12g, separate 5～5.5 hours after-filtration in 80～90 ℃ of glue of temperature, filter cake reclaims separately and contains chrome protein, and filtrate adds Na
2HPO
48～10 parts, left standstill 12-15 hour, clear liquid is by 731 or 732 resin columns.Liquid after treatment.Add 0.05～0.3 part of microbial enzyme, be warmed up to 50-60 ℃, degraded 3.5-4 hour, be warmed up to 80-85 ℃ of insulation sterilization in 15-30 minute then, in vacuum tightness 0.06-0.1MPa, temperature 70-85 ℃ of concentrating under reduced pressure, obtaining solid content is the 20-50% liquid product, with the liquid product spraying drying, sterile packed promptly gets solid state collagen protein powder and polypeptide powder product again.
Claims (3)
1. the manufacture method of a collagen protein is characterized in that:
A, choose 100 parts of chrome shavinge or chrome leather pieces, add 100～150 parts in tap water, 1～5 part of nonionogenic tenside in 15～55 ℃ of temperature, stirred 60～180 minutes, venting liquid, cleaned 2-3 time for 200～600 parts with flowing water, and crowded (getting rid of) is dried standby,
B, with 100 parts of standby raw materials, add 150～600 parts of deionized waters, regulate pH10～11 for 2.0～10 parts with alkali, separated 0.5～5.5 hour in 80～90 ℃ of glue of temperature, filter, filter cake reclaims separately and contains chrome protein, filtrate feeds CO
2Or adding Na
2CO
3, NaHCO
3, Na
2HPO
4Or NaH
2PO
40.6～12 parts, left standstill 5～15 hours, deliming, clear liquid is handled by Zeo-karb, makes highly purified collagen protein source,
C, through the collagen liquid of plastic resin treatment, add 0.01～0.2 part of biological enzyme, be warmed up to 30～60 ℃, degraded 0.5～4 hour with high activity, be warmed up to 80～85 ℃ then, be incubated 15～30 minutes, after the sterilization, in vacuum tightness 0.06～0.10MPa, 70～85 ℃ of concentrating under reduced pressure of temperature, the acquisition solid content is 20～50% liquid product, again with liquid product spraying drying, sterile packed, promptly gets solid state collagen protein powder and polypeptide powder product.
2. according to the manufacture method of the described collagen protein of claim 1, it is characterized in that active biological enzyme is a trypsinase, the pancreas galactase, stomach en-, microbial enzyme are or/and papoid is at least a.
3. according to the manufacture method of claim 1 or 2 described collagen proteins, it is characterized in that regulating pH alkali is NH
3Water, NaOH, KOH, Na
2CO
3, NaHCO
3, CaO, Ca (OH)
2Or milk of lime is at least a.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CNB001205315A CN1133652C (en) | 2000-11-01 | 2000-11-01 | Process for preparing collagen |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CNB001205315A CN1133652C (en) | 2000-11-01 | 2000-11-01 | Process for preparing collagen |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN1351083A CN1351083A (en) | 2002-05-29 |
| CN1133652C true CN1133652C (en) | 2004-01-07 |
Family
ID=4588217
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CNB001205315A Expired - Fee Related CN1133652C (en) | 2000-11-01 | 2000-11-01 | Process for preparing collagen |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN1133652C (en) |
Families Citing this family (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN100434529C (en) * | 2005-04-22 | 2008-11-19 | 黄磊 | III type proteinic small peptide and preparation technique thereof |
| CN100441165C (en) * | 2006-06-05 | 2008-12-10 | 成都珂萝瑞诗化妆品有限公司 | Cosmetics containing biological active collagen |
| CN101993960B (en) * | 2010-11-23 | 2013-08-21 | 福建冠兴皮革有限公司 | Leatherworking retanning method using chromium leather scraps |
| CN102199193A (en) * | 2011-03-28 | 2011-09-28 | 中国科学院过程工程研究所 | Method for separating functional polypeptide from antler glue based on affinity chromatography |
| CN102199192A (en) * | 2011-03-29 | 2011-09-28 | 中国科学院过程工程研究所 | Method for separating functional polypeptide from tortoise-shell glue |
| JP6377431B2 (en) * | 2014-06-26 | 2018-08-22 | 富士フイルム株式会社 | Beverage composition |
| CN114057865A (en) * | 2021-11-15 | 2022-02-18 | 河北中皮东明科技有限公司 | Method for reducing ash content of collagen |
-
2000
- 2000-11-01 CN CNB001205315A patent/CN1133652C/en not_active Expired - Fee Related
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| Publication number | Publication date |
|---|---|
| CN1351083A (en) | 2002-05-29 |
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