CN101186786B - 一种从制革废皮边角料中提取未变性天然胶原的方法 - Google Patents
一种从制革废皮边角料中提取未变性天然胶原的方法 Download PDFInfo
- Publication number
- CN101186786B CN101186786B CN200710300903.1A CN200710300903A CN101186786B CN 101186786 B CN101186786 B CN 101186786B CN 200710300903 A CN200710300903 A CN 200710300903A CN 101186786 B CN101186786 B CN 101186786B
- Authority
- CN
- China
- Prior art keywords
- collagen
- sex change
- natural collagen
- scrap
- change natural
- 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.)
- Expired - Fee Related
Links
- 102000008186 Collagen Human genes 0.000 title claims abstract description 53
- 108010035532 Collagen Proteins 0.000 title claims abstract description 53
- 229920001436 collagen Polymers 0.000 title claims abstract description 48
- 238000000034 method Methods 0.000 title claims abstract description 23
- 239000010985 leather Substances 0.000 title claims abstract description 19
- 239000002699 waste material Substances 0.000 title description 11
- 239000000463 material Substances 0.000 claims abstract description 10
- 108091005804 Peptidases Proteins 0.000 claims abstract description 8
- 239000013049 sediment Substances 0.000 claims abstract description 8
- 239000002253 acid Substances 0.000 claims abstract description 6
- 230000008859 change Effects 0.000 claims description 25
- 230000008569 process Effects 0.000 claims description 12
- 239000012530 fluid Substances 0.000 claims description 10
- 239000000284 extract Substances 0.000 claims description 9
- 239000002994 raw material Substances 0.000 claims description 8
- 239000000243 solution Substances 0.000 claims description 8
- 102000035195 Peptidases Human genes 0.000 claims description 7
- 239000007788 liquid Substances 0.000 claims description 7
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 6
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 claims description 4
- 206010053262 Skin swelling Diseases 0.000 claims description 4
- 238000001556 precipitation Methods 0.000 claims description 4
- 239000006228 supernatant Substances 0.000 claims description 4
- 239000008399 tap water Substances 0.000 claims description 4
- 235000020679 tap water Nutrition 0.000 claims description 4
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims description 3
- 239000011780 sodium chloride Substances 0.000 claims description 3
- 238000003756 stirring Methods 0.000 claims description 3
- 210000002784 stomach Anatomy 0.000 claims description 3
- 241000233866 Fungi Species 0.000 claims description 2
- 239000012670 alkaline solution Substances 0.000 claims description 2
- 238000005119 centrifugation Methods 0.000 claims description 2
- 238000000502 dialysis Methods 0.000 claims description 2
- 238000000605 extraction Methods 0.000 claims description 2
- 238000002203 pretreatment Methods 0.000 claims description 2
- 239000003513 alkali Substances 0.000 abstract description 10
- 230000001105 regulatory effect Effects 0.000 abstract 2
- 239000004365 Protease Substances 0.000 abstract 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 abstract 1
- 235000013305 food Nutrition 0.000 description 7
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 6
- 239000003795 chemical substances by application Substances 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 108010010803 Gelatin Proteins 0.000 description 3
- 239000008273 gelatin Substances 0.000 description 3
- 229920000159 gelatin Polymers 0.000 description 3
- 235000019322 gelatine Nutrition 0.000 description 3
- 235000011852 gelatine desserts Nutrition 0.000 description 3
- 230000003301 hydrolyzing effect Effects 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- 206010022998 Irritability Diseases 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 229910052791 calcium Inorganic materials 0.000 description 2
- 239000011575 calcium Substances 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000002537 cosmetic Substances 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 238000004090 dissolution Methods 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 239000003292 glue Substances 0.000 description 2
- 239000000413 hydrolysate Substances 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000002910 solid waste Substances 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 108060008539 Transglutaminase Proteins 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 230000003796 beauty Effects 0.000 description 1
- 235000013361 beverage Nutrition 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000001311 chemical methods and process Methods 0.000 description 1
- 229910052804 chromium Inorganic materials 0.000 description 1
- 239000011651 chromium Substances 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- JEIPFZHSYJVQDO-UHFFFAOYSA-N ferric oxide Chemical compound O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 description 1
- 108010025899 gelatin film Proteins 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000000976 ink Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000001473 noxious effect Effects 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 239000004014 plasticizer Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000007639 printing Methods 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000005507 spraying Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000005477 standard model Effects 0.000 description 1
- 229920001169 thermoplastic Polymers 0.000 description 1
- 239000004416 thermosoftening plastic Substances 0.000 description 1
- 230000017423 tissue regeneration Effects 0.000 description 1
- 102000003601 transglutaminase Human genes 0.000 description 1
- 125000000391 vinyl group Chemical group [H]C([*])=C([H])[H] 0.000 description 1
- 229920002554 vinyl polymer Polymers 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
Landscapes
- Cosmetics (AREA)
- Treatment And Processing Of Natural Fur Or Leather (AREA)
Abstract
一种从制革废皮边角料中提取未变性天然胶原的方法，其特点是按重量份将牛片灰碱皮边角料100份，用碱调节pH＝8-12使皮溶胀24-48小时，用浓度为15-60g/L溶液pH＝8-12的H2O2漂白3-8小时，再经脱钙、淘洗、过滤得沉渣；取上述沉渣100份，加入蛋白酶0.5-6份，用酸调节pH＝2-4，于温度4-6℃搅拌1-3天，离心分离得到胶原溶液，用0.5-3mNaCl盐析，沉淀经离心分离后用0.1-2m乙酸溶解反复处理2次，经膜透析，获得5-8％未变性天然牛皮胶原蛋白液。
Description
本案由中国专利200610022188.5分案申请
技术领域
本发明涉及一种从制革废皮边角料中提取未变性天然胶原的方法，属于制革固体废弃物高附加值转化领域。
背景技术
据不完全统计，我国每年加工猪、牛等皮革1.7亿张，约产生70万吨的边角料废弃物(不含铬)。其中主要是原皮修边边角料、片灰皮或硝皮产生的边角料。这些固体废弃物是造成皮革工业污染严重的重要因素之一。由于它们的主要成分是胶原蛋白，利用皮边角料提取优质胶原蛋白，深度开发成高附加值产品，不仅可以为制革工业提供了解决固体废弃物污染的途径，更为重要的是，动物质资源的综合开发和高值利用，必将产生巨大的经济、环境和社会效益。
牛皮制革主要采用片灰碱皮技术，因此产生了大量的废灰碱皮边角料。而对于档次比较低的猪皮而言，由于采用硝皮工艺可以提高对胶原纤维的松散作用，使裸皮的厚度差异变小，反绒革起绒好，绒毛细致，所以近几年来，很多猪皮制革都采用了片硝皮工艺，从而产生了大量的废硝皮边角料。(赵令仪猪皮服装革硝皮工艺的利弊分析。四川皮革，1997，2：9)以牛皮的废灰碱皮边角料和猪皮的废硝皮边角料为原料提取未变性天然胶原可以大大提高这些废弃物的利用价值，变废为宝。
国内外的大量研究显示，皮边角料废弃物主要用于制造胶原的降解产物。在早期阶段，制革厂产生的废灰碱皮边角料多用来制作胶水，它的附加值不高，而且对环境造成了严重的污染，因此逐渐被淘汰。(Purps，Klaus.MASCHINENLEIMLEDER AUS DER LEDERHER STELLUNG.Left bracket Glue Stock fromLeather Production right bracket.Bundesminist Forsch Technol ForschungsberTechnol Forsch Entwickl，1977，7：54)皮边角料废弃物的综合利用逐渐向较高的附加值领域发展。美国专利报道了用中性或碱性蛋白酶消解原料皮和灰碱皮的皮边角料可以制得明胶(United States Patent：4220724)，用戊二醛作为交联剂与明胶反应可以制得食用级的胶原肠衣。用甘油作为可塑剂与明胶混合便可以得到机械性能比较好的凝胶膜，该膜可以用作非食品的包装材料(Taylor，M.M.；Liu，C.K.；Latona，N..Enzymatic modification of hydrolysis productsFrom collagen using a microbial transglutaminase.II.Preparation offilms.JALCA，2002，97(6)：225～234)。有关研究也证明了制革厂修边、切削产生的皮边角料是制作胶原基化妆品的原料。(Novel technique for the preparation ofcollagen derivatives for cosmetic-part 1：Preparation and characterisation of collagenproducts Ranqanayaki，M.D.；Ranqanathan，T.S.；Jayaraman，K.S..Research andIndustry，1988，33(3)：205～210)从制革厂的废皮边角料中得到水解胶原，然后按一定的比例加到聚乙烯醇中，所得薄膜的透水性能和生物降解能力都有所提高。该薄膜更适宜作医用包装袋。(Alexy，P.；Bakos，D.；Crkonova，G.；Kramarova，Z.Poly(vinyl alcohol)-collagen hydrolysate thermoplastic blends：II.Water penetrationand biodegradability of melt extruded films。Polymer Testing，2003，22(7)：811～818)国内在皮边角料废弃物的利用方面也由大量的报道。将片灰碱皮产生的边角料经脱钙，酸碱处理后，用多种酶结合降解，然后经分离、浓缩、喷雾干燥后得到食用级的水解胶原蛋白粉(张铭让、林炜、穆畅道等，从皮边角料中提取胶原及其在食品中的应用.四川食品与发酵，2000，3：61～65)。用不同的单一酶和复合酶水解经过物理和化学方法预处理的皮边角废料，最终得到5种不同分子量分布范围的胶原蛋白多肽样品，其中高分子量胶原多肽适宜作为凝胶剂或保水剂用于制作可食性胶原膜和化妆品面膜。中、低分子量胶原多肽既可直接作为基料用于各种饮料、美容食品和化妆品的生产，又可作为保湿剂、乳化稳定剂和发泡剂。(王碧、贾冬英、罗红平等.皮边角废料提取胶原蛋白的功能特性.中国皮革，2002，31(15)：13～16)
综上所述，从制革产生的皮边角料废弃物中提取的产物都是水解胶原，它不具有生物活性，附加值不高。未变性天然胶原具有独特的生物相容性、生物降解性和低抗原性，在烧伤、创伤、硬组织修复方面有很大的应用前景。(ChiH.Lee，Anuj Singla and Yugyung Lee，Biochemical application of collagen，InternationJournal of Pharmaceutics，2001，221：1-22)因此从皮边角料废弃物中提取未变性天然胶原可以大大提高它的利用价值。
发明内容
本发明的目的是针对现有技术的不足提供一种从制革废皮边角料中提取未变性天然胶原的方法。其特点是用脱钙液脱除牛片灰碱皮边角料中的钙，于低温和酸性条件下用蛋白酶提取获得未变性天然胶原。
本发明的目的由以下技术实现，其中所述原料份数除特殊说明外，均为重量份数。
从制革废皮边角料中提取未变性天然胶原的方法
1、原料的预处理
将牛片灰碱皮边角料，绞碎，取100份，用碱溶液调节pH＝8-12使皮溶胀24-48小时，用浓度为15-60g/L，溶液pH＝8-12的H2O2漂白3-8小时，再用150-250份的脱钙液脱钙24-48小时，自来水充分淘洗，过滤得沉渣，备用；
2、未变性天然胶原的提取
将上述已预处理的原料100份，加入蛋白酶0.5-6份，用酸调节pH＝2-4，于温度4-6℃搅拌1-3天，得到未变性天然胶原蛋白液。
3、未变性天然胶原的纯化
将上述胶原蛋白液，用16000-20000rpm高速离心机分离，除去滤渣，上层清液加入0.5-3MNaCl盐析，所得沉淀经离心分离后用0.1-2M乙酸溶解，如此反复盐析处理1-3次，再经膜透析处理，获得5-8％未变性天然牛皮胶原蛋白液。
脱钙液为0.1-1.0M EDTA脱钙液或0.2-1.2MHCl脱钙液中的任一种。
蛋白酶为胃蛋白酶、537蛋白酶或真菌复合酶中的任一种。
制得的未变性天然胶原用粘度法测其变性温度，测试结果详见图1所示，结果表明：牛皮未变性天然胶原的变性温度为35-40℃。用SDS-PAGE测试胶原蛋白的分子量及其分布，结果详见图2所示。所得未变性天然胶原可以用于高级美容化妆品和保健品领域。
本发明具有如下优点：
1.发明在降低制革固废物污染的同时，找出了一条制革废皮边角料的高附加值利用途径。
2.本发明用脱钙液脱除牛皮片灰碱皮边角料中的钙，在酸性条件下于温度4-6℃用蛋白酶提取获得未变性天然胶原。
3.本发明制得的天然胶原不同于水解胶原，它具有独特的生物相容性、生物降解性和低抗原性，在食品、化妆品、生物工程等领域有广阔的应用前景。
附图说明
图1为牛皮胶原的折算粘度(F)-温度(T)图
图2牛皮胶原的SDS-PAGE电泳图，
其中M为标准样品，1为猪皮胶原，2为牛皮胶原
具体实施方式
下面通过实施例对本发明进行具体描述，有必要在此指出的是本实施例只用于对本发明进行进一步说明，不能理解为对本发明保护范围的限制，该领域的技术熟练人员可以根据上述本发明的内容作出一些非本质的改进和调整。
实施例1：取牛片灰碱皮边角料，绞碎，取100g，用2M NaOH溶液调节pH＝8使皮溶胀24小时，用浓度为30g/L溶液pH＝8的H2O2漂白3小时，再用200g0.5M EDTA脱钙液脱钙24小时，自来水充分淘洗，过滤得沉渣，用酸调节pH＝2.5，加入胃蛋白酶2g，于温度4-6℃搅拌24小时。离心除去滤渣，上清液中加入0.7M的NaCl盐析，用0.5M乙酸溶解沉淀，得到浓度为5％的牛皮未变性天然胶原溶液约600g。
实施例2：取牛片灰碱皮边角料，绞碎，取100g，用2M NaOH溶液调节pH＝12使皮溶胀48小时，用浓度为60g/L溶液pH＝10的H2O2漂白8小时，再用250g的1.0M HCl脱钙液脱钙48小时，自来水充分淘洗，过滤得沉渣，用酸调节pH＝3，加入537蛋白酶5g，于温度4-6℃搅拌48小时，离心除去滤渣，上清液中加入2.1M的NaCl盐析，用0.5M乙酸溶解沉淀，得到浓度为8％的牛皮未变性天然胶原溶液约650g。
Claims (3)
1.一种从制革废皮边角料中提取未变性天然胶原的方法，其特征在于该方法包括以下步骤：
(1)原料的预处理
将牛片灰碱皮边角料，绞碎，取100重量份，用碱溶液调节pH＝8-12使皮溶胀24-48小时，用浓度为15-60g/L溶液pH＝8-12的H2O2漂白3-8小时，再用150-250重量份的脱钙液脱钙24-48小时，自来水充分淘洗，过滤得沉渣，备用；
(2)未变性天然胶原的提取
将上述已预处理的原料100重量份，加入蛋白酶0.5-6重量份，用酸调节pH为2-4，于温度4-6℃搅拌1-3天，得到未变性天然胶原蛋白液；
(3)未变性天然胶原的纯化
将上述胶原蛋白液，用16000-20000rpm高速离心机分离，除去滤渣，上清液中加入0.5-3M的NaCl盐析，沉淀经离心分离后用0.1-2M乙酸溶解，如此反复盐析1-3次，再经膜透析处理，获得5-8％未变性天然牛皮胶原蛋白液。
2.如权利要求1所述从制革废皮边角料中提取未变性天然胶原的方法，其特征在于脱钙液为0.1-1.0M EDTA或者0.2-1.2M HCl中的任一种。
3.如权利要求1所述从制革废皮边角料中提取未变性天然胶原的方法，其特征在于蛋白酶为胃蛋白酶、537蛋白酶或真菌复合酶中的任一种。
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN200710300903.1A CN101186786B (zh) | 2006-11-06 | 2006-11-06 | 一种从制革废皮边角料中提取未变性天然胶原的方法 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN200710300903.1A CN101186786B (zh) | 2006-11-06 | 2006-11-06 | 一种从制革废皮边角料中提取未变性天然胶原的方法 |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN200610022188.5A Division CN100526410C (zh) | 2006-11-06 | 2006-11-06 | 一种从制革废皮边角料中提取未变性天然胶原的方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN101186786A CN101186786A (zh) | 2008-05-28 |
| CN101186786B true CN101186786B (zh) | 2010-06-09 |
Family
ID=39479413
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN200710300903.1A Expired - Fee Related CN101186786B (zh) | 2006-11-06 | 2006-11-06 | 一种从制革废皮边角料中提取未变性天然胶原的方法 |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN101186786B (zh) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2019111275A1 (en) | 2017-12-04 | 2019-06-13 | Council Of Scientific And Industrial Research | A process for complete utilization of raw hide / skin to yield valuable products |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101647816B (zh) * | 2008-08-13 | 2012-11-28 | 代龙 | 一种动物皮类的酶解产物及其用途 |
| CN105010737A (zh) * | 2015-07-27 | 2015-11-04 | 徐州鸿丰高分子材料有限公司 | 基于制革碱皮去肉废渣制备肉粉的方法 |
| CN111334551B (zh) * | 2020-04-01 | 2022-06-28 | 湖北瑞邦生物科技有限公司 | 一种牛皮胶原蛋白肽的生产工艺 |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1407640A (zh) * | 2001-09-03 | 2003-04-02 | 浙江南都电源动力股份有限公司 | 纳米SiO2复合玻璃棉隔板 |
| KR20030074577A (ko) * | 2003-09-02 | 2003-09-19 | 주식회사 젤텍 | 멸균된 순수 수용성 콜라겐 펩타이드의 제조방법 |
| CN1597742A (zh) * | 2004-08-19 | 2005-03-23 | 四川大学 | 水溶性未变性天然胶原的制备方法 |
| CN1597741A (zh) * | 2004-08-19 | 2005-03-23 | 四川大学 | 未变性天然鱼胶原的制备方法 |
-
2006
- 2006-11-06 CN CN200710300903.1A patent/CN101186786B/zh not_active Expired - Fee Related
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1407640A (zh) * | 2001-09-03 | 2003-04-02 | 浙江南都电源动力股份有限公司 | 纳米SiO2复合玻璃棉隔板 |
| KR20030074577A (ko) * | 2003-09-02 | 2003-09-19 | 주식회사 젤텍 | 멸균된 순수 수용성 콜라겐 펩타이드의 제조방법 |
| CN1597742A (zh) * | 2004-08-19 | 2005-03-23 | 四川大学 | 水溶性未变性天然胶原的制备方法 |
| CN1597741A (zh) * | 2004-08-19 | 2005-03-23 | 四川大学 | 未变性天然鱼胶原的制备方法 |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2019111275A1 (en) | 2017-12-04 | 2019-06-13 | Council Of Scientific And Industrial Research | A process for complete utilization of raw hide / skin to yield valuable products |
Also Published As
| Publication number | Publication date |
|---|---|
| CN101186786A (zh) | 2008-05-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN100526410C (zh) | 一种从制革废皮边角料中提取未变性天然胶原的方法 | |
| Li et al. | Research progress on resource utilization of leather solid waste | |
| Noorzai et al. | Collagen extraction from various waste bovine hide sources | |
| Holkar et al. | Valorization of keratin based waste | |
| John Sundar et al. | Recovery and utilization of proteinous wastes of leather making: a review | |
| Krishnamoorthy et al. | Greener approach to leather tanning process: D-Lysine aldehyde as novel tanning agent for chrome-free tanning | |
| US5316942A (en) | Process for the production of low-cost soluble high-molecular weight collagen | |
| Chen et al. | Preparation and functional evaluation of collagen oligopeptide-rich hydrolysate from fish skin with the serine collagenolytic protease from Pseudoalteromonas sp. SM9913 | |
| de Menezes et al. | Industrial sustainability of microbial keratinases: production and potential applications | |
| CN101186786B (zh) | 一种从制革废皮边角料中提取未变性天然胶原的方法 | |
| Ningthoujam et al. | Keratinaceous wastes and their valorization through keratinolytic microorganisms | |
| CN105543315A (zh) | 胶原蛋白类发泡剂、其复配改性发泡剂以及二者的制备方法 | |
| CN106588340A (zh) | 一种低盐高浓度的氨基酸液体肥料的制备方法 | |
| CN102276716A (zh) | 一种从牛蛙皮中提取未变性天然胶原的方法 | |
| Senthilkumar et al. | Extraction of keratin from keratinous wastes: current status and future directions | |
| Wanyonyi et al. | Alkaliphilic enzymes and their application in novel leather processing technology for next-generation tanneries | |
| Said | Synthesis of collagen from Bali cattle's hide using a combination of acid and alkali on the extracting process. | |
| CN100480394C (zh) | 胶原蛋白-羧甲基纤维素共混制备移膜的方法 | |
| Lu et al. | Highly efficient shrimp shell recovery by solid-state fermentation with Streptomyces sp. SCUT-3 | |
| Ocak | Collagen hydrolysate/chitosan/keratin-based ternary films from bio-wastes of the leather and poultry industries against plastic waste generation | |
| Kiew et al. | Screening and empirical kinetic models of collagen extraction from selected Malaysian freshwater fish | |
| Matinong et al. | Collagen Extraction from Animal Skin. Biology 2022, 11, 905 | |
| Liu et al. | Efficient and clean preparation of pure collagen fiber woven materials from bovine hides using alkali-activated alkaline protease | |
| CN102407085B (zh) | 采用酶法水解制革下脚料为原料制备表面活性剂的方法 | |
| Negash G et al. | Production and characterization of glue from tannery hide trimming waste |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| C14 | Grant of patent or utility model | ||
| GR01 | Patent grant | ||
| C17 | Cessation of patent right | ||
| CF01 | Termination of patent right due to non-payment of annual fee |
Granted publication date: 20100609 Termination date: 20101106 |