CN1403583A - Prepn of natural active protein and peptide - Google Patents
Prepn of natural active protein and peptide Download PDFInfo
- Publication number
- CN1403583A CN1403583A CN 02133462 CN02133462A CN1403583A CN 1403583 A CN1403583 A CN 1403583A CN 02133462 CN02133462 CN 02133462 CN 02133462 A CN02133462 A CN 02133462A CN 1403583 A CN1403583 A CN 1403583A
- Authority
- CN
- China
- Prior art keywords
- peptide
- protease
- natural
- enzymolysis
- protein
- 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.)
- Granted
Links
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 38
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 38
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 24
- 108091005804 Peptidases Proteins 0.000 claims abstract description 27
- 238000000034 method Methods 0.000 claims abstract description 22
- 102000004190 Enzymes Human genes 0.000 claims abstract description 15
- 108090000790 Enzymes Proteins 0.000 claims abstract description 15
- 238000006243 chemical reaction Methods 0.000 claims abstract description 11
- 238000002360 preparation method Methods 0.000 claims abstract description 11
- 239000008367 deionised water Substances 0.000 claims abstract description 8
- 229910021641 deionized water Inorganic materials 0.000 claims abstract description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 8
- 238000003756 stirring Methods 0.000 claims abstract description 7
- 238000009826 distribution Methods 0.000 claims abstract description 6
- 238000004128 high performance liquid chromatography Methods 0.000 claims abstract description 6
- 238000004321 preservation Methods 0.000 claims abstract description 6
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims abstract description 6
- 239000004365 Protease Substances 0.000 claims description 25
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 25
- 239000000047 product Substances 0.000 claims description 15
- 241001465754 Metazoa Species 0.000 claims description 14
- 150000001875 compounds Chemical class 0.000 claims description 12
- 239000002994 raw material Substances 0.000 claims description 11
- 239000007795 chemical reaction product Substances 0.000 claims description 10
- 238000005842 biochemical reaction Methods 0.000 claims description 9
- 238000001976 enzyme digestion Methods 0.000 claims description 9
- 230000000813 microbial effect Effects 0.000 claims description 8
- 244000068988 Glycine max Species 0.000 claims description 7
- 235000010469 Glycine max Nutrition 0.000 claims description 7
- 240000008042 Zea mays Species 0.000 claims description 7
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 claims description 7
- 235000002017 Zea mays subsp mays Nutrition 0.000 claims description 7
- 235000005822 corn Nutrition 0.000 claims description 7
- 241000196324 Embryophyta Species 0.000 claims description 6
- 238000005238 degreasing Methods 0.000 claims description 6
- 230000009849 deactivation Effects 0.000 claims description 5
- 238000007710 freezing Methods 0.000 claims description 5
- 230000008014 freezing Effects 0.000 claims description 5
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 claims description 4
- 102000002322 Egg Proteins Human genes 0.000 claims description 4
- 108010000912 Egg Proteins Proteins 0.000 claims description 4
- 239000002253 acid Substances 0.000 claims description 4
- 235000014103 egg white Nutrition 0.000 claims description 4
- 210000000969 egg white Anatomy 0.000 claims description 4
- 238000010792 warming Methods 0.000 claims description 4
- 239000003513 alkali Substances 0.000 claims description 3
- 238000002203 pretreatment Methods 0.000 claims description 3
- 239000003643 water by type Substances 0.000 claims description 3
- 230000035484 reaction time Effects 0.000 claims description 2
- 238000005070 sampling Methods 0.000 claims description 2
- 238000002156 mixing Methods 0.000 abstract description 3
- 102000035195 Peptidases Human genes 0.000 abstract description 2
- 238000004140 cleaning Methods 0.000 abstract 1
- 239000002131 composite material Substances 0.000 abstract 1
- 238000001816 cooling Methods 0.000 abstract 1
- 238000010438 heat treatment Methods 0.000 abstract 1
- 239000005445 natural material Substances 0.000 abstract 1
- 235000019833 protease Nutrition 0.000 abstract 1
- 239000000376 reactant Substances 0.000 abstract 1
- 230000001105 regulatory effect Effects 0.000 abstract 1
- 230000008569 process Effects 0.000 description 12
- 102000008186 Collagen Human genes 0.000 description 4
- 108010035532 Collagen Proteins 0.000 description 4
- 230000004071 biological effect Effects 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 229920001436 collagen Polymers 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 210000002784 stomach Anatomy 0.000 description 3
- 238000005903 acid hydrolysis reaction Methods 0.000 description 2
- 230000000975 bioactive effect Effects 0.000 description 2
- 230000000593 degrading effect Effects 0.000 description 2
- 238000003912 environmental pollution Methods 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 239000003531 protein hydrolysate Substances 0.000 description 2
- 108010022579 ATP dependent 26S protease Proteins 0.000 description 1
- 102100031780 Endonuclease Human genes 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 108090000708 Proteasome Endopeptidase Complex Proteins 0.000 description 1
- 102000004245 Proteasome Endopeptidase Complex Human genes 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- JEIPFZHSYJVQDO-UHFFFAOYSA-N ferric oxide Chemical compound O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000012567 medical material Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 229930014626 natural product Natural products 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
Landscapes
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
Abstract
The present invention is the preparation process of natural active protein and peptide. The natural material with rich protein is processed through defatting, cleaning, homogenizing, mixing with deionized water inside a bioreactor, pH regulating to 5-8, heating to 70-90 deg.c, maintaining and stirring for 10-30 min, quick cooling to 30-50 deg.c and mixing with composite proteinase for enzymolysis for 2-6 hr. During enzymolysis, the reactant is sampled once every 0.5 hr, and the molecular weight distribution of the product is determined in SDS-PAGE or HPLC/MS method. According to the requirement on the molecular weight of target product, the enzymolysis degree is judged, the end time of enzymolysis is determined, enzyme is deactivated immediately after finishing the reaction and the product is filtered and frozen for preservation.
Description
One, technical field
The present invention relates to the preparation method of natural active protein and peptide, belong to the biological products manufacture field.
Two, background technology
In recent years, the progress of natural proteinoid and peptide is rapid, and people self are to the continuous increase of pure natural product demand, the fashion that the pure natural property material has become people to pursue, and various is that the product of raw material also arises at the historic moment with the pure natural animals and plants.But because of the complex process of preparation natural active protein and peptide, efficient is low, and the product self stability is poor, and cost is high, thereby restricts the widespread use of this product.The analysis reason is as follows:
(1) no matter from 26S Proteasome Structure and Function, the compound that natural bioactive protein and peptide are the occurring in nature kinds, function is the most complicated, thereby it is not strong to separate the actual operation obtain a certain class natural protein or peptide from natural matter;
(2) complex process, agents useful for same and conditional request are comparatively harsh, must keep the proteinic peculiar structure of pure natural, could keep its functions peculiar and biologic activity;
(3) contain the material instability of protein and peptide product, proteinaceous product is subject to proteasome degradation, has increased many labile factors.
China is large agricultural country, and the natural matter of rich in proteins such as animal skin, egg white, soybean or corn is quite abundant.Developed country is widely used in medical material, cosmetics and skincare product, protective foods and functional foodstuff with natural protein and peptide; But China also rests on the roughing stage to its application present stage, and added value is low, causes the wasting of resources and environmental pollution simultaneously.
The biologically active function is the key property of protein and peptide, and the biological activity of protein and peptide depends primarily on its specific three-dimensional arrangement and conformation.In case after three-dimensional arrangement that these are specific and conformation are destroyed, protein will lose activity.General protease method when preparation natural protein and peptide, the inefficiency of protolysate raw material, and required time is long; And the technology that conventional acid hydrolysis and alkali hydrolysis method prepare natural protein and peptide, though the efficient height of protolysate raw material, but its inherent three-dimensional arrangement and conformation are suffered serious destruction to a great extent, and some amino acid may be decomposed simultaneously, thereby makes its product lose biological activity; Acid hydrolysis and basic hydrolysis technology also can be brought environmental pollution in addition.
Three, summary of the invention
The objective of the invention is to provide the preparation method of a kind of natural active protein and peptide at the deficiencies in the prior art, be characterized in using the microbial protease of edible safety and the efficient multicomponent compound protease that various plants, animal protease mix, adopt gentle biochemical reaction system, the activity of considering natural protein and peptide emphatically reclaims, and helps the industrialization of biological activity and functional protein and peptide preparation.
Purpose of the present invention is realized that by following technical measures wherein said raw material umber is parts by weight except that specified otherwise.
The recipe ingredient of natural active protein and peptide preparation is:
100 parts of the natural matters of rich in proteins
100～250 parts of deionized waters
0.02～0.5 part of polynary compound protease
Wherein, the natural matter of rich in proteins is at least a in animal skin, egg white, soybean or the corn; Polynary compound protease is at least a in microbial protease, plant protease and the animal protease.
The preparation method of natural active protein and peptide:
1. will be through strict check be rich in proteinic animal or plant natural matter, animal skin 1-5%Na
2CO
3Solution carries out degreasing, and soybean and corn are used rinsed with deionized water 3 times with the degreasing of physical squeezing method;
2. through 100～250 parts of 100 parts of the proteinaceous natural matters of above-mentioned pre-treatment and homogenate and deionized waters, add in the biochemical reactor;
3. regulate pH=5～8 with acid or alkali, be warming up to 70～90 ℃, insulated and stirred 10～30 minutes is cooled to 30～50 ℃ then rapidly;
4. add 0.02～0.5 part of polynary compound protease in biochemical reactor, after stirring, enzyme digestion reaction 2～6 hours;
5. sampling in per 0.5 hour once adopts SDS-PAGE or HPLC/MS method to measure the molecular weight distribution of biochemical reaction product, and according to the requirement to target product molecular weight size, judgement native protein raw material is determined the enzymolysis reaction time by the degree of enzymolysis;
6. with enzyme deactivation, reaction product is filtered the freezing preservation in back.
The present invention has following advantage:
1. abandon conventional acid system, alkaline process and general enzyme process, the enzyme of use be eat, efficient multicomponent compound protease that the microbial protease of safety and various plants or animal protease mix;
2. before the enzyme digestion reaction, animal collagen 70～90 ℃ of insulated and stirred effects 10～30 minutes, can be changed the senior spirane structure of collagen, be beneficial to effective enzymolysis of proteolytic enzyme, warm-up time is short, and is very little to the activity influence of natural protein and peptide;
3. isolated microbial proteinous endonuclease capable acts on senior spirane structure such as collagen effectively from the natural protein leavened food, so this enzyme particularly to collagen protein, has good enzymolysis to multiple natural protein;
4. owing to added microorganism efficient protein enzyme in the polynary prozyme, other multiple protein enzymes have been added again, these enzymes act synergistically in the process of degrade proteins mutually, the native protein raw material of degrading more efficiently, and this is that other single enzymes or general prozyme can not reach;
5. according to target product control biochemical reaction process, the peptide chain in the directional enzymatic native protein raw material;
6. adopt gentle biochemical reaction system, prepared protein and peptide can keep its specific three-dimensional arrangement and conformation effectively, to guarantee its bioactive existence;
7. because the present invention abandons the shortcoming of conventional acid system, alkaline process and general enzyme process, its technical process, the native protein raw material of can not only degrading effectively, and be friendly to environment;
8. the employed enzyme of biochemical reaction of the present invention all is edible, so its product is a safe green.
Four, embodiment
Below by embodiment the present invention is carried out concrete description; be necessary to be pointed out that at this following examples only are used for the present invention is further detailed; but 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 according to the content of the invention described above.
Embodiment 1
(1) animal skin 3% Na
2CO
3Solution carries out degreasing, uses rinsed with deionized water 3 times;
(2) with after the pretreated animal skin double centner homogenate, mix for 150 kilograms, join in the biochemical reactor with deionized water;
(3) regulate pH=7, stir maintenance 10 minutes for 85 ℃, be cooled to 40 ℃ rapidly in temperature;
(4) add polynary compound protease (by microbial protease, papoid, bromeline, stomach en-and trypsinase approximately by 6: 1: 1: 1: 1 mixed) 20 restrain in biochemical reactor, after stirring, enzyme digestion reaction 2～6 hours;
(5) got one time sample in the enzymolysis process in per 0.5 hour, and adopt SDS-PAGE or HPLC/MS method to measure the molecular weight distribution situation of biochemical reaction product,, determine the enzyme digestion reaction termination time according to requirement to target product molecular weight size;
(6) with enzyme deactivation, reaction product is filtered, freezing preservation.
Embodiment 2
(1) with egg white double centner and deionized water double centner, join in the biochemical reactor behind the thorough mixing;
(2) regulate pH=7, be warming up to 40 ℃;
(3) add polynary compound protease (by microbial protease, papoid, bromeline, stomach en-and trypsinase approximately by 6: 1: 1: 1: 1 mixed) 20 grams in biochemical reactor, after stirring, enzyme digestion reaction 2～6 hours;
(4) got one time sample in the enzymolysis process in per 0.5 hour, and adopt SDS-PAGE or HPLC/MS method to measure the molecular weight distribution situation of biochemical reaction product,, determine the enzyme digestion reaction termination time according to requirement to target product molecular weight size;
(5) with enzyme deactivation, reaction product is filtered, freezing preservation.
Embodiment 3
(1) will clean through the soybean or the corn of strict check, pre-treatment such as squeezing, degreasing;
(2) with pretreated soybean or the homogenate of corn double centner, mix, join in the biochemical reactor with the deionized water double centner;
(3) regulate pH=7, be warming up to 40 ℃;
(4) add polynary compound protease (by microbial protease, papoid, bromeline, stomach en-and trypsinase approximately by 6: 1: 1: 1: 1 mixed) 25 restrain in biochemical reactor, after stirring, enzyme digestion reaction 2～6 hours;
(5) got one time sample in the enzymolysis process in per 0.5 hour, and adopt SDS-PAGE or HPLC/MS method to measure the molecular weight distribution situation of biochemical reaction product,, determine the enzyme digestion reaction termination time according to requirement to target product molecular weight size;
(6) with enzyme deactivation, reaction product is filtered, freezing preservation.
Claims (2)
1. the starting raw material prescription composition (by weight) of natural active protein and peptide preparation is:
100 parts of the natural matters of rich in proteins
100～250 parts of deionized waters
0.02～0.5 part of polynary compound protease
Wherein, the natural matter of rich in proteins is at least a in animal skin, egg white, soybean or the corn; Polynary compound protease is at least a in microbial protease, plant protease and the animal protease.
2. according to the preparation method of described natural active protein of claim 1 and peptide, it is characterized in that:
(1) animal skin 1-5%Na
2CO
3Solution carries out degreasing, and soybean and corn are used rinsed with deionized water 3 times with the degreasing of physical squeezing method;
(2) 100 parts of native protein raw materials after above-mentioned pre-treatment and homogenate and deionized water are 100～250 parts, add in the biochemical reactor;
(3) regulate pH=5～8 with acid or alkali, be warming up to 70～90 ℃, insulated and stirred 10～30 minutes is cooled to 30～50 ℃ then rapidly;
(4) add 0.02～0.5 part of polynary compound protease, after stirring, enzyme digestion reaction 2～6 hours;
(5) sampling in per 0.5 hour once adopts SDS-PAGE or HPLC/MS method to measure the molecular weight distribution of biochemical reaction product, and according to the requirement to target product molecular weight size, judgement native protein raw material is determined the enzymolysis reaction time by the degree of enzymolysis; Reaction makes enzyme deactivation after finishing at once;
(6) reaction product is filtered the freezing preservation in back.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN 02133462 CN1226419C (en) | 2002-07-12 | 2002-07-12 | Prepn of natural active protein and peptide |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN 02133462 CN1226419C (en) | 2002-07-12 | 2002-07-12 | Prepn of natural active protein and peptide |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN1403583A true CN1403583A (en) | 2003-03-19 |
| CN1226419C CN1226419C (en) | 2005-11-09 |
Family
ID=4747206
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN 02133462 Expired - Lifetime CN1226419C (en) | 2002-07-12 | 2002-07-12 | Prepn of natural active protein and peptide |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN1226419C (en) |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN100338224C (en) * | 2004-04-01 | 2007-09-19 | 广西大学 | Method for preparing peptide of soybean through continuous enzyme membrane reaction of soyabean protein |
| CN101263861B (en) * | 2008-05-08 | 2011-03-23 | 广西广明药业有限公司 | Preparation animal protolysate |
| CN101264316B (en) * | 2008-05-08 | 2011-06-22 | 广西广明药业有限公司 | Preparation of medicinal protolysate |
| CN102994605A (en) * | 2012-11-28 | 2013-03-27 | 张有聪 | Method for producing high-efficiency biological peptide through enzymolysis and microbe fermentation |
| CN101824455B (en) * | 2009-03-06 | 2013-07-17 | 香港百特有限公司 | Soy protein oligopeptide, and preparation method and use thereof |
| CN103305580A (en) * | 2013-07-03 | 2013-09-18 | 广州金娜宝生物科技有限公司 | Method for preparing collagen peptide from mammal skin and bone |
-
2002
- 2002-07-12 CN CN 02133462 patent/CN1226419C/en not_active Expired - Lifetime
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN100338224C (en) * | 2004-04-01 | 2007-09-19 | 广西大学 | Method for preparing peptide of soybean through continuous enzyme membrane reaction of soyabean protein |
| CN101263861B (en) * | 2008-05-08 | 2011-03-23 | 广西广明药业有限公司 | Preparation animal protolysate |
| CN101264316B (en) * | 2008-05-08 | 2011-06-22 | 广西广明药业有限公司 | Preparation of medicinal protolysate |
| CN101824455B (en) * | 2009-03-06 | 2013-07-17 | 香港百特有限公司 | Soy protein oligopeptide, and preparation method and use thereof |
| CN102994605A (en) * | 2012-11-28 | 2013-03-27 | 张有聪 | Method for producing high-efficiency biological peptide through enzymolysis and microbe fermentation |
| CN102994605B (en) * | 2012-11-28 | 2014-03-19 | 张有聪 | Method for producing high-efficiency biological peptide through enzymolysis and microbe fermentation |
| CN103305580A (en) * | 2013-07-03 | 2013-09-18 | 广州金娜宝生物科技有限公司 | Method for preparing collagen peptide from mammal skin and bone |
Also Published As
| Publication number | Publication date |
|---|---|
| CN1226419C (en) | 2005-11-09 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN103642843B (en) | Fermentation medium containing carbamide class nitrogen source and its purposes for producing secondary metabolite, enzyme and recombiant protein | |
| CN105494890A (en) | Enzymolysis and fermentation combined method for improving feeding nutritional value of rapeseed meal | |
| CN101948900A (en) | Method for extracting hydrolyzed collagen from bovine cartilage | |
| CN1470640A (en) | Collagenic protein powder, and its preparing method and use | |
| CN1226419C (en) | Prepn of natural active protein and peptide | |
| CN111418713B (en) | Feed for regulating intestinal health of micropterus salmoides | |
| CN1733925A (en) | Method with discarded protein Preparation Moriamin S | |
| CN103642885A (en) | Method for producing wheat biological active peptide by fermentation | |
| CN1633910A (en) | Sea cucumber oral liquid production method | |
| CN114956908A (en) | Deep sea fish peptide composite microbial fertilizer and preparation method thereof | |
| CN1110258C (en) | Enzymolysis process for preparing new protein source | |
| CN113481270B (en) | Method for extracting glycopeptide from scallop skirt | |
| CN105325701A (en) | Preparing method for biological active partner granulated feed | |
| Ovissipour et al. | Use of hydrolysates from Yellowfin tuna Thunnus albacares fisheries by-product as a nitrogen source for bacteria growth media | |
| CN110663813B (en) | Fish meal microbial fermentation and enzymolysis method | |
| CN1164728C (en) | Animal nutritious health wine and its producing process | |
| CN1552889A (en) | Use and preparation of collagen protein and collagen polypeptide | |
| GB2421890A (en) | Method for producing a palatability enhancer for a foodstuff | |
| CN102127579A (en) | Preparation process of mixed milk peptide | |
| KR20040065201A (en) | A manufacturing process of amino acid liquid fertilizer | |
| CN104642719A (en) | High-protein microbial fermentation feed and preparation method thereof | |
| CN1483340A (en) | Protein single fodder containing microelement chelate and preparation process thereof | |
| Calzoni et al. | Mixed microbial and thermal degradation of agricultural derived plant wastes. | |
| KR20000058843A (en) | The method for manufacturing of health drink | |
| CN1623412A (en) | Earthworm active peptide antibacerial feed material and its production method |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| ASS | Succession or assignment of patent right |
Owner name: GUANGDONG OU RUI KA BIOLOGICAL ENGINEERING CO., L Free format text: FORMER OWNER: XINYOU BIOTECHNOLOGY, CO., LTD., CHENGDU CITY Effective date: 20050715 |
|
| C41 | Transfer of patent application or patent right or utility model | ||
| TA01 | Transfer of patent application right |
Effective date of registration: 20050715 Address after: 510515, Guangdong, Guangzhou Province Road, Guangzhou Road, Beijing long building, 11 floor Applicant after: GUANGDONG OURIKA BIOTECHNOLOGY Co.,Ltd. Address before: 610031 23A1 building, Dahua building, No. 71, Lime Street, Chengdu, Sichuan Applicant before: Chengdu Xinyou Biotechnology Co.,Ltd. |
|
| C14 | Grant of patent or utility model | ||
| GR01 | Patent grant | ||
| C41 | Transfer of patent application or patent right or utility model | ||
| TR01 | Transfer of patent right |
Effective date of registration: 20081219 Address after: Yuexiu District Guangyuan West Road Guangzhou City No. 121 Building No. thirty-third the first floor of the United States Bo Patentee after: GUANGZHOU JORBLE BIOTECHNOLOGY Co.,Ltd. Address before: Floor 11, Beijing long tower, Guangzhou Road, Tonghe Road, Guangzhou, Guangdong Patentee before: GUANGDONG OURIKA BIOTECHNOLOGY Co.,Ltd. |
|
| ASS | Succession or assignment of patent right |
Owner name: GUANGZHOU JINNABAO BIOTECHNOLOGY CO., LTD. Free format text: FORMER OWNER: GUANGDONG OU RUI KA BIOLOGICAL ENGINEERING CO., LTD. Effective date: 20081219 |
|
| ASS | Succession or assignment of patent right |
Owner name: XIE JUN Free format text: FORMER OWNER: GUANGZHOU JORBLE SCIENCE +TECHNOLOGY CO., LTD. Effective date: 20100706 |
|
| C41 | Transfer of patent application or patent right or utility model | ||
| COR | Change of bibliographic data |
Free format text: CORRECT: ADDRESS; FROM: 510410 NO.33RD, 1ST FLOOR, MAIN BUILDING, MEIBO CITY, NO.121, GUANGYUAN WEST ROAD, YUEXIU DISTRICT, GUANGZHOU CITY TO: 510642 ROOM 505, BUILDING 18, NO.483, WUSHAN ROAD, TIANHE DISTRICT, GUANGZHOU CITY |
|
| TR01 | Transfer of patent right |
Effective date of registration: 20100706 Address after: 510642, room 18, building 483, No. five, 505 mountain road, Guangzhou, Tianhe District Patentee after: Xie Jun Address before: 510410 Guangzhou city Yuexiu District Guangyuan West Road No. 121 Building No. thirty-third the first floor of the United States Bo Patentee before: GUANGZHOU JORBLE BIOTECHNOLOGY Co.,Ltd. |
|
| ASS | Succession or assignment of patent right |
Owner name: GUANGZHOU GREEN VALLEY BIOTECHNOLOGY CO., LTD. Free format text: FORMER OWNER: XIE JUN Effective date: 20110615 |
|
| C41 | Transfer of patent application or patent right or utility model | ||
| COR | Change of bibliographic data |
Free format text: CORRECT: ADDRESS; FROM: 510642 ROOM 505, BUILDING 18, NO. 483, WUSHAN ROAD, TIANHE DISTRICT, GUANGZHOU CITY TO: 510080 ROOM 1905, TOWER 1, DONGJUN PLAZA, NO. 836, DONGFENG EAST ROAD, YUEXIU DISTRICT, GUANGZHOU CITY |
|
| TR01 | Transfer of patent right |
Effective date of registration: 20110615 Address after: Plaza 836 No. 510080 Guangzhou Yuexiu District City Dongfeng Road 1 room 1905 Patentee after: Guangzhou ruigu Biological Technology Co.,Ltd. Address before: 510642, room 18, building 483, No. five, 505 mountain road, Guangzhou, Tianhe District Patentee before: Xie Jun |
|
| ASS | Succession or assignment of patent right |
Owner name: HUAINAN JIARUI BIOTECHNOLOGY LLC Free format text: FORMER OWNER: GUANGZHOU GREEN VALLEY BIOTECHNOLOGY CO., LTD. Effective date: 20150730 |
|
| C41 | Transfer of patent application or patent right or utility model | ||
| TR01 | Transfer of patent right |
Effective date of registration: 20150730 Address after: 232002 Anhui Province, Huainan city tianjia'an District National Road West (Ancheng Economic Development Zone) Patentee after: Huainan Jiarun biotechnology LLC Address before: Plaza No. 836 Guangzhou Yuexiu District City, Guangdong province 510000 Dongfeng East Road 1 room 1905 Patentee before: Guangzhou ruigu Biological Technology Co.,Ltd. |
|
| C56 | Change in the name or address of the patentee | ||
| CP01 | Change in the name or title of a patent holder |
Address after: 232002 Anhui Province, Huainan city tianjia'an District National Road West (Ancheng Economic Development Zone) Patentee after: ANHUI JIARUN BIOTECHNOLOGY CO.,LTD. Address before: 232002 Anhui Province, Huainan city tianjia'an District National Road West (Ancheng Economic Development Zone) Patentee before: Huainan Jiarun biotechnology LLC |
|
| TR01 | Transfer of patent right |
Effective date of registration: 20220216 Address after: 510642 No. five, 483 mountain road, Guangzhou, Guangdong, Tianhe District Patentee after: Xie Jun Address before: 232002 Guoqing West Road, tianjia'an District, Huainan City, Anhui Province Patentee before: ANHUI JIARUN BIOTECHNOLOGY CO.,LTD. |
|
| TR01 | Transfer of patent right | ||
| CX01 | Expiry of patent term |
Granted publication date: 20051109 |
|
| CX01 | Expiry of patent term |