CN112321692A - Method for diluting renaturation of soybean 11S globulin guanidine hydrochloride after denaturation treatment - Google Patents
Method for diluting renaturation of soybean 11S globulin guanidine hydrochloride after denaturation treatment Download PDFInfo
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- CN112321692A CN112321692A CN202011278510.7A CN202011278510A CN112321692A CN 112321692 A CN112321692 A CN 112321692A CN 202011278510 A CN202011278510 A CN 202011278510A CN 112321692 A CN112321692 A CN 112321692A
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- soybean
- guanidine hydrochloride
- globulin
- renaturation
- protein
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- 229960000789 guanidine hydrochloride Drugs 0.000 title claims abstract description 53
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 title claims abstract description 53
- 235000010469 Glycine max Nutrition 0.000 title claims abstract description 46
- 244000068988 Glycine max Species 0.000 title claims abstract description 44
- 238000004153 renaturation Methods 0.000 title claims abstract description 42
- 101710102211 11S globulin Proteins 0.000 title claims abstract description 38
- 101710190853 Cruciferin Proteins 0.000 title claims abstract description 38
- 238000000034 method Methods 0.000 title claims abstract description 32
- 238000004925 denaturation Methods 0.000 title claims abstract description 31
- 230000036425 denaturation Effects 0.000 title claims abstract description 31
- 238000007865 diluting Methods 0.000 title claims abstract description 16
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 42
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 42
- 239000012460 protein solution Substances 0.000 claims abstract description 40
- 239000000843 powder Substances 0.000 claims abstract description 14
- 238000004108 freeze drying Methods 0.000 claims abstract description 11
- 239000000872 buffer Substances 0.000 claims abstract description 4
- 239000007853 buffer solution Substances 0.000 claims description 11
- 238000010790 dilution Methods 0.000 claims description 10
- 239000012895 dilution Substances 0.000 claims description 10
- 238000003756 stirring Methods 0.000 claims description 9
- 239000000243 solution Substances 0.000 claims description 6
- 238000002156 mixing Methods 0.000 claims description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims 1
- 238000012792 lyophilization process Methods 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 abstract description 40
- 239000003398 denaturant Substances 0.000 abstract description 13
- 108010073771 Soybean Proteins Proteins 0.000 abstract description 11
- 235000019710 soybean protein Nutrition 0.000 abstract description 11
- 239000000853 adhesive Substances 0.000 abstract description 4
- 230000001070 adhesive effect Effects 0.000 abstract description 4
- 238000011161 development Methods 0.000 abstract description 3
- 239000002245 particle Substances 0.000 description 18
- 238000001514 detection method Methods 0.000 description 9
- 238000002983 circular dichroism Methods 0.000 description 7
- 150000002333 glycines Chemical class 0.000 description 7
- 238000000227 grinding Methods 0.000 description 7
- 239000007788 liquid Substances 0.000 description 7
- 210000000582 semen Anatomy 0.000 description 7
- 238000007873 sieving Methods 0.000 description 7
- 238000004587 chromatography analysis Methods 0.000 description 6
- 238000003760 magnetic stirring Methods 0.000 description 5
- 239000008055 phosphate buffer solution Substances 0.000 description 3
- 238000013459 approach Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 125000001841 imino group Chemical group [H]N=* 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
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Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
Abstract
The invention discloses a method for diluting renaturation of soybean 11S globulin guanidine hydrochloride after denaturation treatment, belonging to the technical field of renaturation of protein. The method provided by the invention specifically comprises the following steps: the method comprises the following steps: extracting soybean 11S globulin, and freeze-drying; step two: carrying out denaturation treatment on the freeze-dried soybean 11S protein powder by using guanidine hydrochloride to obtain a denatured protein solution; step three: the denatured protein solution was diluted with PBS buffer so that the concentration of the denaturant was reduced and the protein renaturation occurred. The method provided by the invention is simple and stable, has great significance for improving the utilization value of the soybean protein, and provides support and help for the development and utilization of the soybean protein adhesive.
Description
Technical Field
The invention relates to a method for diluting renaturation of soybean 11S globulin guanidine hydrochloride after denaturation treatment, belonging to the technical field of renaturation of protein.
Background
The protein can be denatured under the treatment conditions of heat, high pressure, and the addition of some chemical reagents, etc., thereby causing partial loss of biological activity, for reversibly denatured proteins, when the degree of denaturation is small, if the denaturation factors are removed or the environment where the proteins are located is changed, the denatured proteins can partially or completely restore the original conformation and function, the current methods for studying protein denaturation include changing the pH value, heating, adding denaturants (such as guanidine hydrochloride and urea), etc., the protein structure commonly used for renaturation study is simple, and bovine serum albumin, lysozyme, alkaline phosphatase, etc. are common. The renaturation phenomenon of soybean protein is only studied, so that a method for diluting renaturation after the guanidine hydrochloride denaturation treatment of soybean 11S globulin is very necessary.
Disclosure of Invention
The invention aims to provide a method for diluting and renaturing the denatured soybean 11S globulin guanidine hydrochloride, which is simple to operate and high in efficiency.
A method for diluting and renaturing soybean 11S globulin guanidine hydrochloride after denaturation treatment comprises the following steps:
step one, performing freeze drying treatment on soybean 11S globulin to obtain soybean 11S globulin powder;
secondly, performing denaturation treatment on the soybean 11S globulin powder treated in the step one by using a guanidine hydrochloride solution to obtain a denatured protein solution;
and step three, diluting the denatured protein solution by using a PBS buffer solution, and performing renaturation treatment on the denatured protein solution to obtain renaturated protein solution.
Further, the conditions of the freeze-drying treatment in the first step are as follows: the treatment temperature is-45 ℃ and the treatment time is 24 h.
Further, the concentration of the guanidine hydrochloride solution in the second step is 8 mol/L.
Further, the concentration of the denatured protein solution obtained in the second step is 1 mg/mL-20 mg/mL.
Further, in the second step, the condition of the denaturation processing is as follows: mixing soybean 11S globulin powder and guanidine hydrochloride solution, magnetically stirring for 30min, and standing at 25 deg.C for 8 hr.
Further, in step three, the PBS buffer solution is 0.01mol/L, and the pH value is 7.0 phosphate buffer solution.
Further, the concentration of guanidine hydrochloride in the renaturation protein liquid obtained in the third step is 0.4-8 mol/L.
Further, the concentration of the protein in the renaturation protein solution obtained in the third step is 1 mg/mL.
Further, the renaturation treatment conditions in the third step are as follows: the denatured protein solution was mixed with PBS buffer, magnetically stirred for 30min, and then allowed to stand at 25 ℃ for 12 hours.
Further, the viscosity of the renaturation protein liquid obtained in the third step is 87 mPa.s.
The invention has the following beneficial effects: the method adopts guanidine hydrochloride to denature the soybean 11S globulin, after the soybean 11S globulin is diluted and renatured by PBS buffer solution, the tertiary structure of part of the secondary structure is recovered, the viscosity of the soybean 11S globulin is greatly improved, the method is simple and stable, has great significance for improving the utilization value of the soybean protein, and provides support and help for the development, development and utilization of the soybean protein adhesive.
Drawings
FIG. 1 is a graph of the secondary structure of soy 11S globulin in renaturation protein solutions containing various concentrations of guanidine hydrochloride prepared in examples 1 to 7;
FIG. 2 is a graph showing the tertiary structure of soy 11S globulin in renaturation protein solutions containing various concentrations of guanidine hydrochloride prepared in examples 1 to 7;
FIG. 3 is a graph showing the viscosity of renaturation protein solutions containing different guanidine hydrochloride concentrations prepared in examples 1 to 7.
Detailed Description
The experimental procedures used in the following examples are conventional unless otherwise specified. The materials, reagents, methods and apparatus used, unless otherwise specified, are conventional in the art and are commercially available to those skilled in the art.
Example 1:
the method comprises the following steps: grinding semen glycines, sieving, defatting, extracting soybean 11S globulin, and freeze drying.
Step two: carrying out denaturation treatment on the freeze-dried soybean 11S protein powder by using 8M guanidine hydrochloride, magnetically stirring for 30min, and standing at 25 ℃ for 8 hours to obtain a completely denatured protein solution, wherein the concentration of the guanidine hydrochloride is 8M, and the concentration of the soybean protein is 1 mg/mL.
The obtained completely denatured protein solution was subjected to secondary and tertiary structure detection by circular dichroism chromatography, particle size detection by a particle size analyzer, and viscosity detection by a viscometer, and the results are shown in fig. 1, fig. 2, fig. 3, and table 1.
Example 2:
the method comprises the following steps: grinding semen glycines, sieving, defatting, extracting soybean 11S globulin, and freeze drying.
Step two: and (3) carrying out denaturation treatment on the freeze-dried soybean 11S protein powder by using 8M guanidine hydrochloride, carrying out magnetic stirring for 30min, and standing at 25 ℃ for 8 hours to obtain a denatured protein solution, wherein the concentration of the soybean protein is 2 mg/mL.
Step three: diluting the denatured protein solution with PBS buffer solution of 0.01M and pH7.0 to reduce the concentration of denaturant guanidine hydrochloride to obtain renaturated protein solution, wherein the concentration of guanidine hydrochloride is reduced to 4M, the protein concentration is 1mg/mL, magnetically stirring is carried out for 30min, the renaturation temperature is 25 ℃, and the time is 12 h.
The obtained renaturation protein liquid is subjected to secondary structure and tertiary structure detection by adopting a circular dichroism chromatography, the particle size is detected by a particle size analyzer, the viscosity is detected by a viscosity analyzer, and the results are shown in figure 1, figure 2, figure 3 and table 1.
Example 3:
the method comprises the following steps: grinding semen glycines, sieving, defatting, extracting soybean 11S globulin, and freeze drying.
Step two: and (3) carrying out denaturation treatment on the freeze-dried soybean 11S protein powder by using 8M guanidine hydrochloride, carrying out magnetic stirring for 30min, and standing at 25 ℃ for 8 hours to obtain a denatured protein solution, wherein the concentration of the soybean protein is 4 mg/mL.
Step three: diluting the denatured protein solution with PBS buffer solution of 0.01M and pH7.0 to reduce the concentration of denaturant guanidine hydrochloride to obtain renaturated protein solution, wherein the concentration of guanidine hydrochloride denaturant is reduced to 2M, the protein concentration is 1mg/mL, magnetically stirring is carried out for 30min, the renaturation temperature is 25 ℃, and the time is 12 h.
The obtained renaturation protein liquid is subjected to secondary structure and tertiary structure detection by adopting a circular dichroism chromatography, the particle size is detected by a particle size analyzer, the viscosity is detected by a viscosity analyzer, and the results are shown in figure 1, figure 2, figure 3 and table 1.
Example 4:
the method comprises the following steps: grinding semen glycines, sieving, defatting, extracting soybean 11S globulin, and freeze drying.
Step two: and (3) carrying out denaturation treatment on the freeze-dried soybean 11S protein powder by using 8M guanidine hydrochloride, carrying out magnetic stirring for 30min, and standing at 25 ℃ for 8 hours to obtain a denatured protein solution, wherein the concentration of the soybean protein is 8 mg/mL.
Step three: diluting the denatured protein solution with PBS buffer solution of 0.01M and pH7.0 to reduce the concentration of denaturant guanidine hydrochloride to obtain renaturated protein solution, wherein the concentration of denaturant guanidine hydrochloride is reduced to 1M, the protein concentration is 1mg/mL, magnetically stirring is carried out for 30min, the renaturation temperature is 25 ℃, and the time is 12 h.
The obtained renaturation protein liquid is subjected to secondary structure and tertiary structure detection by adopting a circular dichroism chromatography, the particle size is detected by a particle size analyzer, the viscosity is detected by a viscosity analyzer, and the results are shown in figure 1, figure 2, figure 3 and table 1.
Example 5:
the method comprises the following steps: grinding semen glycines, sieving, defatting, extracting soybean 11S globulin, and freeze drying.
Step two: and (3) carrying out denaturation treatment on the freeze-dried soybean 11S protein powder by using 8M guanidine hydrochloride, carrying out magnetic stirring for 30min, and standing at 25 ℃ for 8 hours to obtain a denatured protein solution, wherein the concentration of the soybean protein is 10 mg/mL.
Step three: diluting the denatured protein solution with PBS buffer solution of 0.01M and pH7.0 to reduce the concentration of denaturant guanidine hydrochloride to obtain renaturated protein solution, wherein the concentration of denaturant guanidine hydrochloride is reduced to 0.8M, the concentration of protein is 1mg/mL, magnetically stirring is carried out for 30min, the renaturation temperature is 25 ℃, and the time is 12 h.
The obtained renaturation protein liquid is subjected to secondary structure and tertiary structure detection by adopting a circular dichroism chromatography, the particle size is detected by a particle size analyzer, the viscosity is detected by a viscosity analyzer, and the results are shown in figure 1, figure 2, figure 3 and table 1.
Example 6:
the method comprises the following steps: grinding semen glycines, sieving, defatting, extracting soybean 11S globulin, and freeze drying.
Step two: and (3) carrying out denaturation treatment on the freeze-dried soybean 11S protein powder by using 8M guanidine hydrochloride, carrying out magnetic stirring for 30min, and standing at 25 ℃ for 8 hours to obtain a denatured protein solution, wherein the concentration of the soybean protein is 20 mg/mL.
Step three: diluting the denatured protein solution with PBS buffer solution of 0.01M and pH7.0 to reduce the concentration of denaturant guanidine hydrochloride to obtain renaturated protein solution, wherein the concentration of denaturant guanidine hydrochloride is reduced to 0.4M, the concentration of protein is 1mg/mL, magnetically stirring is carried out for 30min, the renaturation temperature is 25 ℃, and the time is 12 h.
The obtained renaturation protein liquid is subjected to secondary structure and tertiary structure detection by adopting a circular dichroism chromatography, the particle size is detected by a particle size analyzer, the viscosity is detected by a viscosity analyzer, and the results are shown in figure 1, figure 2, figure 3 and table 1.
Example 7:
the method comprises the following steps: grinding semen glycines, sieving, defatting, extracting soybean 11S globulin, and freeze drying.
Step two: dissolving the freeze-dried soybean 11S protein powder with PBS buffer solution of 0.01M and pH7.0, wherein the protein concentration is 1mg/mL, the guanidine hydrochloride concentration is 0M, and magnetically stirring for 30min to obtain a natural protein solution.
The obtained natural protein solution is subjected to secondary structure and tertiary structure detection by a circular dichroism method, the particle size is detected by a particle size analyzer, the viscosity is detected by a viscosity analyzer, and the results are shown in fig. 1, fig. 2, fig. 3 and table 1.
And (4) analyzing results:
the data in table 1 are as follows:
TABLE 1
| Example final concentration of guanidine hydrochloride | Z-Ave (nm) PBS buffer | Pdi (< 0.7 good) | |
| Example 1 | 8M (completely changing behavior) | 201.3±1.93 | 0.333 |
| Example 2 | 4M | 159.7±2.09 | 0.577 |
| Example 3 | 2M | 140.8±0.95 | 0.644 |
| Example 4 | 1M | 104.8±2.34 | 0.586 |
| Example 5 | 0.8M | 96.06±1.19 | 0.498 |
| Example 6 | 0.4M | 95.06±0.92 | 0.378 |
| Example 7 | 0M (Natural state) | 67.32±0.62 | 0.478 |
As can be seen from Table 1, the particle size of the natural 11S is 67.32nm, and the particle size is increased to 201.3nm after denaturation by 8M GuHCl; from FIG. 1, it can be seen that the protein has lost its tertiary structure at this time, and FIG. 2 shows that the secondary structure of the protein is almost completely lost at this time, because GuHCl can form hydrogen bonds with side chains of various polar amino acids in the protein and carbonyl and imino groups in peptide bonds, thereby changing the hydrogen bond structure inside the native protein to loosen the peptide chain.
Diluting the denatured 11S by phosphate buffer solution, and from the experimental result of particle size, it can be easily seen that the particle size of protein is gradually reduced along with the reduction of GuHCl concentration, and approaches to the natural state, the near ultraviolet result shows that when the concentration of guanidine hydrochloride is reduced to 1M, the positive peak at 284nm begins to be gradually increased, along with the addition of phosphate buffer solution, the concentration of GuHCl is continuously reduced, and when the concentration of GuHCl is 0.4M, the positive peak at 284nm is already very close to the natural state; the far-ultraviolet results show that as the concentration of the denaturant is reduced, the negative peak in the protein spectrum begins to shift to lower wavelengths, and when the concentration of guanidine hydrochloride is reduced to 0.4, the change is no longer obvious, and at the moment, partial beta-folding and alpha-helix of the protein are gradually recovered, the structure of the protein becomes more ordered and gradually approaches to the natural state, but partial secondary structure is still lost compared with the natural state. This is because the developed protein peptide chain undergoes renaturation by dilution due to a decrease in the concentration of the denaturant in the environment.
As can be seen from FIG. 3, when the diluted concentration of guanidine hydrochloride is 4M, the viscosity is highest and reaches 87mPa.s, which is caused by the increase of surface charge, the increase of intermolecular repulsion and the loose molecular structure of protein, while the viscosity of the general adhesive is in the range of 85-115 mPa.s. Therefore, it is considered to be applied to an adhesive and the like in industrial production.
Claims (10)
1. A method for diluting and renaturing soybean 11S globulin guanidine hydrochloride after denaturation treatment is characterized by comprising the following steps:
step one, performing freeze drying treatment on soybean 11S globulin to obtain soybean 11S globulin powder;
secondly, performing denaturation treatment on the soybean 11S globulin powder treated in the step one by using a guanidine hydrochloride solution to obtain a denatured protein solution;
and step three, diluting the denatured protein solution by using a PBS buffer solution, and performing renaturation treatment on the denatured protein solution to obtain renaturated protein solution.
2. The method for dilution renaturation of soybean 11S globulin after guanidine hydrochloride denaturation treatment as claimed in claim 1, wherein said lyophilization process conditions in step one are as follows: the treatment temperature is-45 ℃ and the treatment time is 24 h.
3. The method for dilution renaturation of soybean 11S globulin after guanidine hydrochloride denaturation treatment according to claim 1, wherein the concentration of guanidine hydrochloride solution in the second step is 8 mol/L.
4. The method for dilution renaturation of soybean 11S globulin hydrochloride after guanidine hydrochloride denaturation treatment according to claim 1, characterized in that the concentration of the denatured protein solution obtained in the second step is 1 mg/mL-20 mg/mL.
5. The method for dilution renaturation of soybean 11S globulin after guanidine hydrochloride denaturation treatment as claimed in claim 1, wherein said denaturation treatment conditions in step two are as follows: mixing soybean 11S globulin powder and guanidine hydrochloride solution, magnetically stirring for 30min, and standing at 25 deg.C for 8 hr.
6. The method for performing dilution renaturation after guanidine hydrochloride denaturation treatment on soybean 11S globulin according to claim 1, wherein the PBS buffer solution in the third step is 0.01mol/L and the pH value is 7.0.
7. The method for dilution renaturation of the soybean 11S globulin guanidine hydrochloride after the denaturation treatment according to claim 1, wherein the concentration of guanidine hydrochloride in the renaturation protein solution obtained in the third step is 0.4-8 mol/L.
8. The method for dilution renaturation after guanidine hydrochloride denaturation treatment of soybean 11S globulin according to claim 1, characterized in that the protein concentration in the renaturation protein solution obtained in the third step is 1 mg/mL.
9. The method for dilution renaturation of soybean 11S globulin after guanidine hydrochloride denaturation treatment according to claim 1, characterized in that the renaturation treatment conditions in the third step are as follows: the denatured protein solution was mixed with PBS buffer, magnetically stirred for 30min, and then allowed to stand at 25 ℃ for 12 hours.
10. The method for dilution renaturation of soybean 11S globulin after guanidine hydrochloride denaturation treatment according to claim 1, characterized in that the viscosity of the renaturated protein solution obtained in the third step is 87 mPa.s.
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Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
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| CN1683389A (en) * | 2005-03-14 | 2005-10-19 | 东华大学 | Soybean protein solution and its preparing method |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1683389A (en) * | 2005-03-14 | 2005-10-19 | 东华大学 | Soybean protein solution and its preparing method |
Non-Patent Citations (7)
| Title |
|---|
| 叶为标: "化学改性大豆蛋白木材胶粘剂研究进展", 《粮食与油脂》 * |
| 尹翠玉等: "脲变性大豆蛋白的流变学特性研究", 《大豆科学》 * |
| 张忠慧: "尿素变性大豆蛋白的分子结构及胶粘机理研究", 《中国博士学位论文全文数据库 工程科技Ⅰ辑》 * |
| 朱娴等: "大豆蛋白胶粘剂的改性研究进展", 《中国胶黏剂》 * |
| 栾建美等: "大豆蛋白作为胶粘剂应用的研究进展", 《中国油脂》 * |
| 洪庆慈等: "大豆蛋白改性和黏合性研究", 《中国油脂》 * |
| 邹灵等: "磷酸盐缓冲溶液对变性大豆11S球蛋白构象的影响", 《中国食品科学技术学会第十七届年会摘要集》 * |
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Application publication date: 20210205 |