CN111607584A - Method for immobilizing marine cyclodextrin glucosyltransferase by resin - Google Patents
Method for immobilizing marine cyclodextrin glucosyltransferase by resin Download PDFInfo
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- CN111607584A CN111607584A CN202010498247.6A CN202010498247A CN111607584A CN 111607584 A CN111607584 A CN 111607584A CN 202010498247 A CN202010498247 A CN 202010498247A CN 111607584 A CN111607584 A CN 111607584A
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- 239000011347 resin Substances 0.000 title claims abstract description 32
- 229920005989 resin Polymers 0.000 title claims abstract description 32
- 229920000858 Cyclodextrin Polymers 0.000 title claims abstract description 25
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 title claims abstract description 22
- 238000000034 method Methods 0.000 title claims abstract description 21
- 108010055629 Glucosyltransferases Proteins 0.000 title claims abstract description 15
- 102000000340 Glucosyltransferases Human genes 0.000 title claims abstract description 15
- 230000003100 immobilizing effect Effects 0.000 title claims abstract description 10
- 102000004190 Enzymes Human genes 0.000 claims abstract description 57
- 108090000790 Enzymes Proteins 0.000 claims abstract description 57
- 108010025880 Cyclomaltodextrin glucanotransferase Proteins 0.000 claims abstract description 18
- 239000000243 solution Substances 0.000 claims abstract description 16
- 239000007853 buffer solution Substances 0.000 claims abstract description 15
- CIJQGPVMMRXSQW-UHFFFAOYSA-M sodium;2-aminoacetic acid;hydroxide Chemical compound O.[Na+].NCC([O-])=O CIJQGPVMMRXSQW-UHFFFAOYSA-M 0.000 claims abstract description 4
- 238000005303 weighing Methods 0.000 claims abstract description 4
- 238000001914 filtration Methods 0.000 claims description 6
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 6
- 238000005406 washing Methods 0.000 claims description 5
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 claims description 3
- 230000004913 activation Effects 0.000 claims description 3
- 239000008367 deionised water Substances 0.000 claims description 3
- 229910021641 deionized water Inorganic materials 0.000 claims description 3
- 238000004108 freeze drying Methods 0.000 claims description 3
- 238000002791 soaking Methods 0.000 claims description 3
- 238000003756 stirring Methods 0.000 claims description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 3
- 238000004140 cleaning Methods 0.000 claims description 2
- 108010093096 Immobilized Enzymes Proteins 0.000 abstract description 34
- 230000000694 effects Effects 0.000 abstract description 28
- 238000006243 chemical reaction Methods 0.000 abstract description 7
- 238000001179 sorption measurement Methods 0.000 abstract description 4
- 239000002253 acid Substances 0.000 abstract description 3
- 239000003513 alkali Substances 0.000 abstract description 3
- 238000005516 engineering process Methods 0.000 abstract description 3
- 230000014759 maintenance of location Effects 0.000 abstract description 2
- 229940088598 enzyme Drugs 0.000 description 47
- 229910021645 metal ion Inorganic materials 0.000 description 9
- 239000006228 supernatant Substances 0.000 description 5
- 229940097362 cyclodextrins Drugs 0.000 description 3
- 230000007062 hydrolysis Effects 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 238000007363 ring formation reaction Methods 0.000 description 3
- 238000006555 catalytic reaction Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 238000004132 cross linking Methods 0.000 description 2
- 238000007323 disproportionation reaction Methods 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 1
- 102000004139 alpha-Amylases Human genes 0.000 description 1
- 108090000637 alpha-Amylases Proteins 0.000 description 1
- 229940024171 alpha-amylase Drugs 0.000 description 1
- HFHDHCJBZVLPGP-RWMJIURBSA-N alpha-cyclodextrin Chemical compound OC[C@H]([C@H]([C@@H]([C@H]1O)O)O[C@H]2O[C@@H]([C@@H](O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O3)[C@H](O)[C@H]2O)CO)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@@H]3O[C@@H]1CO HFHDHCJBZVLPGP-RWMJIURBSA-N 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- WHGYBXFWUBPSRW-FOUAGVGXSA-N beta-cyclodextrin Chemical compound OC[C@H]([C@H]([C@@H]([C@H]1O)O)O[C@H]2O[C@@H]([C@@H](O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O3)[C@H](O)[C@H]2O)CO)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@@H]3O[C@@H]1CO WHGYBXFWUBPSRW-FOUAGVGXSA-N 0.000 description 1
- 239000011942 biocatalyst Substances 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- GDSRMADSINPKSL-HSEONFRVSA-N gamma-cyclodextrin Chemical compound OC[C@H]([C@H]([C@@H]([C@H]1O)O)O[C@H]2O[C@@H]([C@@H](O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O[C@H]3O[C@H](CO)[C@H]([C@@H]([C@H]3O)O)O3)[C@H](O)[C@H]2O)CO)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@@H]3O[C@@H]1CO GDSRMADSINPKSL-HSEONFRVSA-N 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- -1 i.e. Proteins 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000005918 transglycosylation reaction Methods 0.000 description 1
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/08—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a synthetic polymer
- C12N11/089—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a synthetic polymer obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
- C12N11/091—Phenol resins; Amino resins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
- C12N9/1051—Hexosyltransferases (2.4.1)
- C12N9/1074—Cyclomaltodextrin glucanotransferase (2.4.1.19)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y204/00—Glycosyltransferases (2.4)
- C12Y204/01—Hexosyltransferases (2.4.1)
- C12Y204/01019—Cyclomaltodextrin glucanotransferase (2.4.1.19)
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Abstract
The invention relates to a method for immobilizing marine cyclodextrin glucosyltransferase by resin, which belongs to the technical field of biology and comprises the following steps: weighing activated resin MI-BSI, adding the activated resin MI-BSI into CGTase enzyme solution with the concentration of 0.067mg/mL, preparing the enzyme solution by glycine-sodium hydroxide buffer solution with the pH value of 9, and immobilizing the activated resin MI-BSI and the CGTase enzyme solution for 8 hours in a shaking table with the temperature of 35 ℃ and the rpm of 200, wherein the mass-volume ratio of the activated resin MI-BSI to the CGTase enzyme solution is 10:1 (mg/mL). The invention adopts the immobilization technology of adsorption and covalent bonding method, the reaction condition is mild, the operation is simple, the cost is lower, the thermal stability of the immobilized cyclodextrin glucosyltransferase is better than that of free enzyme, the pH stability is better than that of the free enzyme, the tolerance to acid and alkali is enhanced, the reusability of the immobilized enzyme is good, the immobilized enzyme can be reused for 10 times, and the retention rate of the relative enzyme activity is more than 65%.
Description
Technical Field
The invention belongs to the technical field of biology, and particularly relates to a method for immobilizing marine cyclodextrin glucosyltransferase by resin.
Background
Cyclodextrin glucosyltransferases (CGTase, EC2.4.1.19), which are important members of the alpha-amylase family 13, catalyze four reactions, hydrolysis, cyclization, coupling and disproportionation. Among the four reactions, the cyclization reaction, the disproportionation reaction and the coupling reaction are transglycosylation reactions, and have high activity and low hydrolysis activity, and the control of the hydrolysis activity is favorable for the production of cyclodextrin, wherein the cyclization reaction is a characteristic reaction for producing cyclodextrin, and CGTase is used as a biocatalyst mainly for catalyzing the conversion of starch into cyclodextrin in industry. Cyclodextrins (CD) include primarily alpha-CD, beta-CD, and gamma-CD. The cyclodextrin is a molecule with a cylindrical structure, and based on the special structure that the interior of the cyclodextrin is hydrophobic and the exterior of the cyclodextrin is hydrophilic, the cyclodextrin and the derivatives thereof have great application prospects in the food industry, the biotechnology, the pharmaceutical industry, the cosmetics industry, the chemical industry and other aspects. Therefore, there is also an increasing research on CGTase required for the production of cyclodextrins.
The immobilized enzyme is a new technology developed in the sixties of the twentieth century. The localization and restriction of immobilized enzymes, i.e., enzymes, means that free enzymes are bound or restricted in a certain region by binding the free enzymes to a carrier, and the free enzymes cannot move freely but can still perform their specific catalytic reactions. After the enzyme is immobilized, the enzyme is easy to separate from a product and a substrate, can be effectively recovered and reused, and has enhanced thermal stability and operation stability compared with free enzyme. The traditional immobilization method mainly comprises an adsorption method, an embedding method, a cross-linking method, a covalent bonding method and the like, wherein the binding force between an enzyme and a carrier in the adsorption method is not strong, and the enzyme molecules are easy to separate from the carrier; the enzyme liquid in the embedding method is easy to run off and is not easy to catalyze macromolecular substrates; cross-linking methods are generally used in combination with other methods; in the covalent binding method, the enzyme is firmly bound with the carrier, but the enzyme activity is influenced due to the fierce immobilization condition.
Disclosure of Invention
The invention aims to provide a method for immobilizing marine cyclodextrin glucosyltransferase by a covalent bonding method, which has the characteristics of simple operation, low cost, good immobilized enzyme stability, reusability and the like.
The invention is realized by the following technical scheme:
a method for immobilizing marine cyclodextrin glucosyltransferase by resin comprises the following specific steps:
(1) the carrier activation selects amino functional resin MI-BSI as a carrier, and the carrier is activated by the following steps before immobilization: adding 0.1M PBS buffer solution with pH8.0 into the carrier, soaking and cleaning for 1h, filtering and draining, wherein the mass-volume ratio of the carrier to the PBS buffer solution is 1:4(g/ml), adding equal volume of 0.1M PBS buffer solution with pH8.0 and containing 2% glutaraldehyde, slowly stirring for 1h at 25 ℃, filtering, washing the carrier for 3-5 times by deionized water, and freeze-drying to obtain an activated carrier;
(2) accurately weighing activated resin MI-BSI, adding the resin MI-BSI into CGTase enzyme solution with the concentration of 0.067mg/mL, preparing the enzyme solution by glycine-sodium hydroxide buffer solution with the pH value of 9, and immobilizing the resin MI-BSI and the CGTase enzyme solution for 8 hours in a shaking table at the temperature of 35 ℃ and the rpm of 200, wherein the mass-to-volume ratio of the activated resin MI-BSI to the CGTase enzyme solution is 10:1 (mg/mL).
The marine microorganism cyclodextrin glucosyltransferase is prepared from marine product resources of yellow sea aquatic research institute and enzyme laboratories.
Compared with the prior art, the invention has the beneficial effects that:
1. the amino functional resin provided by the invention has the advantages of amino functional groups and the like, and is widely applied to the research in the field of biotechnology.
2. The invention adopts the immobilization technology of adsorption and covalent bonding method, has mild reaction condition, simple operation and lower cost
3. The heat stability of the immobilized cyclodextrin glucosyltransferase is superior to that of free enzyme, the pH stability is superior to that of the free enzyme, the tolerance to acid and alkali is enhanced, the reusability of the immobilized enzyme is good, the immobilized enzyme is reused for 10 times, and the retention rate of the relative enzyme activity is over 65 percent.
Drawings
FIG. 1: pH stability of immobilized enzyme
FIG. 2: metal ion tolerance of immobilized enzyme
FIG. 3: stability of operation of immobilized enzyme
Detailed Description
The technical solutions of the present invention are further illustrated by the following examples, but the scope of the present invention is not limited by the examples in any way. And are not limited to the following examples:
example 1
A method for immobilizing marine cyclodextrin glucosyltransferase by resin specifically comprises the following steps:
(1) screening immobilized carriers, respectively weighing certain resins, treating the resins before immobilization, adding CGTase enzyme solution with certain enzyme protein concentration, and shaking and fixing for a certain time. After the immobilization is finished, separating the resin of the immobilized enzyme from the supernatant, washing the resin and the supernatant for multiple times by using a buffer solution until the content of the enzyme protein in the supernatant is zero, and measuring the influence of different resins on the recovery rate of the enzyme activity and the protein immobilization rate. Screening resin with highest enzyme activity recovery rate and protein immobilization rate as immobilized carrier (resin including MA-WP8, MA-P9, MI-BSI, MC-300EP, MI-BN4, LX-1000EP and LX-1000 HA);
(2) activation of the carrier: adding 40ml of 0.1M PBS (pH 8.0) buffer solution into 10g of carrier, soaking and washing for 1h, filtering and draining, adding 0.1M PBS (pH 8.0) buffer solution containing 40ml of 2% glutaraldehyde, slowly stirring for 1h at 25 ℃, filtering, washing the carrier with deionized water for 3-5 times, and freeze-drying to obtain the activated carrier. (3) 10mg of activated amino functional resin was weighed out accurately, 1mL of CGTase enzyme solution with an enzyme protein concentration of 0.067mg/mL was added, and the mixture was fixed in a shaker at 35 ℃ and 200rpm for 8 hours. After the immobilization is finished, the immobilized CGTase is separated from the supernatant, the CGTase is repeatedly washed by glycine-sodium hydroxide buffer solution until the content of enzyme protein in the supernatant is zero, and the enzyme activity recovery rate and the protein immobilization rate of the immobilized enzyme are analyzed.
The marine microorganism cyclodextrin glucosyltransferase is prepared from marine product resources of yellow sea aquatic research institute and enzyme laboratory laboratories
Example 2 pH stability of immobilized enzyme
Respectively placing free enzyme and immobilized enzyme in buffer solutions with pH of 4, 5, 6, 7, 8, 9, 10, 11, and 12, treating for 2h, measuring enzyme activity, and exploring influence of pH on immobilized enzyme and free enzyme activity with highest enzyme activity of 100%
And (3) placing the free enzyme and the immobilized enzyme under the condition of pH 4-12 to act for 2h, measuring the enzyme activity and researching the influence of pH on the enzyme activity. As shown in FIG. 1, the results of the catalytic performance showed that the enzyme activities of the immobilized enzyme and the free enzyme increased with increasing pH at pH 4-9, and decreased with increasing pH at pH 9-12. However, under the same pH condition, the relative enzyme activity of the immobilized enzyme is higher than that of the free enzyme, which shows that after the CGTase is immobilized by a resin MI-BSI carrier, the immobilized enzyme has higher tolerance to acid and alkali than the free enzyme.
Example 3 tolerance of immobilized enzymes to Metal ions
Adding K into free enzyme and immobilized enzyme respectively+、Ca2+、Mn2+、Ba2+、Fe2+、Fe3+、Al3+、Cu2+、Mg2+Waiting 9 metal ions to ensure that the final concentration of the solution is 5mmol/L, then processing for 2h, measuring the enzyme activity, and exploring the influence of the metal ions on the activity of the immobilized enzyme and the free enzyme by taking the highest enzyme activity as 100 percent
Placing the free enzyme and the immobilized enzyme in solutions of different metal ions for acting for 2h, measuring the enzyme activity and researching the influence of different metal ions on the enzyme activity. As shown in FIG. 2, after different metal ions are treated, the enzyme activities of free enzyme and immobilized enzyme are changed, except for Mg2+In addition, the immobilized enzymes have stronger tolerance to metal ions than free enzymes. By metal ions Al3+、Fe2 +、Fe3+After treatment, the activity of the CGTase is obviously inhibited.
Example 4 operational stability of immobilized enzymes
After a certain amount of immobilized enzyme is reacted, the immobilized enzyme is magnetically adsorbed, the immobilized enzyme is washed for a plurality of times by using buffer solution, the enzyme activity of the immobilized enzyme is continuously measured, the enzyme activity measured for the first time is 100 percent, the immobilized enzyme is washed and used for the catalytic reaction of the next batch, the reaction is continuously carried out for 5 times, the residual enzyme activity of the immobilized enzyme is measured, and the operation stability of the immobilized enzyme is researched.
After the resin MI-BSI immobilized marine cyclodextrin glucosyltransferase is repeatedly used for 10 times, as shown in figure 3, the relative enzyme activity of the amino functional resin MI-BSI immobilized marine cyclodextrin glucosyltransferase is still kept at 68.2 percent, which shows that the resin MI-BSI carrier immobilized CGTase has a good combination effect, and the immobilized enzyme has good operation stability.
Claims (1)
1. A method for immobilizing marine cyclodextrin glucosyltransferase is characterized by comprising the following steps:
(1) the carrier activation selects amino functional resin MI-BSI as a carrier, and the carrier is activated by the following steps before immobilization: adding 0.1M PBS buffer solution with the pH value of 8.0 into the carrier, soaking and cleaning for 1h, filtering and draining, wherein the mass-volume ratio of the carrier to the PBS buffer solution is 1:4, the unit of the proportion is g/ml, adding equal volume of 0.1M PBS buffer solution with the pH value of 8.0 and containing 2% glutaraldehyde, slowly stirring for 1h at 25 ℃, filtering, washing the carrier for 3-5 times by using deionized water, and freeze-drying to obtain an activated carrier;
(2) accurately weighing activated resin MI-BSI, adding the resin MI-BSI into CGTase enzyme solution with the concentration of 0.067mg/mL, preparing the enzyme solution by glycine-sodium hydroxide buffer solution with the pH value of 9, fixing the activated resin MI-BSI and the CGTase enzyme solution for 8 hours in a shaking table with the temperature of 35 ℃ and the rpm of 10: 1.
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112048498A (en) * | 2020-09-14 | 2020-12-08 | 江苏省奥谷生物科技有限公司 | Preparation method for improving yield of beta-cyclodextrin |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108977430A (en) * | 2018-09-14 | 2018-12-11 | 中国水产科学研究院黄海水产研究所 | A kind of process for fixation of marine microorganism cyclodextrin glycosyltransferase |
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Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN108977430A (en) * | 2018-09-14 | 2018-12-11 | 中国水产科学研究院黄海水产研究所 | A kind of process for fixation of marine microorganism cyclodextrin glycosyltransferase |
Non-Patent Citations (5)
| Title |
|---|
| JÉSSIE DA NATIVIDADE SCHÖFFER等: "Directed immobilization of CGTase: The effect of the enzyme orientation on the enzyme activity and its use in packed-bed reactor for continuous production of cyclodextrins", 《PROCESS BIOCHEMISTRY》 * |
| 刘桂林: "《生物技术概论》", 30 September 2010, 中国农业大学出版社 * |
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| 郭姣梅: "海洋环糊精葡萄糖基转移酶的固定化及其性能研究", 《硕士中国优秀硕士学位论文全文数据库 工程科技Ⅰ辑》 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112048498A (en) * | 2020-09-14 | 2020-12-08 | 江苏省奥谷生物科技有限公司 | Preparation method for improving yield of beta-cyclodextrin |
| CN112048498B (en) * | 2020-09-14 | 2023-10-03 | 江苏省奥谷生物科技有限公司 | Preparation method for improving beta-cyclodextrin yield |
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