CN114231521B - Preparation method and application of modified attapulgite immobilized enzyme - Google Patents
Preparation method and application of modified attapulgite immobilized enzyme Download PDFInfo
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- CN114231521B CN114231521B CN202111532423.4A CN202111532423A CN114231521B CN 114231521 B CN114231521 B CN 114231521B CN 202111532423 A CN202111532423 A CN 202111532423A CN 114231521 B CN114231521 B CN 114231521B
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- 229960000892 attapulgite Drugs 0.000 title claims abstract description 71
- 229910052625 palygorskite Inorganic materials 0.000 title claims abstract description 71
- 108010093096 Immobilized Enzymes Proteins 0.000 title claims abstract description 35
- 238000002360 preparation method Methods 0.000 title claims abstract description 10
- ULGZDMOVFRHVEP-RWJQBGPGSA-N Erythromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)C(=O)[C@H](C)C[C@@](C)(O)[C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 ULGZDMOVFRHVEP-RWJQBGPGSA-N 0.000 claims abstract description 60
- 229960003276 erythromycin Drugs 0.000 claims abstract description 30
- 239000000243 solution Substances 0.000 claims abstract description 22
- 108090000790 Enzymes Proteins 0.000 claims abstract description 21
- 230000000593 degrading effect Effects 0.000 claims abstract description 13
- 239000000463 material Substances 0.000 claims abstract description 13
- 238000003756 stirring Methods 0.000 claims abstract description 12
- 239000010865 sewage Substances 0.000 claims abstract description 8
- 241000233866 Fungi Species 0.000 claims abstract description 6
- 238000004108 freeze drying Methods 0.000 claims abstract description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 6
- 239000008055 phosphate buffer solution Substances 0.000 claims abstract description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 16
- 238000001035 drying Methods 0.000 claims description 7
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 claims description 5
- 230000001580 bacterial effect Effects 0.000 claims description 5
- 230000001105 regulatory effect Effects 0.000 claims description 5
- 238000005406 washing Methods 0.000 claims description 5
- 239000002253 acid Substances 0.000 claims description 4
- 230000007935 neutral effect Effects 0.000 claims description 3
- 238000001914 filtration Methods 0.000 claims description 2
- 238000007873 sieving Methods 0.000 claims description 2
- 239000004927 clay Substances 0.000 claims 2
- 238000012986 modification Methods 0.000 claims 1
- 230000004048 modification Effects 0.000 claims 1
- 238000000643 oven drying Methods 0.000 claims 1
- 102000004190 Enzymes Human genes 0.000 abstract description 20
- 230000009286 beneficial effect Effects 0.000 abstract description 2
- 230000003321 amplification Effects 0.000 abstract 1
- 238000003199 nucleic acid amplification method Methods 0.000 abstract 1
- 230000015556 catabolic process Effects 0.000 description 11
- 238000006731 degradation reaction Methods 0.000 description 11
- 101100279950 Escherichia coli ereB gene Proteins 0.000 description 6
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 6
- 108090000623 proteins and genes Proteins 0.000 description 6
- 238000000034 method Methods 0.000 description 5
- 230000000694 effects Effects 0.000 description 4
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 230000003115 biocidal effect Effects 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 2
- PXHVJJICTQNCMI-UHFFFAOYSA-N Nickel Chemical compound [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 238000006555 catalytic reaction Methods 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 230000035899 viability Effects 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 239000006087 Silane Coupling Agent Substances 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000003912 environmental pollution Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000002715 modification method Methods 0.000 description 1
- 229910052759 nickel Inorganic materials 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229910021642 ultra pure water Inorganic materials 0.000 description 1
- 239000012498 ultrapure water Substances 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 239000002351 wastewater Substances 0.000 description 1
Classifications
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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
- C12N11/14—Enzymes or microbial cells immobilised on or in an inorganic carrier
-
- C—CHEMISTRY; METALLURGY
- C02—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
- C02F—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
- C02F3/00—Biological treatment of water, waste water, or sewage
- C02F3/34—Biological treatment of water, waste water, or sewage characterised by the microorganisms used
- C02F3/342—Biological treatment of water, waste water, or sewage characterised by the microorganisms used characterised by the enzymes used
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
-
- C—CHEMISTRY; METALLURGY
- C02—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
- C02F—TREATMENT OF WATER, WASTE WATER, SEWAGE, OR SLUDGE
- C02F2101/00—Nature of the contaminant
- C02F2101/30—Organic compounds
- C02F2101/34—Organic compounds containing oxygen
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02W—CLIMATE CHANGE MITIGATION TECHNOLOGIES RELATED TO WASTEWATER TREATMENT OR WASTE MANAGEMENT
- Y02W10/00—Technologies for wastewater treatment
- Y02W10/10—Biological treatment of water, waste water, or sewage
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- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Microbiology (AREA)
- Genetics & Genomics (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biodiversity & Conservation Biology (AREA)
- Inorganic Chemistry (AREA)
- Hydrology & Water Resources (AREA)
- Environmental & Geological Engineering (AREA)
- Water Supply & Treatment (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Abstract
The invention relates to a modified attapulgite immobilized enzyme, a preparation method and application thereof, belonging to the technical field of material and bioengineering intersection. The preparation method of the modified attapulgite immobilized enzyme comprises the following steps: firstly modifying the modified attapulgite, then dissolving erythromycin degrading enzyme and the modified attapulgite in phosphate buffer solution according to a certain proportion, adjusting the pH value of the solution to be 6.0-8.0, stirring for 3-4 hours at 20-30 ℃, and freeze-drying to obtain the modified attapulgite immobilized enzyme. The modified attapulgite immobilized enzyme has remarkable stability and recoverability, can effectively degrade fungus residues containing erythromycin, sewage and water in the environment, and is beneficial to the amplification application in industrialization.
Description
Technical Field
The invention relates to a modified attapulgite immobilized enzyme, a preparation method and application thereof, belonging to the technical field of material and bioengineering intersection.
Background
China is the largest antibiotic producing country, the exporting country and the consuming country in the world, and the annual output exceeds 20 ten thousand tons. Among them, erythromycin is the earliest antibiotic found and widely applied to clinic, and the production of erythromycin brings about a great deal of fungus dregs and waste liquid containing erythromycin, which brings about environmental risks and limits the development of the antibiotic industry in China. Compared with other methods, the microbial degradation method has the advantages of low cost, high efficiency, small environmental pollution and the like, so compared with other methods, the microbial degradation method is the most ideal method for degrading antibiotics at the present stage, however, the direct use of bacteria can generate the problem of enrichment of resistance genes, and therefore, the enzyme is excavated from the microorganisms to realize the degradation of erythromycin becomes a research hot spot. The existing erythromycin degrading enzyme ereB can effectively degrade erythromycin under mild conditions, but has higher application cost due to the irrecoverable enzyme, thereby limiting the popularization and application thereof.
Disclosure of Invention
The invention aims to overcome the defects of the prior art, and provides a modified attapulgite immobilized enzyme, a preparation method and application thereof, wherein the modified attapulgite immobilized enzyme has remarkable stability and recoverability, can effectively degrade fungus residues containing erythromycin, sewage and water in the environment, and is beneficial to amplifying application in industrialization.
In order to solve the technical problems, the invention provides a preparation method of modified attapulgite immobilized enzyme, which comprises the following steps: firstly, modifying an attapulgite material, then dissolving erythromycin degrading enzyme and modified attapulgite in a phosphate buffer solution, adjusting the pH value to 6.0-8.0, stirring for 3-4 hours at 20-30 ℃, and freeze-drying to obtain the modified attapulgite immobilized enzyme.
The specific modification method of the attapulgite material comprises the following steps:
Stirring attapulgite in 2mol/L hydrochloric acid at 60 ℃ for 2 hours, filtering, washing to be neutral, drying, crushing, and sieving with a 100-mesh sieve, wherein the mass volume ratio of the attapulgite to the hydrochloric acid solution is 1g:10mL;
Adding 15% (volume fraction) of KH570 (silane coupling agent) aqueous solution into the obtained attapulgite, regulating the pH value to 3-4 by hydrochloric acid, stirring for 12 hours at normal temperature, centrifuging, washing and drying to obtain KH570 coupled attapulgite, wherein the volume ratio of the attapulgite to the KH570 solution is 1g:5mL;
Adding KH570 coupling attapulgite into 8% (volume fraction) glutaraldehyde solution, stirring for 12 hours, and drying to obtain modified attapulgite, wherein the mass volume ratio of KH570 coupling attapulgite to 8% glutaraldehyde is 1g:10mL.
Modified attapulgite immobilized enzyme:
The erythromycin degrading enzyme and the modified attapulgite are dissolved in phosphate buffer solution according to a certain proportion, the pH value of the solution is regulated to 6.0-8.0, and the solution is stirred for 3-4 hours at 20-30 ℃, and the modified attapulgite immobilized enzyme is obtained by freeze drying.
Further, the erythromycin degrading enzyme is ereB enzyme; the freeze-drying temperature is-55 to-75 ℃. The mass ratio of the modified attapulgite to the enzyme is 10 to 1.
Preferably, the phosphate buffer is adjusted to a pH of 6.0 to 8.0 with K 2HPO4 and KH 2PO4.
The application of the modified attapulgite immobilized enzyme in degrading erythromycin-containing bacterial residues, sewage and water in the environment.
Drawings
FIG. 1 is an SDSPAGE electrophoretogram of an enzyme obtained by expression purification;
FIG. 2 is a modified attapulgite material prepared;
FIG. 3 is a modified attapulgite immobilized enzyme material prepared;
FIG. 4 is a graph of the relative viability of a modified attapulgite immobilized enzyme material at different cycle numbers;
FIG. 5 is a graph showing the degradation rate of a modified attapulgite immobilized enzyme material applied to erythromycin fermentation mold residues;
FIG. 6 is a graph showing the degradation rate of a modified attapulgite immobilized enzyme material applied to a water body containing erythromycin.
Detailed Description
The invention is further described below with reference to examples. The following examples are only for more clearly illustrating the technical aspects of the present invention, and are not intended to limit the scope of the present invention.
Example 1
Expression and purification of proteins of interest
Screening a gene sequence of the efficient degradation erythromycin enzyme from a protein database, using the gene sequence as a template, using Primer software to design a corresponding Primer, and obtaining a target fragment through PCR; constructing recombinant plasmids by taking the corresponding plasmids as vectors; expression was induced at low temperature in E.coli using IPTG.
Because the target protein contains his label, can be adsorbed by nickel in Ni-NTA or imidazole, so that imidazole solution with different concentrations can be used for eluting and purifying.
The expression of the enzyme was detected by SDS-PAGE.
As shown in FIG. 1, the bands of the purified lanes were significantly pure, indicating successful expression purification.
Example 2
The invention provides a preparation method of modified attapulgite immobilized enzyme, which comprises the following steps:
1. Preparation of modified Attapulgite
15G of attapulgite is weighed in 150mL of 2mol/L hydrochloric acid, stirred for 2 hours at 60 ℃, filtered, washed to be neutral, dried, crushed and sieved by a 100-mesh sieve, and the acid-modified attapulgite is obtained.
Adding 10g of acid modified attapulgite into 50mL of 15% KH570 aqueous solution, regulating the pH value to 3-4 by using hydrochloric acid, stirring for 12h at normal temperature, centrifuging, washing and drying to obtain KH570 coupled attapulgite.
And (3) taking the attapulgite, adding glutaraldehyde solution with a certain concentration for crosslinking, and drying to obtain the modified attapulgite.
Immobilization of ereB enzyme
And (3) adding a proper amount of modified attapulgite into ereB enzyme solution (the mass ratio of the attapulgite to the enzyme is 10 to 1) (0.1 mol/L phosphate buffer solution is prepared), adjusting the pH value of the solution to 7.0, stirring for 4 hours at 25 ℃, and freeze-drying to obtain the modified attapulgite immobilized enzyme.
Example 3
Enzyme activity under different cycle numbers
Adding 1mL of erythromycin methanol solution with the concentration of 10g/L into 100mL of ultrapure water to prepare 100mg/L of erythromycin solution; 1mL of 100mg/L erythromycin solution is taken to be added with 0.1g of prepared modified attapulgite immobilized enzyme, the mixture is placed in a shaking table for reaction for five minutes at 25 ℃ for 300 r.p., the mixture is taken out and placed in a centrifuge for 12000 r.p.1 for 1 min, the supernatant reaction solution is taken out, the content of residual erythromycin is measured by high performance liquid chromatography, and then 1mL of erythromycin solution is added to the modified attapulgite immobilized enzyme, and the test is repeated for 10 times (as shown in figure 3).
As can be seen from fig. 4, the residual viability after ten repetitions also reached 70.90%.
Example 4
Application of modified attapulgite immobilized enzyme in different environments
1. Application of modified attapulgite immobilized enzyme in fungus dreg
Taking 100mL of erythromycin bacteria residues, and measuring the erythromycin concentration to be about 650 mg/L; then adding 0.65g of prepared modified attapulgite immobilized enzyme, and reacting for 30min at normal temperature and normal pressure. Stirring to promote catalysis, degrading rate of 30min reaches 82% (as shown in figure 4), centrifuging to collect material, and repeating the above steps to reuse the material with recovery rate of 70%.
The control group was prepared by adding an equal amount of free ereB enzyme to the same system.
As can be seen from FIG. 5, the modified attapulgite immobilized enzyme has a half-life period of about 20 minutes in the bacterial residues, and has better effect and better degradation efficiency and rate compared with the free enzyme.
2. Application of modified attapulgite immobilized enzyme in erythromycin-containing wastewater
Taking 100mL of pharmaceutical factory sewage, and measuring the erythromycin concentration to be about 350 mg/L; then adding 0.35g of prepared modified attapulgite immobilized enzyme, placing the mixture at normal temperature and normal pressure for reaction for 30min, stirring to promote catalysis, and centrifugally collecting the material, wherein the recovery rate reaches 85%.
The control group is that the same amount of free ereB enzyme is added into the same system, and the degradation efficiency and the degradation rate are better than those of the free enzyme.
From fig. 6, the degradation effect of the modified attapulgite immobilized enzyme in the water body is better than that in the fungus dreg, and the degradation effect reaches 92% in 30 minutes.
Claims (4)
1. The application of the modified attapulgite immobilized enzyme in degrading fungus dreg and sewage containing erythromycin is characterized in that the preparation method of the modified attapulgite immobilized enzyme comprises the following steps:
(1) Modification of the attapulgite material:
Stirring attapulgite in 2 mol/L hydrochloric acid at 60 ℃ for 2 hours, filtering, washing to be neutral, drying, crushing and sieving to obtain acid-treated attapulgite;
Adding the acid-treated attapulgite into KH570 water solution, regulating the pH value to 3-4 by hydrochloric acid, stirring at normal temperature, centrifuging, washing, and drying to obtain KH 570-coupled attapulgite;
Adding KH570 coupled attapulgite into glutaraldehyde solution with volume fraction of 8%, stirring, and oven drying to obtain modified attapulgite;
(2) The erythromycin degrading enzyme ereB enzyme and the modified attapulgite clay are dissolved in phosphate buffer solution according to the mass ratio of 10 to 1, the pH value of the solution is regulated to 6.0-8.0, and the solution is stirred for 3-4 hours at 20-30 ℃, and the modified attapulgite clay immobilized enzyme is obtained by freeze drying.
2. The application of the modified attapulgite immobilized enzyme in degrading erythromycin-containing bacterial residues and sewage according to claim 1, wherein the mass-volume ratio of the attapulgite to the hydrochloric acid solution in the step (1) is 1g:10mL.
3. The application of the modified attapulgite immobilized enzyme in degrading erythromycin-containing bacterial residues and sewage according to claim 1, wherein the volume ratio of the attapulgite treated by acid to the KH570 solution is 1g:5mL.
4. The application of the modified attapulgite immobilized enzyme in degrading erythromycin-containing bacterial residues and sewage according to claim 1, wherein the mass-volume ratio of KH570 coupled attapulgite to glutaraldehyde solution is 1g:10 And (3) mL.
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| CN102382811A (en) * | 2011-11-08 | 2012-03-21 | 中国农业科学院油料作物研究所 | Preparation method of attapulgite immobilized enzyme for ester exchange reaction |
| CN113736769A (en) * | 2021-08-28 | 2021-12-03 | 常州大学 | MOFs immobilized enzyme and preparation method and application thereof |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN102382811A (en) * | 2011-11-08 | 2012-03-21 | 中国农业科学院油料作物研究所 | Preparation method of attapulgite immobilized enzyme for ester exchange reaction |
| CN113736769A (en) * | 2021-08-28 | 2021-12-03 | 常州大学 | MOFs immobilized enzyme and preparation method and application thereof |
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| Title |
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| 有机改性凹凸棒土交联吸附法固定化磷脂酶A1 研究;陶明等;粮食与油脂(第11期);第12-15页 * |
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