CN106811458A - A kind of method of the preparation method of immobilization laccase carrier and degraded micro quantity organic pollutant - Google Patents

A kind of method of the preparation method of immobilization laccase carrier and degraded micro quantity organic pollutant Download PDF

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CN106811458A
CN106811458A CN201710213939.XA CN201710213939A CN106811458A CN 106811458 A CN106811458 A CN 106811458A CN 201710213939 A CN201710213939 A CN 201710213939A CN 106811458 A CN106811458 A CN 106811458A
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laccase
preparation
immobilization
carrier
immobilization laccase
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张耿崚
王小琴
李清荷
陈细妹
韩业鉅
鄧昊
孙健
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Guangdong University of Technology
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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
    • A—HUMAN NECESSITIES
    • A62—LIFE-SAVING; FIRE-FIGHTING
    • A62D—CHEMICAL MEANS FOR EXTINGUISHING FIRES OR FOR COMBATING OR PROTECTING AGAINST HARMFUL CHEMICAL AGENTS; CHEMICAL MATERIALS FOR USE IN BREATHING APPARATUS
    • A62D3/00—Processes for making harmful chemical substances harmless or less harmful, by effecting a chemical change in the substances
    • A62D3/02—Processes for making harmful chemical substances harmless or less harmful, by effecting a chemical change in the substances by biological methods, i.e. processes using enzymes or microorganisms
    • 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
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0055—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10)
    • C12N9/0057—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10) with oxygen as acceptor (1.10.3)
    • C12N9/0061—Laccase (1.10.3.2)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y110/00—Oxidoreductases acting on diphenols and related substances as donors (1.10)
    • C12Y110/03—Oxidoreductases acting on diphenols and related substances as donors (1.10) with an oxygen as acceptor (1.10.3)
    • C12Y110/03002—Laccase (1.10.3.2)
    • A—HUMAN NECESSITIES
    • A62—LIFE-SAVING; FIRE-FIGHTING
    • A62D—CHEMICAL MEANS FOR EXTINGUISHING FIRES OR FOR COMBATING OR PROTECTING AGAINST HARMFUL CHEMICAL AGENTS; CHEMICAL MATERIALS FOR USE IN BREATHING APPARATUS
    • A62D2101/00—Harmful chemical substances made harmless, or less harmful, by effecting chemical change
    • A62D2101/20—Organic substances

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  • Immobilizing And Processing Of Enzymes And Microorganisms (AREA)

Abstract

The application belongs to enzyme immobilization technology field, and in particular to a kind of method of preparation method of immobilization laccase carrier and degraded micro quantity organic pollutant.The invention provides a kind of preparation method of immobilization laccase carrier, its preparation process is simple, with low cost, the immobilization laccase carrier for obtaining is high with the Percentage bound of enzyme, the reactivity of laccase itself is not only maintained, the stability of laccase is further improved and is realized the purpose that laccase is recycled.Present invention also offers a kind of preparation method of immobilization laccase, obtained by the way that foregoing immobilization laccase carrier and laccase are mixed into fixation；When above-mentioned immobilization laccase is applied into the micro quantity organic pollutant in degraded environmental sample, its degradation efficiency is up to 92%, and degradation time is short, and catabolite non-secondary pollution, environmental protection.

Description

A kind of preparation method of immobilization laccase carrier and micro quantity organic pollutant of degrading Method
Technical field
The invention belongs to enzyme immobilization technology field, and in particular to a kind of preparation method of immobilization laccase carrier and degraded The method of micro quantity organic pollutant.
Background technology
Micro quantity organic pollutant has the characteristics of concentration is low, toxicity is big, its stable chemical nature, can persistently be present in nature In environment, it is fat-soluble it is strong, be easily absorbed by organisms, but be difficult and degraded by body.The various organic dirt of correlative study display category There is certain correlation between the mutagenicity and carcinogenicity that contaminate thing.According to pertinent literature, various environmental samples as Table water, underground water, sludge sediment can even be detected in Trace Organic Pollutants in Drinking Water, and its concentration is from ng/L To μ g/L.Therefore, the micro quantity organic pollutant in environment of how effectively degrading receives greatly concern in recent years.With adopt Compared with the technology of the treatment micro quantity organic pollutant such as membrane technology, reverse osmosis technology, high-level oxidation technology and electrochemical techniques, adopted Be considered as current most promising technology with ferment treatment micro quantity organic pollutant of degrading, its reaction condition is gentle, with compared with Atopic high and speed, compared with most of chemical catalysis processes, the energy of ferment treatment consumption is less, with low cost.
Laccase (Laccase EC 1.10.3.2) is a kind of cupric polyphenol oxidase, and its effect is mainly catalysis oxidation also Original reaction.Laccase is broadly divided into：Fungal laccase and bacterial laccase.Most of laccases have and 4 have individual copper ion, collectively form laccase Activated centre, plays a crucial role in catalytic reaction.This four copper ions are combined in albumen inner height conservative region, according to its electricity Sub- paramagnetic resonance and spectral signature can be divided into following three class：1 I type copper ion, 1 II type copper ion and 2 III type copper ions. Catalysis of the laccase to substrate is main to be completed by four synergies of copper ion.Numerous studies show that I type copper ion is laccase Catalysis oxidation substrate, " entrance " that receives substrate electron, and the three core copper ion clusters that II type and III type copper ion are constituted are then oxygen Gas is reduced to the position of water.Electronics in laccase intramolecular is transmitted from I type copper ion to three core copper ion races.Laccase can be by molecule Oxygen is reduced directly to water, in the presence of no hydrogen peroxide and other secondary metabolites, can be catalyzed substantial amounts of phenols and fragrance The oxidative degradation of aminated compounds, is a kind of environmentally friendly enzyme, at aspects such as wastewater treatment, paper industry, environmental protection With significant application value.
The free laccase deactivation easily with the change of environment in use, storage stability is low, easily mixes miscellaneous Matter difficult separation and recycling, these all further limit the promotion and application of laccase.Enzyme immobilization technology is nearly more than ten years development The enzyme application technology got up, immobilised enzymes while its efficient selectivity and gentle enzymic catalytic reaction characteristic is kept, and gram The weak point of enzyme is taken, therefore has been the stability for improving free state laccase and having that realization is recycled to being fixed of laccase Efficacious prescriptions method.The material of current enzyme immobilization carrier is mainly shitosan, silica gel, activated carbon, macromolecular filter membrane and electrospinning fibre etc., But existing enzyme immobilization carrier exists in various degree, and low enzyme Percentage bound, inferior separating effect, repeat usage be low, preparation technology is multiple Miscellaneous and relatively costly the problems such as.
The content of the invention
In view of this, it is an object of the invention to provide a kind of preparation method of immobilization laccase carrier, its preparation technology Simply, and thus obtained immobilization laccase is activity stabilized, repeat usage is high, can be efficiently applied to degrade micro- in environment Amount organic pollution.
Technical scheme is as follows：
The invention provides a kind of preparation method of immobilization laccase carrier, comprise the following steps：
A) silica is placed in 3- aminopropyl triethoxysilane solution, is reacted, obtain 3- aminopropyl-triethoxies The silica of silane surfaces modification；
The silica of the 3- aminopropyl triethoxysilane surface modifications that b) will be obtained in step a) is placed in crosslinking agent Cross-linking reaction is carried out, the immobilization laccase carrier is obtained.
Preferably, crosslinking agent described in step b) is glutaraldehyde, maleic anhydride or carbodiimides.
It is furthermore preferred that the glutaraldehyde is the mixed solution of glutaraldehyde and kaliumphosphate buffer；
The concentration of volume percent of glutaraldehyde is 2.5%~10% in the mixed solution；
It is furthermore preferred that the time of the cross-linking reaction is 1h~6h, the temperature of the cross-linking reaction is 25 DEG C -40 DEG C.
Preferably, 3- aminopropyl triethoxysilanes solution described in step a) are the third of 3- aminopropyl triethoxysilanes Ketone solution；
The concentration of volume percent of 3- aminopropyl triethoxysilanes is in the 3- aminopropyl triethoxysilanes solution 2%~10%.
Preferably, silica described in step a) is silicon oxide pellets；
A diameter of 1~2cm of the silicon oxide pellets.
Present invention also offers a kind of preparation method of immobilization laccase, the immobilization laccase that above-mentioned preparation method is obtained Carrier and laccase solution mix, and obtain the immobilization laccase.
Preferably, the activity of the laccase is 1.5~3.0U/mL.
Preferably, described being blended on shaking table is carried out, and its rotating speed is 90rpm~120rpm；
The time of the mixing is 24h~48h.
Present invention also offers a kind of method of micro quantity organic pollutant of degrading, the immobilization that aforementioned preparation process is obtained Laccase and the sample containing micro quantity organic pollutant mix, micro quantity organic pollutant of degrading.
Preferably, the temperature of the degraded is 30~80 DEG C, and pH is 2~8；
The time of the degraded is 4h~10h.
In sum, the invention provides a kind of preparation method of immobilization laccase carrier, its preparation process is simple, cost Cheap, the immobilization laccase carrier for obtaining is high with the Percentage bound of enzyme, not only maintains the reactivity of laccase itself, further improves The stability of laccase and the purpose for realizing laccase recycling.Present invention also offers a kind of preparation side of immobilization laccase Method, is obtained by the way that foregoing immobilization laccase carrier and laccase are mixed into fixation, and preparation process is simple, the immobilization laccase tool for obtaining Active stabilization, can for a long time preserve, be easily isolated recovery and the advantages of can be recycled；It is applied in degraded environmental sample Micro quantity organic pollutant when, its degradation efficiency is up to 92%, and degradation time is short, and catabolite non-secondary pollution, green Environmental protection.
Brief description of the drawings
In order to illustrate more clearly about the embodiment of the present invention or technical scheme of the prior art, below will be to embodiment or existing The accompanying drawing to be used needed for having technology description is briefly described, it should be apparent that, drawings in the following description are only this Inventive embodiment, for those of ordinary skill in the art, on the premise of not paying creative work, can also basis The accompanying drawing of offer obtains other accompanying drawings.
Fig. 1 is degradation rate and laccase activity of the immobilization laccase to double (4- hydroxy phenyls) propane of 2,2- in embodiment 3 Influence；
Fig. 2 is that the storage stability of immobilization laccase in embodiment 4 investigates result.
Specific embodiment
Technical scheme is clearly and completely described below in conjunction with the specific embodiment of the invention, it is clear that Described embodiment is a part of embodiment of the invention, rather than whole embodiments.Those skilled in the art should manage Solution, modifies to specific embodiment of the invention or some technical characteristics is replaced on an equal basis, without deviating from the present invention The spirit of technical scheme, all should cover in the scope of protection of the invention.
The preparation of the immobilization laccase of embodiment 1
1) the commercially available ore SiO for being evenly distributed with cellular micropore is taken2, it is milled into multiple quality about 0.5g, diameter about It is the SiO of 1.1cm2(specific surface area is 1.7005m to bead2/g)；Then, adopt and SiO is washed with deionized2Bead, and put 24h is dried with 45 DEG C of conditions in electric drying oven with forced convection, it is stand-by.
2) by step 1) in SiO after drying2Bead is immersed in the second of 3- aminopropyls three that 12.5mL concentration is 6vol% Surface modification 24h is carried out in TMOS solution (APTES), then carrier table is rested on to clean with deionized water rinsing 4 times The organic phase in face, then be placed under 45 DEG C of temperature conditionss and dry 24h.
3) by step 2) in SiO after surface modification2Bead is immersed in the glutaraldehyde that 12.5mL concentration is 7.5vol% In solution, it is placed in 30 DEG C on rail mounted shaking table, 90rpm is crosslinked 2h, is then cleaned for several times with 50mL deionized waters, then at 45 DEG C Under the conditions of dry 48h, being fixed laccase carrier.
4) by step 3) in the immobilization laccase carrier that obtains be placed in the laccase solution that 5mL activity is 2U/mL, be placed in rail With 30 DEG C, 100rpm vibrations 24h on road shaking table so that laccase can be uniformly fixed on carrier, being fixed laccase.
To step 4) in the immobilization laccase that obtains carry out enzymatic activity test, with 2'- hydrazines-bis- -3- ethyl-benzothiazoles Quinoline -6- sulfonic acid (ABTS) is substrate, then determines ABTS in 420nm (ε by ultraviolet-uisible spectrophotometermax=3.6 × 104M-1cm-1) change of absorbance at place determines oxidation rate of the enzyme to it.Detailed process is：At room temperature, by step (4) In 0.001mol/LABTS (pH=4.5) solution of the immobilization laccase that obtains and 3mL mix, be placed in rail mounted shaking table with 120rpm shakes up, and solution is collected after 5min and measures its absorbance using ultraviolet specrophotometer immediately, being fixed laccase Activity.
Embodiment 2 investigates APTES, glutaraldehyde to SiO2The influence of bead and Laccase Immobilization Percentage bound
1) dose volume percent concentration is respectively 2%, 4%, 6%, 8% and 10% APTES solution.
2) dose volume percent concentration is respectively 2.5%, 5.0%, 7.5% and 10.0% glutaraldehyde solution.
3) by the step 1 of embodiment 1) in SiO after drying2Bead is immersed in step 1 respectively) prepare 5 kinds of APTES it is molten In liquid, then according to the step 2 in embodiment 1) to step 4) process prepares immobilization laccase, then using UV, visible light Absorbance at spectrophotometric determination 595nm, the protein on immobilization laccase carrier is determined according to the change of absorbance Content, so as to calculate the Percentage bound of laccase and carrier, as a result as shown in table 1, shows that it is the APTES solution of 6vol% to use concentration The Percentage bound highest of the immobilization laccase carrier for obtaining.
4) by the step 1 of embodiment 1) in SiO after drying2Bead is immersed in step 2 respectively) prepare 5 kinds of glutaraldehydes In solution, then according to the step 2 in embodiment 1) and step 4) process prepares immobilization laccase, then using it is ultraviolet can The absorbance seen at spectrophotometric determination 595nm, the albumen on immobilization laccase carrier is determined according to the change of absorbance Matter content, so as to calculate the Percentage bound of laccase and carrier, as a result as shown in table 2, shows that it is the penta 2 of 7.5vol% to use concentration The Percentage bound highest of the immobilization laccase carrier that aldehyde solution is obtained.
Table 1
Table 2
Influence of the immobilization laccase of embodiment 3 to the degradation rate and laccase activity of BPA
Free state laccase using activity as 2U/mL investigates the immobilization laccase obtained in embodiment 1 to 2,2- as control The influence of the degradation efficiency and laccase activity of double (4- hydroxy phenyls) propane (BPA).At 50 DEG C, by immobilization laccase and BPA is dissolved in citrate buffer (0.05mol/L, pH4.5), the final concentration of 100mg/L of BPA.Then, sampled every 1h And using the change in concentration of BPA in high-efficient liquid phase analysis solution to be measured.Result shows, after 1h, degraded of the immobilization laccase to BPA Up to 71%, free state laccase is 61% to the degradation rate of BPA to rate, and the activity of immobilization laccase is the 78% of initial activity, and is swum Amorph laccase is only the 40% of initial activity.After 6h, up to 92%, now the activity of immobilization laccase is for the degradation rate of BPA 53%, remain to maintain of a relatively high activity；And the degradation efficiency that the activity of free state laccase only has 16%, BPA also only reaches 85%.Result as shown in figure 1, compared with free state laccase, immobilization laccase in enzyme activity, stability and degraded BPA efficiency all It is obviously improved, therefore immobilization laccase prepared by the present invention can be reached at reduction by reusing and improving degradation efficiency Manage the requirement of cost.
Embodiment 4
Immobilization laccase in embodiment 1 is stored in kaliumphosphate buffer (0.5mol/L, pH=7.0), in 4 DEG C of ice Case is preserved, and week about, tests the activity of laccase.Measurement result is as shown in Fig. 2 the immobilization laccase relative activity of the 3rd week is 90%, it is higher by free state laccase 29%；The free state laccase relative activity of the 7th, 8 weeks is respectively 15%, 9%, immobilization laccase Relative activity be 81%, 79%, show that immobilization laccase storage stability has greatly improved compared to free state laccase.

Claims (10)

1. a kind of preparation method of immobilization laccase carrier, it is characterised in that comprise the following steps：
A) silica is placed in 3- aminopropyl triethoxysilane solution, is reacted, obtain 3- aminopropyl triethoxysilanes The silica of surface modification；
The silica of the 3- aminopropyl triethoxysilane surface modifications that b) will be obtained in step a) is placed in crosslinking agent and carries out Cross-linking reaction, obtains the immobilization laccase carrier.
2. preparation method according to claim 1, it is characterised in that crosslinking agent described in step b) is glutaraldehyde, along fourth Enedioic acid acid anhydride or carbodiimides.
3. preparation method according to claim 2, it is characterised in that the glutaraldehyde is glutaraldehyde and kaliumphosphate buffer Mixed solution；
The concentration of volume percent of glutaraldehyde is 2.5%~10% in the mixed solution；
The time of the cross-linking reaction is 1h~6h；
The temperature of the cross-linking reaction is 25 DEG C -40 DEG C.
4. preparation method according to claim 1, it is characterised in that 3- aminopropyl triethoxysilanes described in step a) Solution is the acetone soln of 3- aminopropyl triethoxysilanes；
In the 3- aminopropyl triethoxysilanes solution concentration of volume percent of 3- aminopropyl triethoxysilanes be 2%~ 10%.
5. preparation method according to claim 1, it is characterised in that silica described in step a) is that silica is small Ball；
A diameter of 1~2cm of the silicon oxide pellets.
6. a kind of preparation method of immobilization laccase, it is characterised in that by preparation method described in claim 1 to 5 any one Immobilization laccase carrier and the laccase solution mixing for obtaining, obtain the immobilization laccase.
7. preparation method according to claim 6, it is characterised in that the activity of the laccase is 1.5~3.0U/mL.
8. preparation method according to claim 6, it is characterised in that described being blended on shaking table is carried out, and its rotating speed is 90rpm~120rpm；
The time of the mixing is 24h~48h.
9. it is a kind of degrade micro quantity organic pollutant method, it is characterised in that will described in claim 6 to 8 any one prepare The immobilization laccase that method is obtained and the sample mixing containing micro quantity organic pollutant, micro quantity organic pollutant of degrading.
10. method according to claim 9, it is characterised in that the temperature of the degraded is 30~80 DEG C, pH is 2~8；
The time of the degraded is 4h~10h.
CN201710213939.XA 2017-04-01 2017-04-01 A kind of method of the preparation method of immobilization laccase carrier and degraded micro quantity organic pollutant Pending CN106811458A (en)

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Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN109439189A (en) * 2018-11-21 2019-03-08 中国船舶重工集团公司第七二五研究所 A kind of process for fixation of antifouling enzyme on inorganic coating surface
CN109971177A (en) * 2019-04-16 2019-07-05 无锡纯宇环保制品有限公司 A kind of polybag of rapid and natural degradation
CN110760502A (en) * 2019-05-07 2020-02-07 宁波大学 Laccase co-crosslinking immobilization method
CN114349182A (en) * 2022-01-07 2022-04-15 南京工业大学 Method for degrading bisphenol A in solutions with different pH values by using metal organic framework ZIF-8 immobilized laccase

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CN102994491A (en) * 2012-07-12 2013-03-27 浙江大学 Immobilization method of Thermus lipase

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CN102994491A (en) * 2012-07-12 2013-03-27 浙江大学 Immobilization method of Thermus lipase

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Cited By (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN109439189A (en) * 2018-11-21 2019-03-08 中国船舶重工集团公司第七二五研究所 A kind of process for fixation of antifouling enzyme on inorganic coating surface
CN109439189B (en) * 2018-11-21 2020-12-18 中国船舶重工集团公司第七二五研究所 Method for immobilizing antifouling enzyme on surface of inorganic coating
CN109971177A (en) * 2019-04-16 2019-07-05 无锡纯宇环保制品有限公司 A kind of polybag of rapid and natural degradation
CN110760502A (en) * 2019-05-07 2020-02-07 宁波大学 Laccase co-crosslinking immobilization method
CN110760502B (en) * 2019-05-07 2023-03-21 宁波大学 Laccase co-crosslinking immobilization method
CN114349182A (en) * 2022-01-07 2022-04-15 南京工业大学 Method for degrading bisphenol A in solutions with different pH values by using metal organic framework ZIF-8 immobilized laccase
CN114349182B (en) * 2022-01-07 2023-11-14 南京工业大学 Method for degrading bisphenol A in solutions with different pH values by adopting metal-organic framework ZIF-8 immobilized laccase

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Application publication date: 20170609