CN110637970B - Application of syringaldehyde as mediator participating in degradation of mycotoxin by laccase - Google Patents

Application of syringaldehyde as mediator participating in degradation of mycotoxin by laccase Download PDF

Info

Publication number
CN110637970B
CN110637970B CN201910939294.7A CN201910939294A CN110637970B CN 110637970 B CN110637970 B CN 110637970B CN 201910939294 A CN201910939294 A CN 201910939294A CN 110637970 B CN110637970 B CN 110637970B
Authority
CN
China
Prior art keywords
laccase
mycotoxin
syringaldehyde
degradation
mediator
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Active
Application number
CN201910939294.7A
Other languages
Chinese (zh)
Other versions
CN110637970A (en
Inventor
姚斌
苏小运
王晓璐
罗会颖
黄火清
王苑
柏映国
涂涛
王亚茹
张�杰
师霞
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Institute of Animal Science of CAAS
Original Assignee
Institute of Animal Science of CAAS
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Institute of Animal Science of CAAS filed Critical Institute of Animal Science of CAAS
Priority to CN201910939294.7A priority Critical patent/CN110637970B/en
Publication of CN110637970A publication Critical patent/CN110637970A/en
Application granted granted Critical
Publication of CN110637970B publication Critical patent/CN110637970B/en
Active legal-status Critical Current
Anticipated expiration legal-status Critical

Links

Images

Classifications

    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
    • A23L5/20—Removal of unwanted matter, e.g. deodorisation or detoxification
    • A23L5/25—Removal of unwanted matter, e.g. deodorisation or detoxification using enzymes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
    • A23L5/20—Removal of unwanted matter, e.g. deodorisation or detoxification
    • A23L5/27—Removal of unwanted matter, e.g. deodorisation or detoxification by chemical treatment, by adsorption or by absorption
    • 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)

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Genetics & Genomics (AREA)
  • Wood Science & Technology (AREA)
  • Zoology (AREA)
  • Biochemistry (AREA)
  • Polymers & Plastics (AREA)
  • Microbiology (AREA)
  • Food Science & Technology (AREA)
  • Nutrition Science (AREA)
  • General Health & Medical Sciences (AREA)
  • General Engineering & Computer Science (AREA)
  • Molecular Biology (AREA)
  • Biotechnology (AREA)
  • Biomedical Technology (AREA)
  • Medicinal Chemistry (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

The invention belongs to the field of agricultural biology, and particularly relates to application of syringaldehyde as a high-efficiency mediator participating in degradation of mycotoxin by using laccase derived from bacillus subtilis. The invention provides a high-efficiency laccase mediator for mycotoxin degradation. The mediator can assist the laccase from the bacillus subtilis to effectively degrade mycotoxins with different structural types, and is widely applied to the field of mycotoxin detoxification of foods and feeds.

Description

Application of syringaldehyde as mediator participating in degradation of mycotoxin by laccase
Technical Field
The invention belongs to the technical field of agricultural biology, and particularly relates to application of syringaldehyde as a mediator participating in degradation of mycotoxin by laccase.
Background
Mycotoxins are secondary metabolites produced by fungi, mainly pollute stored grain and oil food and feed, and seriously harm human and livestock health. According to the structural characteristics of the mycotoxins, the mycotoxins can be divided into two main classes of aromatic rings and non-aromatic rings, wherein the aromatic rings comprise aflatoxin, zearalenone, citrinin, ochratoxin, patulin, trichothecene toxins and the like; the non-aromatic ring includes fumonisins only. Of these, aflatoxins, zearalenone and deoxynivalenol (vomitoxin) are the most common and most harmful mycotoxins. Therefore, there is a need to establish a simple, effective and environmentally friendly method for detoxification of mycotoxins.
At present, the detoxification method of the feed polluted by mycotoxin mainly comprises a physical method, a chemical method, an adsorption method, a biological method and the like. Physical and chemical detoxification methods have the defects of difficult operation, unstable effect, large loss of nutrient components, influence on the palatability of the feed and the like. Although the adsorption method is simple and easy, the method has the defects of large dosage, low economy, easy secondary pollution and the like. The microbial detoxification method has the advantages of mild action conditions, little influence on sensory properties, palatability and the like of the raw materials, increase in the nutritive value of the raw materials and the like, and is considered to be the optimal detoxification method. Biological detoxification mainly refers to the enzymatic reaction of degrading enzymes to convert toxins into low-toxicity or non-toxicity products, wherein the degrading enzymes comprise oxidases such as laccase, manganese peroxidase, hydrolases (such as esterase) and the like.
In the process of realizing large-scale application of the biological detoxification technology, bacterial strains capable of degrading mycotoxin are searched and screened, characteristic research is carried out on extracellular degrading enzymes produced by the bacterial strains, and degrading enzyme genes are cloned and expressed, so that the bacterial strains are important breakthrough points and development directions in the research field of mycotoxin biodegradation. Therefore, establishing a high-efficiency degradation system for degrading mycotoxin by an enzyme method is the key point of the biological detoxification technology.
The degradation rate of the prior laccase to the mycotoxin is generally low. It is reported in the literature that when dye decolorization is performed using a laccase-mediator system, the effect of the mediator depends on the type of dye being treated. For example, white rot fungus laccase can effectively degrade acid red 73 by taking HBT as a mediator. When the coriolus versicolor laccase is used for pesticide degradation, different pesticide substrates show selectivity for mediators, for example, when pyrimethanil and isoproturon are degraded, the best mediator is the cyanuric acid, and acetosyringone and HBT are the best mediators for degrading chlorothalonil and naprophytin. It follows that suitable mediators of laccases differ significantly by their differences in their substrate-degrading properties.
Disclosure of Invention
The invention aims to provide application of syringaldehyde serving as a mediator participating in degradation of mycotoxin by laccase derived from bacillus subtilis.
The application of syringaldehyde serving as a mediator participating in the degradation of mycotoxin by laccase according to the specific embodiment of the invention is characterized in that the laccase is from bacillus subtilis, and the amino acid sequence of the laccase is shown as SEQ ID No. 1.
According to a specific embodiment of the invention, the mycotoxin is aflatoxin B1And/or zearalenone.
According to a particular embodiment of the invention, aflatoxin B is treated in a buffered solution1And zearalenone, wherein the buffer solution is a Tris-HCl solution with the concentration of 50mM and the pH value of 7.0.
The method for improving the degradation rate of the mycotoxin degraded by the laccase comprises the step of using syringaldehyde as a mediator participating in the degradation of the mycotoxin by the laccase, wherein the laccase is from bacillus subtilis, and the amino acid sequence of the laccase is shown as SEQ ID No. 1.
According to a specific embodiment of the invention, the mycotoxin is aflatoxin B1And/or zearalenone.
According to a particular embodiment of the invention, aflatoxin B is treated in a buffered solution1And zearalenone, wherein the buffer solution is a Tris-HCl solution with the concentration of 50mM and the pH value of 7.0.
The method of the invention can efficiently degrade mycotoxin, has low cost and wide application range, and can be widely applied to the field of feed toxin degrading enzymes.
Drawings
FIG. 1 shows the effect of Bacillus subtilis-derived laccase-syringaldehyde system on aflatoxin B1And zearalenone degradation.
FIG. 2 shows that aflatoxin B is degraded by a recombinant Bacillus subtilis-derived laccase-syringaldehyde system1The result of HPLC analysis of (1);
FIG. 3 shows the HPLC analysis result of the recombinant Bacillus subtilis laccase-syringaldehyde system for degrading zearalenone;
Detailed Description
Test materials and reagents
1. The strain is as follows: an engineered strain of Escherichia coli for producing laccase BsCotA derived from Bacillus subtilis.
2. Biochemical reagents: aflatoxin B1Zearalenone, syringaldehyde; chromatographic purity acetonitrile, trifluoroacetic acid and Tris.
3. Culture medium:
(1) coli culture medium LB (1% peptone, 0.5% yeast extract, 1% NaCl, ph7.0) BsCotA amino acid sequence was as follows:
MTLEKFVDALPIPDTLKPVQQSKEKTYYEVTMEECTHQLHRDLPPTRLWGYNGLF PGPTIEVKRNENVYVKWMNNLPSTHFLPIDHTIHHSDSQHEEPEVKTVVHLHGGV TPDDSDGYPEAWFSKDFEQTGPYFKREVYHYPNQQRGAILWYHDHAMALTRLNV YAGLVGAYIIHDPKEKRLKLPSDEYDVPLLITDRTINEDGSLFYPSAPENPSPSLPNP SIVPAFCGETILVNGKVWPYLEVEPRKYRFRVINASNTRTYNLSLDNGGDFIQIGSD GGLLPRSVKLNSFSLAPAERYDIIIDFTAYEGESIILANSAGCGGDVNPETDANIMQF RVTKPLAQKDESRKPKYLASYPSVQHERIQNIRTLKLAGTQDEYGRPVLLLNNKR WHDPVTETPKVGTTEIWSIINPTRGTHPIHLHLVSFRVLDRRPFDIARYQESGELSY TGPAVPPPPSEKGWKDTIQAHAGEVLRIAATFGPYSGRYVWHCHILEHEDYDMMR PMDITDPHK
example 1 preparation of recombinant laccase BsCotA
BL21(DE3)/BsCotA Escherichia coli engineering strain containing recombinant plasmid is taken and inoculated into 50mL LB culture solution, after shaking culture at 37 ℃ and 220rpm for 12h, the strain is transferred into 300mL LB culture medium according to the proportion of 2 percent, shaking culture at 37 ℃ and 220rpm is carried out for about 3h (OD600 is approximately equal to 0.6), inducer IPTG with the final concentration of 1mM is added, after 15h of induction at 16 ℃, the strain is collected by centrifugation. The cells were resuspended in disodium hydrogen phosphate-citric acid buffer (20mM, pH 7.5). The cells were lysed by ultrasonication. The disrupted cell debris was centrifuged and removed, purified by Ni affinity column chromatography, and the electrophoretically pure eluate was collected and dialyzed into Tris-HCl protein stock (50mM Tris-HCl, pH7.4, 150mM NaCl).
Example 2 BsCotA-mediator System for degradation of aflatoxin B1
Subjecting aflatoxin B1Dissolving the mixture into dimethyl sulfoxide to prepare a mother solution with the concentration of 50mg/L, and reacting according to the following reaction system: 50mM Tris-HCl (pH 7.0), 20. mu.L of aflatoxin B1Solution (50mg/L), 20. mu.L syringaldehyde solution (10mM), 20. mu.L BsCotA (300U/L). The reaction system was set to 3 replicates with the system without laccase BsCotA added as a control. The reaction is carried out at 30 ℃, acetonitrile with three times of volume is added after 10 hours to stop the reaction, and the aflatoxin B is analyzed by High Performance Liquid Chromatography (HPLC)1The degradation rate of (c). The liquid chromatography is Shimadzu Nexera UHPLC high performance liquid chromatography analysis system, and the chromatographic separation column is Zorbax SB-C18 (4.6X 250mm,5 μm), mobile phase A (water of 0.06% TFA), mobile phase B (acetonitrile of 0.05% TFA); gradient elution conditions 0% B for 4 min, 0% -100% B for 15 min, 100% B for 6 min; the detection wavelength is 365 nm.
The results are shown in FIGS. 1 and 2, and a part of aflatoxin B is seen1Has been degraded, the degradation rate is 74.6 percent when the syringaldehyde is used as a mediator, and the degradation rate is only 1.7 percent when the syringaldehyde is not added into the system. Therefore, when syringaldehyde is added into a degradation system, the degradation rate of aflatoxin B1 is improved by 70 times, and the addition of syringaldehyde obviously improves the effect of laccase on aflatoxin B1The degradation rate of (c). The degradation rate of the aspergillus flavus toxin B1 is 30.7 percent by using the laccase from the ganoderma lucidum and the syringaldehyde as a mediator, and the degradation rate is obviously lower than that of the toxin degradation by using the laccase from the bacillus subtilis.
Example 3 BsCotA-mediator System for the degradation of zearalenone
Dissolving zearalenone in dimethyl sulfoxide to prepare a mother solution of 50mg/L, and reacting the mother solution as followsThe method comprises the following steps: 50mM Tris-HCl (pH 7.0), 20. mu.L of aflatoxin B1Solution (50mg/L), 20. mu.L syringaldehyde solution (10mM), 20. mu.L BsCotA (300U/L). The reaction system was set to 3 replicates with the system without laccase BsCotA added as a control. The reaction is carried out at 30 ℃, acetonitrile with three times of volume is added after 10 hours to stop the reaction, and the degradation rate of the zearalenone is analyzed by High Performance Liquid Chromatography (HPLC). The liquid chromatography is Shimadzu Nexera UHPLC high performance liquid chromatography analysis system, and the chromatographic separation column is Zorbax SB-C18 (4.6X 250mm,5 μm), mobile phase A (water of 0.06% TFA), mobile phase B (acetonitrile of 0.05% TFA); gradient elution conditions 0% B for 4 min, 0% -100% B for 15 min, 100% B for 6 min; the detection wavelength was 316 nm.
As shown in fig. 1 and fig. 3, it can be seen that part of zearalenone was degraded, and the degradation rate was 86.9% when syringaldehyde was used as a mediator, while the degradation rate was only 1.6% when no syringaldehyde was added to the system. Therefore, when the syringaldehyde is added into the degradation system, the degradation rate of the zearalenone is improved by 80 times, and the degradation rate of the laccase on the zearalenone is obviously improved by adding the syringaldehyde. The degradation rate of the zearalenone by using the laccase from the ganoderma lucidum and the syringaldehyde as a mediator is 47.8 percent, and the degradation rate is obviously lower than that of the toxin degradation by using the laccase from the bacillus subtilis.
Example 4 BsCotA-mediator System for degrading fumonisin B1
Fumonisin B1Dissolving the mixture into dimethyl sulfoxide to prepare a mother solution of 100mg/L, and reacting according to the following reaction system: 50mM Tris-HCl (pH 7.0), 20. mu.L of fumonisin B1Solution (100mg/L), 20. mu.L syringaldehyde solution (10mM), 20. mu.L BsCotA (300U/L). The reaction system was set to 3 replicates with the system without laccase BsCotA added as a control. The reaction was carried out at 30 ℃ and after 10h the reaction was stopped by adding three volumes of acetonitrile. The Shimadzu Nexera UHPLC system is used together with an AB-SCIEX 5600+ Triple TOF mass spectrometer to treat fumonisin B1And (5) detecting degradation. The chromatographic separation column was Zorbax SB-C18 (4.6X 250mm,5 μm). HPLC mobile phase A was ACN methanol (1:1) and mobile phase B was 0.1% formic acid water. The program is set as follows: 30-70% of solvent A for 10 min;70% of solvent A for 8 min; 100% solvent A,2 min; 30% solvent A, 5 min. The MS analysis parameters were: positive ion, high sensitivity mode; GS1, 50 psi; GS 250 psi; curtain gas, 25 psi; the temperature is 500 ℃; ion spray voltage, 5,500V; CE energy, 35V. + -. 15V.
The results show that the BsCotA-syringaldehyde system is used for fumonisin B1And has no obvious degradation effect.
Sequence listing
<110> institute of feed of Chinese academy of agricultural sciences
Application of syringaldehyde as efficient mediator participating in degradation of mycotoxin by laccase
<160> 1
<170> SIPOSequenceListing 1.0
<210> 1
<211> 513
<212> PRT
<213> Bacillus subtilis
<400> 1
Met Thr Leu Glu Lys Phe Val Asp Ala Leu Pro Ile Pro Asp Thr Leu
1 5 10 15
Lys Pro Val Gln Gln Ser Lys Glu Lys Thr Tyr Tyr Glu Val Thr Met
20 25 30
Glu Glu Cys Thr His Gln Leu His Arg Asp Leu Pro Pro Thr Arg Leu
35 40 45
Trp Gly Tyr Asn Gly Leu Phe Pro Gly Pro Thr Ile Glu Val Lys Arg
50 55 60
Asn Glu Asn Val Tyr Val Lys Trp Met Asn Asn Leu Pro Ser Thr His
65 70 75 80
Phe Leu Pro Ile Asp His Thr Ile His His Ser Asp Ser Gln His Glu
85 90 95
Glu Pro Glu Val Lys Thr Val Val His Leu His Gly Gly Val Thr Pro
100 105 110
Asp Asp Ser Asp Gly Tyr Pro Glu Ala Trp Phe Ser Lys Asp Phe Glu
115 120 125
Gln Thr Gly Pro Tyr Phe Lys Arg Glu Val Tyr His Tyr Pro Asn Gln
130 135 140
Gln Arg Gly Ala Ile Leu Trp Tyr His Asp His Ala Met Ala Leu Thr
145 150 155 160
Arg Leu Asn Val Tyr Ala Gly Leu Val Gly Ala Tyr Ile Ile His Asp
165 170 175
Pro Lys Glu Lys Arg Leu Lys Leu Pro Ser Asp Glu Tyr Asp Val Pro
180 185 190
Leu Leu Ile Thr Asp Arg Thr Ile Asn Glu Asp Gly Ser Leu Phe Tyr
195 200 205
Pro Ser Ala Pro Glu Asn Pro Ser Pro Ser Leu Pro Asn Pro Ser Ile
210 215 220
Val Pro Ala Phe Cys Gly Glu Thr Ile Leu Val Asn Gly Lys Val Trp
225 230 235 240
Pro Tyr Leu Glu Val Glu Pro Arg Lys Tyr Arg Phe Arg Val Ile Asn
245 250 255
Ala Ser Asn Thr Arg Thr Tyr Asn Leu Ser Leu Asp Asn Gly Gly Asp
260 265 270
Phe Ile Gln Ile Gly Ser Asp Gly Gly Leu Leu Pro Arg Ser Val Lys
275 280 285
Leu Asn Ser Phe Ser Leu Ala Pro Ala Glu Arg Tyr Asp Ile Ile Ile
290 295 300
Asp Phe Thr Ala Tyr Glu Gly Glu Ser Ile Ile Leu Ala Asn Ser Ala
305 310 315 320
Gly Cys Gly Gly Asp Val Asn Pro Glu Thr Asp Ala Asn Ile Met Gln
325 330 335
Phe Arg Val Thr Lys Pro Leu Ala Gln Lys Asp Glu Ser Arg Lys Pro
340 345 350
Lys Tyr Leu Ala Ser Tyr Pro Ser Val Gln His Glu Arg Ile Gln Asn
355 360 365
Ile Arg Thr Leu Lys Leu Ala Gly Thr Gln Asp Glu Tyr Gly Arg Pro
370 375 380
Val Leu Leu Leu Asn Asn Lys Arg Trp His Asp Pro Val Thr Glu Thr
385 390 395 400
Pro Lys Val Gly Thr Thr Glu Ile Trp Ser Ile Ile Asn Pro Thr Arg
405 410 415
Gly Thr His Pro Ile His Leu His Leu Val Ser Phe Arg Val Leu Asp
420 425 430
Arg Arg Pro Phe Asp Ile Ala Arg Tyr Gln Glu Ser Gly Glu Leu Ser
435 440 445
Tyr Thr Gly Pro Ala Val Pro Pro Pro Pro Ser Glu Lys Gly Trp Lys
450 455 460
Asp Thr Ile Gln Ala His Ala Gly Glu Val Leu Arg Ile Ala Ala Thr
465 470 475 480
Phe Gly Pro Tyr Ser Gly Arg Tyr Val Trp His Cys His Ile Leu Glu
485 490 495
His Glu Asp Tyr Asp Met Met Arg Pro Met Asp Ile Thr Asp Pro His
500 505 510
Lys

Claims (4)

1. The application of syringaldehyde as a mediator participating in degradation of mycotoxin by laccase, wherein the laccase is from bacillus subtilis, the amino acid sequence of the laccase is shown as SEQ ID No.1, and the mycotoxin is aflatoxin B1And/or zearalenone.
2. The use according to claim 1, wherein the laccase and syringaldehyde degrade mycotoxins in Tris-HCl solution at a concentration of 50mM and a pH of 7.0.
3. A method for improving the degradation rate of a laccase for degrading mycotoxin, which is characterized by comprising the step of using syringaldehyde as a mediator participating in degradation of the mycotoxin by the laccase, wherein the laccase is from bacillus subtilis, the amino acid sequence of the laccase is shown as SEQ ID No.1, and the mycotoxin is aflatoxin B1And/or zearalenone.
4. The method of claim 3, wherein the laccase and syringaldehyde degrade mycotoxins in Tris-HCl solution at a concentration of 50mM and pH 7.0.
CN201910939294.7A 2019-09-30 2019-09-30 Application of syringaldehyde as mediator participating in degradation of mycotoxin by laccase Active CN110637970B (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
CN201910939294.7A CN110637970B (en) 2019-09-30 2019-09-30 Application of syringaldehyde as mediator participating in degradation of mycotoxin by laccase

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
CN201910939294.7A CN110637970B (en) 2019-09-30 2019-09-30 Application of syringaldehyde as mediator participating in degradation of mycotoxin by laccase

Publications (2)

Publication Number Publication Date
CN110637970A CN110637970A (en) 2020-01-03
CN110637970B true CN110637970B (en) 2021-07-20

Family

ID=69011988

Family Applications (1)

Application Number Title Priority Date Filing Date
CN201910939294.7A Active CN110637970B (en) 2019-09-30 2019-09-30 Application of syringaldehyde as mediator participating in degradation of mycotoxin by laccase

Country Status (1)

Country Link
CN (1) CN110637970B (en)

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN113462701B (en) * 2021-09-03 2021-11-26 佛山市玉凰生态环境科技有限公司 High-temperature polyphenol oxidase and application thereof in treatment of phenol-containing wastewater
CN113693189B (en) * 2021-09-28 2023-11-17 中国农业科学院北京畜牧兽医研究所 Application and method of manganese peroxidase for degrading patulin
CN114457063A (en) * 2022-03-11 2022-05-10 安徽黑娃食品科技有限公司 Aspergillus flavus toxin B in degradation peanut1Preparation method of immobilized enzyme
CN115211522B (en) * 2022-07-26 2024-01-26 南昌大学 Method for improving laccase degradation mycotoxin by using tannic acid as mediator
CN115812893A (en) * 2022-08-05 2023-03-21 河南农业大学 Mycotoxin degrading agent for feed and application thereof

Citations (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN1158636A (en) * 1994-09-27 1997-09-03 诺沃挪第克公司 Enhancers such as acetosyringone
CN101903527A (en) * 2007-12-14 2010-12-01 诺维信公司 Process for degrading zearalenone in a feed product employing laccase
CN101959425A (en) * 2008-03-05 2011-01-26 诺维信公司 Detoxification of feed products
CN102310451A (en) * 2010-07-06 2012-01-11 郭明辉 Wood fiber plate prepared on basis of laccase mediator system activation
CN103305536A (en) * 2012-03-08 2013-09-18 浙江商达环保有限公司 Laccase gene, engineering bacteria and application
EP2868632A1 (en) * 2013-10-31 2015-05-06 Da Volterra Method for the inactivation of virginiamycin
CN109820132A (en) * 2018-12-07 2019-05-31 中国农业大学 Application of the bacterial laccase CotA albumen in degradation mycotoxin

Patent Citations (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN1158636A (en) * 1994-09-27 1997-09-03 诺沃挪第克公司 Enhancers such as acetosyringone
CN101903527A (en) * 2007-12-14 2010-12-01 诺维信公司 Process for degrading zearalenone in a feed product employing laccase
CN101959425A (en) * 2008-03-05 2011-01-26 诺维信公司 Detoxification of feed products
CN102310451A (en) * 2010-07-06 2012-01-11 郭明辉 Wood fiber plate prepared on basis of laccase mediator system activation
CN103305536A (en) * 2012-03-08 2013-09-18 浙江商达环保有限公司 Laccase gene, engineering bacteria and application
EP2868632A1 (en) * 2013-10-31 2015-05-06 Da Volterra Method for the inactivation of virginiamycin
CN109820132A (en) * 2018-12-07 2019-05-31 中国农业大学 Application of the bacterial laccase CotA albumen in degradation mycotoxin

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
Aflatoxin B1 and M1 Degradation by Lac2 from Pleurotus pulmonarius and Redox Mediators;Loi, Martina et al.;《Toxins》;20160823;第8卷(第9期);1-16 *
Degradation of Aflatoxin B1 and Zearalenone by Bacterial and Fungal Laccases in Presence of Structurally Defined Chemicals and Complex Natural Mediators;Xiaolu Wang et al.;《toxins》;20191022;第11卷(第10期);1-17 *
In vitro single and combined mycotoxins degradation by Ery4 laccase from Pleurotus eryngii and redox mediators;Loi, Martina et al.;《FOOD CONTROL》;20180314;第90卷;401-406 *

Also Published As

Publication number Publication date
CN110637970A (en) 2020-01-03

Similar Documents

Publication Publication Date Title
CN110637970B (en) Application of syringaldehyde as mediator participating in degradation of mycotoxin by laccase
CN110684748B (en) Application of caffeic acid as mediator for degrading mycotoxin by laccase
Cao et al. A fungal enzyme with the ability of aflatoxin B1 conversion: Purification and ESI-MS/MS identification
CN110373395B (en) Lavender mediator for improving degradation rate of laccase to mycotoxin and application thereof
EP3495477B1 (en) Method for the hydrolysis of zearalenone and/or zearalenone derivatives using a polypeptide and use thereof
Moon et al. Antifungal activity and patterns of N-acetyl-chitooligosaccharide degradation via chitinase produced from Serratia marcescens PRNK-1
CN107012131B (en) Manganese peroxidase, gene thereof and application of manganese peroxidase in mycotoxin detoxification
US20210139864A1 (en) Manganese peroxidase, gene thereof, and use thereof in detoxification of mycotoxin
Ahmed et al. Process optimization of L-glutaminase production; a tumour inhibitor from marine endophytic isolate Aspergillus sp. ALAA-2000
CN110353153B (en) Schizonepeta mediator for improving degradation rate of laccase on mycotoxin and application thereof
KR20110049906A (en) Process for production of optically active amine derivative
Rodríguez et al. Enhancing laccase production by white-rot fungus Funalia floccosa LPSC 232 in co-culture with Penicillium commune GHAIE86
Avelar et al. Recombinant expression of a laccase from Coriolopsis gallica in Pichia pastoris using a modified α-factor preproleader
CN109370995B (en) Manganese peroxidase CsMnP and coding gene and application thereof
CN109504666A (en) Manganese peroxidase PcMnP1 and its encoding gene and application
Lebrun et al. Secretion profiles of fungi as potential tools for metal ecotoxicity assessment: A study of enzymatic system in Trametes versicolor
Zhou et al. Purification and characterization of a urethanase from Penicillium variabile
CN110292105B (en) Cucumber mediator for improving degradation rate of laccase to mycotoxin and application thereof
CN110684754B (en) Mycotoxin ZEN degrading enzyme mutant and application thereof
Siebert et al. Enzymatic hydrolysis of kaempferol 3‐O‐(2‴‐O‐sinapoyl‐β‐sophoroside), the key bitter compound of rapeseed (Brassica napus L.) protein isolate
CN110272878A (en) Laccase TvLac and its encoding gene and application
CN111394336A (en) Zearalenone hydrolase as well as coding gene and application thereof
CN109880883A (en) The application of reactive black 5 and the screening technique of degrading mold toxin enzyme
Swiontek Brzezinska et al. Purification and characterization of Streptomyces albidoflavus antifungal components
CN113699127B (en) Method for improving mycotoxin degradation rate of dye decolorizing peroxidase

Legal Events

Date Code Title Description
PB01 Publication
PB01 Publication
SE01 Entry into force of request for substantive examination
SE01 Entry into force of request for substantive examination
TA01 Transfer of patent application right
TA01 Transfer of patent application right

Effective date of registration: 20200805

Address after: 100193 Beijing Old Summer Palace West Road, Haidian District, No. 2

Applicant after: Beijing Institute of Animal Science and Veterinary Medicine, Chinese Academy of Agricultural Sciences

Address before: 100081 Beijing, Zhongguancun, South Street, No. 12, No.

Applicant before: FEED Research Institute CHINESE ACADEMY OF AGRICULTURAL SCIENCES

GR01 Patent grant
GR01 Patent grant