CN109370995A - Manganese peroxidase CsMnP and its encoding gene and application - Google Patents
Manganese peroxidase CsMnP and its encoding gene and application Download PDFInfo
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Abstract
The invention belongs to agricultural biological technical fields, and in particular to manganese peroxidase CsMnP and its encoding gene and application.Invention provides a kind of manganese peroxidase CsMnP, and amino acid sequence is as shown in SEQ ID No.1 or SEQ ID No.3.Manganese peroxidase of the invention can effectively degrade the mycotoxin of different types of structure, can be used as a kind of novel enzyme preparation, be widely used in food and mycotoxin eliminating feed field.
Description
Technical field
The invention belongs to agricultural biological technical fields, and in particular to manganese peroxidase CsMnP and its encoding gene and answer
With.
Background technique
Mycotoxin is fungal secondary metabolite, harmful to the health of domestic animal, poultry and the mankind.Common mycotoxin
Including aflatoxin, zearalenone, vomitoxin (deoxynivalenol), citrinin, ochratoxin, volt
Horse rhzomorph, patulin and single-ended spore mycotoxin can be divided into tool cyclic structure and not have two toxoids of cyclic structure.Greatly
Most mycotoxins belong in the subgroup of tool cyclic structure such as aflatoxin and zearalenone, usually poly- by fungi
Ketone approach is synthesized.For example, aflatoxin (aflatoxin) B1 is generated by aspergillus flavus (Aspergillus flavus),
The five yuan of carbocyclic rings and two dihydrofuran rings arranged side by side of coumarin ring and two sides with core are that very strong liver causes
Cancer object.In addition, the structure of zearalenone is m-dihydroxy-benzoic acid phenol lactone, fumonisins then has 22 carbon p-aminophenyls
Phenol linear backbone, side chain are two the third three acid.
Physical absorption (or inactivation) and bioconversion are main by two kinds of the detoxicating mycotoxin in food and feed
Mode.In addition to this, using microorganism, especially by the enzyme that microorganism generates, it is a kind of new for carrying out the detoxification of mycotoxin
Emerging means.Laccase, pantoic acid lactone hydrolase, peroxidase and some still unclassified enzymes can lead in the prior art
Peroxidating or Hydrolytic Mechanism aflatoxin degradation and zearalenone.From the manganese peroxidating of lignocellulose degrading bacteria
Object enzyme (MnP) is the enzyme of one group of participation lignin oxidation degradation.A few microorganism producing enzyme disclosed in the prior art is only
Can specificity one to two kinds of mycotoxins such as aflatoxin degradation, zearalenone, therefore, in practical applications by
Greatly limitation.
Summary of the invention
The purpose of the present invention is to provide a kind of manganese peroxidase CsMnP.
A further object of the present invention is to provide the encoding genes of above-mentioned manganese peroxidase CsMnP.
A further object of the present invention is to provide the recombinant expression carriers for containing above-mentioned encoding gene.
A further object of the present invention is to provide the recombinant bacterial strains for containing above-mentioned encoding gene.
A further object of the present invention is to provide the preparation methods of above-mentioned manganese peroxidase CsMnP.
A further object of the present invention is to provide the applications of above-mentioned manganese peroxidase CsMnP.
The manganese peroxidase CsMnP of wild type of the invention, amino acid sequence is as shown in SEQ ID No.1:
MAFTSFVALAALVGIASAAPTTICPDGTRVSNHACCAFIPLAEDLQKTIFMNDCGEDAHEVIRLTFHDA
VAISRKLGPKAGGGADGSMLLFPTVEPNFSANNGIDDSVNNLIPFMARHPTVSAGDLVQFAGAVALSNCPGAPRLEF
LAGRPNHTIAAIDGLIPEPQDDVTKILERFDDAGGFTPFEVVSLLASHTVARADKVDETIDAAPFDSTPFTFDTQVF
LEVLLKGVGFPGTDNNTGEVASPLPKGSGNDTGEMRLQSDFALARDPRTACFWQGFVDEQEFMAESFKAAMAKLAIL
GHNRASLTDCSDVVPIPRPAVKKPASFPATTGPKDLELTCRAERFPTLTVDRGAVQALIPHCSNGGQDCPSVQFDGP
A
Wherein, which encodes 379 amino acid, and 18 amino acid of N-terminal are its signal peptide sequence, the sequence of signal peptide
As shown in SEQ ID No.2:
MAFTSFVALAALVGIASA
Therefore, the theoretical molecular weight of mature manganese peroxidase CsMnP is 38.3kDa, amino acid sequence such as SEQ
Shown in ID No.3:
APTTICPDGTRVSNHACCAFIPLAEDLQKTIFMNDCGEDAHEVIRLTFHDAVAISRKLGPKAGGGADGS
MLLFPTVEPNFSANNGIDDSVNNLIPFMARHPTVSAGDLVQFAGAVALSNCPGAPRLEFLAGRPNHTIAAIDGLIPE
PQDDVTKILERFDDAGGFTPFEVVSLLASHTVARADKVDETIDAAPFDSTPFTFDTQVFLEVLLKGVGFPGTDNNTG
EVASPLPKGSGNDTGEMRLQSDFALARDPRTACFWQGFVDEQEFMAESFKAAMAKLAILGHNRASLTDCSDVVPIPR
PAVKKPASFPATTGPKDLELTCRAERFPTLTVDRGAVQALIPHCSNGGQDCPSVQFDGPA
The present invention also provides the gene order for encoding above-mentioned manganese peroxidase CsMnP, genome sequence such as SEQ
Shown in ID No.4:
Atggcctttaccagctttgttgcactggcagcactggttggtattgcaagcgcagcaccgaccaccat
ttgtccggatggcacccgtgttagcaatcatgcatgttgtgcatttattccgctggcagaagatctgcagaaaacc
atttttatgaacgattgtggtgaagatgcccatgaagttattcgtctgacctttcatgatgcagttgcaattagcc
gtaaactgggtccgaaagccggtggtggtgcagatggtagcatgctgctgtttccgaccgttgaaccgaattttag
cgcaaataatggcattgatgatagcgtgaataacctgattccgtttatggcacgtcatccgaccgtgagtgccggt
gatctggttcagtttgccggtgcagttgccctgagcaattgtccgggtgcaccgcgtctggaatttctggcaggtc
gtccgaatcataccattgcagcaattgatggtctgattccggaaccgcaggatgatgttaccaaaattctggaacg
ttttgatgatgccggtggttttaccccgtttgaagttgttagcctgctggcaagccataccgttgcacgtgccgat
aaagttgatgaaaccattgatgcagcaccgtttgatagcaccccgtttacctttgatacccaggtttttctggaag
ttctgctgaaaggtgttggttttccgggtacagataataacaccggtgaagttgcaagtccgctgccgaaaggtag
cggtaatgataccggtgaaatgcgtctgcagagcgattttgccctggcacgcgatccgcgtaccgcatgtttttgg
cagggttttgttgatgaacaagaatttatggccgagtcctttaaagcagcaatggcaaaactggcaattctgggtc
ataatcgtgcaagcctgaccgattgtagtgatgttgttccgattccgcgtccggcagttaaaaaaccggcaagttt
tccggcaaccaccggtcctaaagatctggaactgacctgtcgtgcagaacgttttccgaccctgaccgttgatcgt
ggtgcagttcaggcactgattccgcattgtagcaatggtggccaggattgtccgagcgtgcagtttgatggtccgg
cataa
Manganese peroxidase CsMnP coding gene sequence overall length 1137bp.Wherein, the base sequence of signal peptide such as SEQ ID
Shown in No.5:
Atggcctttaccagctttgttgcactggcagcactggttggtattgcaagcgca
CDNA (the removing signal peptide) sequence of mature manganese peroxidase CsMnP is as shown in SEQ ID No.6:
Gcaccgaccaccatttgtccggatggcacccgtgttagcaatcatgcatgttgtgcatttattccgct
ggcagaagatctgcagaaaaccatttttatgaacgattgtggtgaagatgcccatgaagttattcgtctgaccttt
catgatgcagttgcaattagccgtaaactgggtccgaaagccggtggtggtgcagatggtagcatgctgctgtttc
cgaccgttgaaccgaattttagcgcaaataatggcattgatgatagcgtgaataacctgattccgtttatggcacg
tcatccgaccgtgagtgccggtgatctggttcagtttgccggtgcagttgccctgagcaattgtccgggtgcaccg
cgtctggaatttctggcaggtcgtccgaatcataccattgcagcaattgatggtctgattccggaaccgcaggatg
atgttaccaaaattctggaacgttttgatgatgccggtggttttaccccgtttgaagttgttagcctgctggcaag
ccataccgttgcacgtgccgataaagttgatgaaaccattgatgcagcaccgtttgatagcaccccgtttaccttt
gatacccaggtttttctggaagttctgctgaaaggtgttggttttccgggtacagataataacaccggtgaagttg
caagtccgctgccgaaaggtagcggtaatgataccggtgaaatgcgtctgcagagcgattttgccctggcacgcga
tccgcgtaccgcatgtttttggcagggttttgttgatgaacaagaatttatggccgagtcctttaaagcagcaatg
gcaaaactggcaattctgggtcataatcgtgcaagcctgaccgattgtagtgatgttgttccgattccgcgtccgg
cagttaaaaaaccggcaagttttccggcaaccaccggtcctaaagatctggaactgacctgtcgtgcagaacgttt
tccgaccctgaccgttgatcgtggtgcagttcaggcactgattccgcattgtagcaatggtggccaggattgtccg
agcgtgcagtttgatggtccggcataa
The present invention also provides the recombinant vector comprising above-mentioned manganese peroxidase gene C sMnP, preferably pCold I-
CsMnP.Manganese peroxidase enzyme gene of the invention is inserted between suitable restriction enzyme cleavage sites of the expression vector, its core is made
Nucleotide sequence is operable to be linked to the expression control sequence.As the most preferred embodiment of the invention, this is sent out
Bright manganese peroxidase gene C sMnP is inserted between the NdeI-BamHI restriction enzyme site on plasmid pCold I, is made
The nucleotide sequence is located at the downstream of CSPA promoter and is regulated and controled by it, obtains expression of recombinant e. coli plasmid pCold I-
CsMnP。
The present invention also provides the recombinant bacterial strains comprising above-mentioned manganese peroxidase gene C sMnP, preferably recombination large intestine
Bacillus strain BL21 (DE3)/CsMnP.
The present invention also provides a kind of methods for preparing manganese peroxidase CsMnP, comprising the following steps:
(1) host cell is converted with above-mentioned recombinant vector, obtains recombinant bacterial strain；
(2) recombinant bacterial strain is cultivated, induction recombination manganese peroxidase expresses；
(3) manganese peroxidase CsMnP is purified.
The present invention provides the applications of above-mentioned manganese peroxidase CsMnP, especially in terms of detoxicating mycotoxin of degrading,
It has good degradation rate to aflatoxin B1, zearalenone, vomitoxin, fumonisins B1.
Detailed description of the invention
Fig. 1 display recombination manganese peroxidase CsMnP is to aflatoxin B1, zearalenone, vomitoxin, volt horse
The degradation rate of rhzomorph B1；
The HPLC of Fig. 2 display recombination manganese peroxidase CsMnP degrading aflatoxin B 1 analyzes result；
The HPLC of Fig. 3 display recombination manganese peroxidase CsMnP degrading zearalenone analyzes result；
The HPLC of Fig. 4 display recombination manganese peroxidase CsMnP degradation vomitoxin analyzes result；
The HPLC of Fig. 5 display recombination manganese peroxidase CsMnP degrading fumonisins B1 analyzes result.
Specific embodiment
Test material and reagent
1, gene and carrier: coli expression carrier pCold I and bacterial strain BL21 (DE3)；
2, enzyme and other biochemical reagents: restriction endonuclease, recombinase, aflatoxin B1, zearalenone and vomiting poison
Element, fumonisins.
3, culture medium: Escherichia coli culture medium LB (1% peptone, 0.5% yeast extract, 1%NaCl, pH7.0).It is real
Apply the clone of 1 manganese peroxidase CsMnP encoding gene of example
The object of the invention gene source intends wax bacterium (Ceriporiopsis in On Polyporaceae worm
subvermispora)。
Design specific primer:
CsMnP-F:5'-CATATCGAAGGTAGGCATATGGCACCGACCACCAT-3'；
CsMnP-R:5'-GACAAGCTTGAATTCGGATCCTGCCGGACCATCAA-3'。
PCR amplification is carried out by template of the plasmid with target gene.The electrophoresis on 1% Ago-Gel is cut glue and is obtained
Target fragment will be connected with the pCold I carrier of NdeI-BamHI double digestion by the method for homologous recombination after segment recycling,
TransI cloning host is converted, sequence verification obtains oxide enzyme CsMnP encoding gene.
The preparation of the recombination of embodiment 2 manganese peroxidase CsMnP
By the expression of recombinant e. coli plasmid pCold I-CsMnP containing manganese peroxidase gene C sMnP of acquisition
It converts e. coli bl21 (DE3), obtains recombinant escherichia coli strain BL21 (DE3)/CsMnP.
The recombinant expression carrier of the manganese peroxidase gene C sMnP containing signal peptide sequence is constructed in the same way.
BL21 (DE3)/CsMnP bacterial strain containing recombinant plasmid is taken, is inoculated in 50mL LB culture solution, 37 DEG C of 220rpm
After shaken cultivation 12h, in the switching of 2% ratio in 300mL LB culture medium, 37 DEG C of 220rpm shaken cultivations about 2h (OD590 ≈
0.5).The inducer IPTG of 60 μ L concentration 1M is added after ice-water bath processing after 10 DEG C of 220rpm are cultivated 30 minutes, in 10 DEG C
220rpm continues to cultivate 6h.The CaCl of 33 μ L concentration 1M is added in 9h incubation per hour later2, 330 μ L concentration 10g/L's
Hemin (Hemin is dissolved in 0.1M NaOH).10 DEG C of 220rpm continue cultivate 10h after thalline were collected by centrifugation.Take ultrasonic method method
Thallus is cracked, affinitive layer purification is carried out using nickel column and obtains single CsMnP albumen.
Embodiment 3 recombinates manganese peroxidase CsMnP degrading aflatoxin B 1
Aflatoxin B1 is dissolved into the mother liquor that 50mg/L is configured in dimethyl sulfoxide, by following reaction system: 70 μ
L malonic acid buffer (0.2M, pH 5.0), 20 μ L aflatoxin B1 solution (50mg/L), 5 μ L manganese sulfates (40mM), 100 μ L
Manganese peroxidase (1000U/L), 5 μ L hydrogen peroxide (4mM).System manganese peroxidase not to be added is reacted as control
System sets 3 repetitions.Reaction carries out at 30 DEG C, and the methanol that three times volume is added after 48h terminates reaction, using high-efficient liquid phase color
Compose the degradation rate of (HPLC) analysis aflatoxin B1.Liquid chromatogram is Shimadzu Nexera UHPLC efficient liquid phase chromatographic analysis system
System, chromatography column are Zorbax SB-C18 (4.6 × 250mm, 5 μm), mobile phase A (water of 0.06%TFA), Mobile phase B
(acetonitrile of 0.05%TFA)；Condition of gradient elution 0%B is eluted 4 minutes, and 0%-100%B is eluted 15 minutes, 100%B elution 6
Minute；Detection wavelength 365nm.
As a result as shown in Figure 1 and Figure 2, it is seen that most of aflatoxin has been degraded, degradation rate 80.8%.
Embodiment 4 recombinates manganese peroxidase CsMnP degrading zearalenone
Zearalenone is dissolved into the mother liquor that 50mg/L is configured in dimethyl sulfoxide, by following reaction system: 70 μ
L malonic acid buffer (0.2M, pH 5.0), 20 μ L zearalenone solution (50mg/L), 5 μ L manganese sulfates (40mM), 100 μ L
Manganese peroxidase (1000U/L), 5 μ L hydrogen peroxide (4mM).System manganese peroxidase not to be added is reacted as control
System sets 3 repetitions.Reaction carries out at 30 DEG C, and the methanol that three times volume is added after 48h terminates reaction, using high-efficient liquid phase color
Compose the degradation rate of (HPLC) analysis zearalenone.Liquid chromatogram is Shimadzu Nexera UHPLC efficient liquid phase chromatographic analysis system
System, chromatography column are Zorbax SB-C18 (4.6 × 250mm, 5 μm), mobile phase A (water of 0.06%TFA), Mobile phase B
(acetonitrile of 0.05%TFA)；Condition of gradient elution 0%B is eluted 4 minutes, and 0%-100%B is eluted 15 minutes, 100%B elution 6
Minute；Detection wavelength 316nm.
As a result as shown in Figure 1, Figure 3, it is seen that most of zearalenone has been degraded, degradation rate 78.9%.
Embodiment 5 recombinates manganese peroxidase CsMnP degradation vomitoxin
Vomitoxin is dissolved into the mother liquor that 100mg/L is configured in methanol, by following reaction system: 70 μ L malonic acid are slow
Fliud flushing (0.2M, pH 5.0), 20 μ L vomitoxin solution (100mg/L), 5 μ L manganese sulfates (40mM), 100 μ L manganese peroxidases
(1000U/L), 5 μ L hydrogen peroxide (4mM).The system of manganese peroxidase not to be added as control, reaction system sets 3 weights
It is multiple.Reaction carries out at 30 DEG C, and the methanol that three times volume is added after 48h terminates reaction, using high performance liquid chromatography (HPLC) point
Analyse the degradation rate of vomitoxin.Liquid chromatogram is Shimadzu Nexera UHPLC efficient liquid phase chromatographic analysis system, chromatography column
For Zorbax SB-C18 (4.6 × 250mm, 5 μm), mobile phase A (water), Mobile phase B (methanol)；Condition of gradient elution 20%B is washed
20 minutes de-, 20%-100%B is eluted 1 minute, and 100%B is eluted 6 minutes；Detection wavelength 220nm.
As a result as Figure 1 and Figure 4, it is seen that most of vomitoxin has been degraded, degradation rate 86.3%.
Embodiment 6 recombinates manganese peroxidase CsMnP degrading fumonisins B1
Fumonisins B1 is dissolved into the mother liquor that 100mg/L is configured in DMSO, by following reaction system: 70 μ L malonic acid
Buffer (0.2M, pH 5.0), 20 μ L fumonisins B1 solution (100mg/L), 5 μ L manganese sulfates (40mM), 100 μ L manganese peroxidating
Enzyme (1000U/L), 5 μ L hydrogen peroxide (4mM).The system of manganese peroxidase not to be added as control, reaction system sets 3
It repeats.Reaction carries out at 30 DEG C, and the methanol that three times volume is added after 48h terminates reaction, using high performance liquid chromatography (HPLC)-
The degradation rate of mass spectrum (MS) combination analysis fumonisins B1.Liquid chromatogram is Shimadzu Nexera UHPLC efficient liquid phase chromatographic analysis
System, chromatography column are Zorbax SB-C18 (4.6X 250,5um), mobile phase A (water of 0.1% formic acid), Mobile phase B
(acetonitrile: methanol 1:1)；Condition of gradient elution 30%-100%B gradient elution 10 minutes, 30%B are eluted 18 minutes, and 100%B is washed
It is 2 minutes de-；Mass spectrum is SCIEX Triple TOF analysis system, and Mass Spectrometry Conditions are CE:35V ± 15V, Ion source gas:
50, TEM 500 DEG C, ISVF 5500V, sean:m/z 100-1000 (object 721).
As a result as shown in Figure 1, shown in Figure 5, it is seen that part fumonisins has been degraded, degradation rate 21.3%.
Sequence table
<110>Institute of Feeds,China Academy of Agriculture Sciences
<120>manganese peroxidase CsMnP and its encoding gene and application
<160> 6
<170> SIPOSequenceListing 1.0
<210> 2
<211> 378
<212> PRT
<213>on Polyporaceae worm intends wax bacterium (Ceriporiopsis subvermispora)
<400> 2
Met Ala Phe Thr Ser Phe Val Ala Leu Ala Ala Leu Val Gly Ile Ala
1 5 10 15
Ser Ala Ala Pro Thr Thr Ile Cys Pro Asp Gly Thr Arg Val Ser Asn
20 25 30
His Ala Cys Cys Ala Phe Ile Pro Leu Ala Glu Asp Leu Gln Lys Thr
35 40 45
Ile Phe Met Asn Asp Cys Gly Glu Asp Ala His Glu Val Ile Arg Leu
50 55 60
Thr Phe His Asp Ala Val Ala Ile Ser Arg Lys Leu Gly Pro Lys Ala
65 70 75 80
Gly Gly Gly Ala Asp Gly Ser Met Leu Leu Phe Pro Thr Val Glu Pro
85 90 95
Asn Phe Ser Ala Asn Asn Gly Ile Asp Asp Ser Val Asn Asn Leu Ile
100 105 110
Pro Phe Met Ala Arg His Pro Thr Val Ser Ala Gly Asp Leu Val Gln
115 120 125
Phe Ala Gly Ala Val Ala Leu Ser Asn Cys Pro Gly Ala Pro Arg Leu
130 135 140
Glu Phe Leu Ala Gly Arg Pro Asn His Thr Ile Ala Ala Ile Asp Gly
145 150 155 160
Leu Ile Pro Glu Pro Gln Asp Asp Val Thr Lys Ile Leu Glu Arg Phe
165 170 175
Asp Asp Ala Gly Gly Phe Thr Pro Phe Glu Val Val Ser Leu Leu Ala
180 185 190
Ser His Thr Val Ala Arg Ala Asp Lys Val Asp Glu Thr Ile Asp Ala
195 200 205
Ala Pro Phe Asp Ser Thr Pro Phe Thr Phe Asp Thr Gln Val Phe Leu
210 215 220
Glu Val Leu Leu Lys Gly Val Gly Phe Pro Gly Thr Asp Asn Asn Thr
225 230 235 240
Gly Glu Val Ala Ser Pro Leu Pro Lys Gly Ser Gly Asn Asp Thr Gly
245 250 255
Glu Met Arg Leu Gln Ser Asp Phe Ala Leu Ala Arg Asp Pro Arg Thr
260 265 270
Ala Cys Phe Trp Gln Gly Phe Val Asp Glu Gln Glu Phe Met Ala Glu
275 280 285
Ser Phe Lys Ala Ala Met Ala Lys Leu Ala Ile Leu Gly His Asn Arg
290 295 300
Ala Ser Leu Thr Asp Cys Ser Asp Val Val Pro Ile Pro Arg Pro Ala
305 310 315 320
Val Lys Lys Pro Ala Ser Phe Pro Ala Thr Thr Gly Pro Lys Asp Leu
325 330 335
Glu Leu Thr Cys Arg Ala Glu Arg Phe Pro Thr Leu Thr Val Asp Arg
340 345 350
Gly Ala Val Gln Ala Leu Ile Pro His Cys Ser Asn Gly Gly Gln Asp
355 360 365
Cys Pro Ser Val Gln Phe Asp Gly Pro Ala
370 375
<210> 2
<211> 18
<212> PRT
<213>on Polyporaceae worm intends wax bacterium (Ceriporiopsis subvermispora)
<400> 2
Met Ala Phe Thr Ser Phe Val Ala Leu Ala Ala Leu Val Gly Ile Ala
1 5 10 15
Ser Ala
<210> 3
<211> 360
<212> PRT
<213>on Polyporaceae worm intends wax bacterium (Ceriporiopsis subvermispora)
<400> 3
Ala Pro Thr Thr Ile Cys Pro Asp Gly Thr Arg Val Ser Asn His Ala
1 5 10 15
Cys Cys Ala Phe Ile Pro Leu Ala Glu Asp Leu Gln Lys Thr Ile Phe
20 25 30
Met Asn Asp Cys Gly Glu Asp Ala His Glu Val Ile Arg Leu Thr Phe
35 40 45
His Asp Ala Val Ala Ile Ser Arg Lys Leu Gly Pro Lys Ala Gly Gly
50 55 60
Gly Ala Asp Gly Ser Met Leu Leu Phe Pro Thr Val Glu Pro Asn Phe
65 70 75 80
Ser Ala Asn Asn Gly Ile Asp Asp Ser Val Asn Asn Leu Ile Pro Phe
85 90 95
Met Ala Arg His Pro Thr Val Ser Ala Gly Asp Leu Val Gln Phe Ala
100 105 110
Gly Ala Val Ala Leu Ser Asn Cys Pro Gly Ala Pro Arg Leu Glu Phe
115 120 125
Leu Ala Gly Arg Pro Asn His Thr Ile Ala Ala Ile Asp Gly Leu Ile
130 135 140
Pro Glu Pro Gln Asp Asp Val Thr Lys Ile Leu Glu Arg Phe Asp Asp
145 150 155 160
Ala Gly Gly Phe Thr Pro Phe Glu Val Val Ser Leu Leu Ala Ser His
165 170 175
Thr Val Ala Arg Ala Asp Lys Val Asp Glu Thr Ile Asp Ala Ala Pro
180 185 190
Phe Asp Ser Thr Pro Phe Thr Phe Asp Thr Gln Val Phe Leu Glu Val
195 200 205
Leu Leu Lys Gly Val Gly Phe Pro Gly Thr Asp Asn Asn Thr Gly Glu
210 215 220
Val Ala Ser Pro Leu Pro Lys Gly Ser Gly Asn Asp Thr Gly Glu Met
225 230 235 240
Arg Leu Gln Ser Asp Phe Ala Leu Ala Arg Asp Pro Arg Thr Ala Cys
245 250 255
Phe Trp Gln Gly Phe Val Asp Glu Gln Glu Phe Met Ala Glu Ser Phe
260 265 270
Lys Ala Ala Met Ala Lys Leu Ala Ile Leu Gly His Asn Arg Ala Ser
275 280 285
Leu Thr Asp Cys Ser Asp Val Val Pro Ile Pro Arg Pro Ala Val Lys
290 295 300
Lys Pro Ala Ser Phe Pro Ala Thr Thr Gly Pro Lys Asp Leu Glu Leu
305 310 315 320
Thr Cys Arg Ala Glu Arg Phe Pro Thr Leu Thr Val Asp Arg Gly Ala
325 330 335
Val Gln Ala Leu Ile Pro His Cys Ser Asn Gly Gly Gln Asp Cys Pro
340 345 350
Ser Val Gln Phe Asp Gly Pro Ala
355 360
<210> 4
<211> 1137
<212> DNA
<213>on Polyporaceae worm intends wax bacterium (Ceriporiopsis subvermispora)
<400> 4
atggccttta ccagctttgt tgcactggca gcactggttg gtattgcaag cgcagcaccg 60
accaccattt gtccggatgg cacccgtgtt agcaatcatg catgttgtgc atttattccg 120
ctggcagaag atctgcagaa aaccattttt atgaacgatt gtggtgaaga tgcccatgaa 180
gttattcgtc tgacctttca tgatgcagtt gcaattagcc gtaaactggg tccgaaagcc 240
ggtggtggtg cagatggtag catgctgctg tttccgaccg ttgaaccgaa ttttagcgca 300
aataatggca ttgatgatag cgtgaataac ctgattccgt ttatggcacg tcatccgacc 360
gtgagtgccg gtgatctggt tcagtttgcc ggtgcagttg ccctgagcaa ttgtccgggt 420
gcaccgcgtc tggaatttct ggcaggtcgt ccgaatcata ccattgcagc aattgatggt 480
ctgattccgg aaccgcagga tgatgttacc aaaattctgg aacgttttga tgatgccggt 540
ggttttaccc cgtttgaagt tgttagcctg ctggcaagcc ataccgttgc acgtgccgat 600
aaagttgatg aaaccattga tgcagcaccg tttgatagca ccccgtttac ctttgatacc 660
caggtttttc tggaagttct gctgaaaggt gttggttttc cgggtacaga taataacacc 720
ggtgaagttg caagtccgct gccgaaaggt agcggtaatg ataccggtga aatgcgtctg 780
cagagcgatt ttgccctggc acgcgatccg cgtaccgcat gtttttggca gggttttgtt 840
gatgaacaag aatttatggc cgagtccttt aaagcagcaa tggcaaaact ggcaattctg 900
ggtcataatc gtgcaagcct gaccgattgt agtgatgttg ttccgattcc gcgtccggca 960
gttaaaaaac cggcaagttt tccggcaacc accggtccta aagatctgga actgacctgt 1020
cgtgcagaac gttttccgac cctgaccgtt gatcgtggtg cagttcaggc actgattccg 1080
cattgtagca atggtggcca ggattgtccg agcgtgcagt ttgatggtcc ggcataa 1137
<210> 5
<211> 54
<212> DNA
<213>on Polyporaceae worm intends wax bacterium (Ceriporiopsis subvermispora)
<400> 5
atggccttta ccagctttgt tgcactggca gcactggttg gtattgcaag cgca 54
<210> 6
<211> 1083
<212> DNA
<213>on Polyporaceae worm intends wax bacterium (Ceriporiopsis subvermispora)
<400> 6
gcaccgacca ccatttgtcc ggatggcacc cgtgttagca atcatgcatg ttgtgcattt 60
attccgctgg cagaagatct gcagaaaacc atttttatga acgattgtgg tgaagatgcc 120
catgaagtta ttcgtctgac ctttcatgat gcagttgcaa ttagccgtaa actgggtccg 180
aaagccggtg gtggtgcaga tggtagcatg ctgctgtttc cgaccgttga accgaatttt 240
agcgcaaata atggcattga tgatagcgtg aataacctga ttccgtttat ggcacgtcat 300
ccgaccgtga gtgccggtga tctggttcag tttgccggtg cagttgccct gagcaattgt 360
ccgggtgcac cgcgtctgga atttctggca ggtcgtccga atcataccat tgcagcaatt 420
gatggtctga ttccggaacc gcaggatgat gttaccaaaa ttctggaacg ttttgatgat 480
gccggtggtt ttaccccgtt tgaagttgtt agcctgctgg caagccatac cgttgcacgt 540
gccgataaag ttgatgaaac cattgatgca gcaccgtttg atagcacccc gtttaccttt 600
gatacccagg tttttctgga agttctgctg aaaggtgttg gttttccggg tacagataat 660
aacaccggtg aagttgcaag tccgctgccg aaaggtagcg gtaatgatac cggtgaaatg 720
cgtctgcaga gcgattttgc cctggcacgc gatccgcgta ccgcatgttt ttggcagggt 780
tttgttgatg aacaagaatt tatggccgag tcctttaaag cagcaatggc aaaactggca 840
attctgggtc ataatcgtgc aagcctgacc gattgtagtg atgttgttcc gattccgcgt 900
ccggcagtta aaaaaccggc aagttttccg gcaaccaccg gtcctaaaga tctggaactg 960
acctgtcgtg cagaacgttt tccgaccctg accgttgatc gtggtgcagt tcaggcactg 1020
attccgcatt gtagcaatgg tggccaggat tgtccgagcg tgcagtttga tggtccggca 1080
taa 1083
Claims (8)
1. manganese peroxidase CsMnP, which is characterized in that its amino acid sequence such as SEQ ID No.1 or SEQ ID No.3 institute
Show.
2. manganese peroxidase CsMnP gene, which is characterized in that it encodes manganese peroxidase described in claim 1
CsMnP。
3. manganese peroxidase CsMnP gene according to claim 2, which is characterized in that its nucleotide sequence such as SEQ
Shown in ID No.4 or SEQ ID No.6.
4. including the recombinant expression carrier of manganese peroxidase CsMnP gene as claimed in claim 2.
5. including the recombinant bacterial strain of manganese peroxidase CsMnP gene as claimed in claim 2.
6. the method for preparing manganese peroxidase CsMnP described in claim 1, which is characterized in that the method includes following
Step:
(1) host cell is converted with comprising the recombinant expression carrier for encoding manganese peroxidase CsMnP gene, obtains recombinant bacterium
Strain；
(2) recombinant bacterial strain, induction manganese peroxidase CsMnP expression are cultivated；
(3) the manganese peroxidase CsMnP is isolated and purified.
7. the application of manganese peroxidase CsMnP described in claim 1.
8. application of the manganese peroxidase CsMnP described in claim 1 in terms of detoxicating mycotoxin.
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