CN108103048A - Low-temperature matrix metalloproteinase and coding gene and application thereof - Google Patents
Low-temperature matrix metalloproteinase and coding gene and application thereof Download PDFInfo
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- CN108103048A CN108103048A CN201711172228.9A CN201711172228A CN108103048A CN 108103048 A CN108103048 A CN 108103048A CN 201711172228 A CN201711172228 A CN 201711172228A CN 108103048 A CN108103048 A CN 108103048A
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- matrix metalloproteinase
- low temperature
- temperature matrix
- protein
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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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6489—Metalloendopeptidases (3.4.24)
- C12N9/6491—Matrix metalloproteases [MMP's], e.g. interstitial collagenase (3.4.24.7); Stromelysins (3.4.24.17; 3.2.1.22); Matrilysin (3.4.24.23)
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- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Life Sciences & Earth Sciences (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Genetics & Genomics (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Abstract
The invention discloses a low-temperature matrix metalloproteinase and a coding gene and application thereof. The invention firstly discloses a low-temperature matrix metalloproteinase, which is a protein shown in the following (a) or (b): (a) a protein consisting of an amino acid sequence shown in a sequence table SEQ ID NO. 1; (b) the protein with the protein degradation activity under the low temperature condition is obtained by substituting and/or deleting and/or inserting one or more amino acid residues in an amino acid sequence shown in a sequence table SEQ ID NO. 1. The invention further discloses application of the low-temperature matrix metalloproteinase in degrading proteins under a low-temperature condition. The low-temperature matrix metalloproteinase still has high-efficiency protein degradation activity at the low temperature of 10-20 ℃, and has a low heat inactivation temperature.
Description
Technical field
The present invention relates to enzyme engineering fields.More particularly, to a kind of low temperature matrix metalloproteinase and its encoding gene
With application.
Background technology
Matrix metalloproteinase is that a major class needs Ca2+、Zn2+Metal ions are waited as confactor, at the same it is degradable
The protease of various kinds of cell epimatrix composition (collagen, gelatin, viscous protein, fibronectin, proteoglycan etc.).With it
Middle a kind of matrix metalloproteinase with collagen degrading activity is widely used in the industries such as light industry production, health care.
Clostridiopetidase A can be used as the dyeing assistant of leather, have with it to collagenous fibres matrix certain catalytic activity from
And the dyeability of leather can be improved.Leather is a kind of material being made of collagen, right with a variety of crosslinking agents (such as chromium)
After collagen carries out tanning, structures change after reacting generation chemical crosslinking with tanning agent due to collagen.Combination of the enzyme to its substrate
With very high specificity, thus skin will not generate comprehensive hydrolysis after chrome tanning using clostridiopetidase A, collagen, but leather can be made fine
The net structure of dimension becomes more to stretch, and so as to promote infiltration of the dyestuff to grass fiber inside configuration, while also increases leather
With the bare area of dye contacts, and then the coloring of leather is improved.
Medically, the interverbebral disc the dissolving skill developed using clostridiopetidase A be used to treat the diseases such as protrusion of lumber intervertebral disc.In shadow
As under equipment guiding, clostridiopetidase A being injected into exactly in prominent interverbebral disc and its around, it is fine to decompose collagen by clostridiopetidase A
Collagen tissue is dissolved in the pharmacological action of dimension, and protrusion is made to reduce or disappear, to alleviate or eliminate its compressing to nerve fiber,
Achieve the effect that similar with surgical removal of disc protrusion.Clostridiopetidase A is a kind of enzyme of main dissolving collagen, can be effective
Ground dissolves nucleus pulposus and I type and II Collagen Type VI in fibrous ring, the collagenase solution equal with tissue osmotic pressure do not destroy group
Cell and nerve cell are knitted, it is harmless to albumen such as hemoglobin, milk casein, keratan sulfates.
Large-scale application and commercialized clostridiopetidase A is essentially from microorganism (clostridium histolyticum) and land at present
Raw mammal (ox, pig etc.), is room temperature protease, most suitable catalytic temperature is at 30~40 DEG C.And with low temperature collagen hydro
The rare report of matrix metalloproteinase of activity, and it is low-temperature catalyzed compared to constant temperature catalyzing, there is its unique technical advantage, body
Now：
(1) low-temperature catalyzed reduction enzyme reaction temperature, can effectively realize the energy-saving of technique.Before leather coloring
Exemplified by reason, as can in realizing low temperature clostridiopetidase A pre-treatment, will save in cylinder body and heat the energy consumption input of (usual 40 DEG C), and save
The equipment investment that heat transfer with constant temperature is maintained in cylinder body is saved；
(2) low reaction temperatures and the inactivation temperature of corresponding enzyme reduce, and will substantially reduce the non-of side reaction or product
Selective degradation mitigates the injury to handling sample.Disappeared with clostridiopetidase A for the histocyte of mammaliancellculture early period
Exemplified by solution, such as in 37 DEG C of progress, zooblast is in active state, lacks effective oxygen supply in reaction process the digestion process,
Cell is caused to carry out anaerobic respiration, largely generates and accumulates the metabolic by-products such as lactic acid, damages the work of subsequent cell incubation
Property.And if can introduce low temperature clostridiopetidase A substitutes traditional room temperature clostridiopetidase A, the reduction of reaction temperature will significantly be alleviated above-mentioned
Byproducts build-up in the process, so as to improve cell culture activity.
Therefore it provides a kind of matrix metalloproteinase with collagen degrading activity under cryogenic should with important
With value.
The content of the invention
It is an object of the present invention to provide a kind of low temperature matrix metalloproteinase and its encoding gene, which can be
There is protein degradation activity under cryogenic conditions.
It is another object of the present invention to provide the applications of above-mentioned low temperature matrix metalloproteinase.
In order to achieve the above objectives, the present invention uses following technical proposals：
The present invention provides a kind of low temperature matrix metalloproteinase, is named as nrMMP14, from Roche Antarctic Fish
(Notothenia rossii)；The low temperature matrix metalloproteinase is the protein shown in following (a) or (b)：
(a) protein being made of the amino acid sequence shown in sequence table SEQ ID NO.1；
(b) as the amino acid sequence shown in sequence table SEQ ID NO.1 by the substitution of one or more amino acid residues
And/or the protein with albumen degrading activity under cryogenic conditions that missing and/or insertion obtain.
Wherein, amino acid sequence described in the sequence table SEQ ID NO.1 is made of 491 amino acid residues.
The encoding gene of above-mentioned low temperature matrix metalloproteinase falls within protection scope of the present invention in the present invention, described
Encoding gene is such as shown in (a) or (b)：
(a) nucleotide sequence as shown in sequence table SED ID NO.2；
(b) nucleotide sequence of coding amino acid sequence as shown in sequence table SED ID NO.1.
Wherein, 1473 base compositions of the nucleotide sequence shown in sequence table SEQ ID NO.2, coded sequence are from 5 '
The the 1st to the 1473rd bit base is held, encodes the protein of the amino acid sequence as shown in sequence table SED ID NO.1.
It should be noted that expression vector, cell line, engineering bacteria and host strain containing the above-mentioned encoding gene of the present invention are equal
It belongs to the scope of protection of the present invention.
The present invention also provides a kind of methods for expressing the low temperature matrix metalloproteinase, and being will be containing above-mentioned low temperature base
The recombinant expression carrier of matter metalloprotein enzyme coding gene imports host cell, and expression obtains low temperature matrix metalloproteinase.
Wherein, the host can be Escherichia coli, saccharomycete, mammal, insect, hay bacillus, bacillus or breast
Bacillus etc. is preferably saccharomycete.
The saccharomycete is preferably Pasteur's moral Pichia pastoris (Pichia pastoris), such as Pasteur's moral Pichia pastoris
X33。
The carrier that sets out for building the expression of recombinant e. coli carrier and recombinant yeast expression vector can be
The expression vector of expression alien gene in host is stated, can such as be finished in the pEB carriers of expression in escherichia coli and in Pasteur's moral red
PPIC9K, pPIC9, pGAPza of expression etc. in yeast (Pichia pastoris).
Above-mentioned recombinant expression carrier can be built according to a conventional method.
The present invention also provides the applications of above-mentioned low temperature matrix metalloproteinase protein degradation under cryogenic.
The encoding gene that the present invention further additionally provides above-mentioned low temperature matrix metalloproteinase is degraded under cryogenic
The application of albumen.
Further, the albumen includes but not limited to casein, soybean protein, collagen, gelatin, wheat bran albumen etc..
Beneficial effects of the present invention are as follows：
Low temperature matrix metalloproteinase of the present invention has efficient protein degrading activity in 10~20 DEG C of cryogenic conditions, and
Hot inactivation temperature with relatively low (40 DEG C).
Description of the drawings
The specific embodiment of the present invention is described in further detail below in conjunction with the accompanying drawings.
Fig. 1 shows the SDS-PAGE figures of the expression product of recombinant expression carrier pGAPZa-nrMMP14.
Fig. 2 shows low temperature matrix metalloproteinase degradation capability measurement chart.
Specific embodiment
In order to illustrate more clearly of the present invention, the present invention is done further with reference to preferred embodiments and drawings
It is bright.Similar component is indicated with identical reference numeral in attached drawing.It will be appreciated by those skilled in the art that institute is specific below
The content of description is illustrative and be not restrictive, and should not be limited the scope of the invention with this.
The acquisition of 1 low temperature matrix metalloproteinase gene of embodiment and expression 1, the low temperature base of low temperature matrix metalloproteinase
The foundation of matter metalloprotease gene transcribed library
Roche Antarctic Fish (Notothenia rossii) adult fish takes oral cavity sample, liquid nitrogen flash freezer, in -80 through vivisection
It DEG C saves backup.Tissue samples are after liquid nitrogen grinding, with reference to total with the extraction of RNAiso Plus (Takara, Dalian) kit
RNA.RNA sample is after RNase-free DNase I digestion process removes contaminating genomic DNA, agarose gel electrophoresis and purple
Outer spectrophotometer detection, concentration are adjusted to 500ng/ μ L.Using above-mentioned RNA sample as template, through AMV reverse transcription reagent box
(Promega) reverse transcription is cDNA, and -20 DEG C preserve.
2nd, the acquisition of low temperature matrix metalloproteinase gene
Using the cDNA sequence obtained in step 1 as template, PCR reactions, amplification are carried out under the guiding of primer 1 and primer 2
The sequence of low temperature matrix metalloproteinase (nrMMP14) gene.
Primer 1：5’-CTCGAGGCGACGGAGCGACAAGT-3 ' (its nucleotide sequence such as sequence table SED ID NO.3 institutes
Show, dashed part base is Xho I sites)；
Primer 2：5’-GCGGCCGCTTAGCCTCCATCAGTCTTGG-3 ' (its nucleotide sequence such as sequence table SED ID
Shown in NO.4, dashed part base is Not I recognition sites)
In PCR reactions, PCR reaction conditions are：It 94 DEG C, is kept for 5 minutes, is then cycled by following temperature change program
30 times：94 DEG C are warming up to, is kept for 1 minute, is cooled to 54 DEG C, is kept for 1 minute, is warming up to 68 DEG C, is kept for 2 minutes；Then in 68
DEG C, it is kept for 10 minutes, most keeps the temperature 10 minutes after 4 DEG C, terminate amplified reaction.About 1.5kb is obtained by agarose electrophoretic analysis
Single band, through PCR product Purification Kit after PCR product detection, and detectable concentration.PCR product is cloned through TA, even
PMD18-T carriers are connect, convert bacillus coli DH 5 alpha, obtain recombinant plasmid pMD18-nrMMP14 sequencing identifications.Low temperature matrix gold
Proteases gene DNA sequence is as shown in sequence table SEQ ID NO.2, corresponding amino acid sequence such as sequence table SEQ ID
Shown in NO.1.
3rd, the structure of the recombinant expression carrier of low temperature matrix metalloproteinase coding gene sequence
The PCR product both ends obtained have Xho I and Not I restriction endonuclease sites, are limited with Xho I and Not I
Property restriction endonuclease processed is carried out at the same time PCR product and plasmid pGAPZA α double digestion reaction.50 μ L of digestion system：Target fragment or matter
20 5 μ L, Xho I of μ L, 10 × Buffer, 2 μ L, Not I of grain 2 μ L, ddH221 μ L of O, digestion condition are 37 DEG C of reaction 3h.Enzyme
Cut product sequence verification after column recycles.Target fragment and carrier segments carry out Ligation in vitro with T4DNA ligases.Coupled reaction
10 μ L of system：5 μ L, pGAPZA α carriers of target fragment, 2 μ L 10 × T4DNA connections buffer solution, 1 μ L, T4DNA ligases (350U/ μ
L)1μL,ddH21 μ L of O, 16 DEG C of connections are overnight.Connection product converts e. coli jm109, screens, chooses through kalamycin resistance
37 DEG C of shaken cultivation 6-8h of bacterium colony are taken, PCR identifications is carried out respectively and the digestion of recombinant plasmid is identified.The recombinant expression carrier of acquisition
It is named as rear pGAPZA α-nrMMP14.PPIC9K-Dasag is sequenced, it was demonstrated that clone DNA sequence dna and the sequence table of connection
Sequence shown in SEQ ID NO.2 is identical, builds the recombinant expression carrier containing low temperature matrix metalloproteinase gene sequence
PGAPZA α-nrMMP14 are correct.
4th, expression of the low temperature matrix metalloproteinase in Pichia pastoris
After recombinant expression carrier pGAPZA α-nrMMP14 are allowed to linearisation with BspHI digestion with restriction enzyme, use
Electric shock mode imports the carrier pGAPZA α-nrMMP14 of linearisation in Pichia pastoris X33, chosen property medium culture, sieve
Select the high expression bacterial strain of anti-bleomycin.The single bacterium colony grown on picking selective medium is inoculated in 5ml YPD Liquid Cultures
In base (yeast extract 10g/L, peptone 20g/L, glucose 20g/L), 28 DEG C culture 12-24 it is small when after, be transferred to 500mlBMGY training
Support base (1% yeast extract, 2% peptone, yeast nitrogen (YNB) 1.34%, 100mM phosphate buffers pH6.0,4 × 10-5Biology
Element, 1% glycerine) in continue culture to bacterium solution OD600=2-3, adjustment cultivation temperature be 15 DEG C, add glucose induction training
Support, and add when 24 is small glucose thereafter to final concentration of 1%, cultivate to 120 it is small when can stop cultivating.Centrifugation is received
Collect supernatant, 15 μ L supernatants is taken to be detected with SDS-PAGE electrophoresis.The results are shown in Figure 1：Swimming lane 1 is protein standard molecular weight
marker；Swimming lane 2,3,4 is expression product, and arrow represents purpose band, this shows recombinant bacterial strain under glucose low temperature induction
The molecular weight of the protein of expression about 56KDa, it is in the same size with pushing away the theoretical molecular weight (56kd) that section goes out from amino acid.
The low temperature matrix metalloproteinase expressed in Pichia pastoris can be directly secreted into the supernatant of culture solution, supernatant
Protein ingredient is single in liquid, can be directly used for enzyme assay.
The Activity determination (Hydroxyproline assay method) of 2 low temperature matrix metalloproteinase of embodiment
2.1 test principle
Matrix metalloproteinase catalysis solid-state insoluble collagen is decomposed into soluble peptide and enters in solution, is filtered after reaction terminating
Except unreacted albumen, filtrate heating acidolysis is free amino acid.Hydroxyproline is the specific amino acids of collagen, using hydroxyl dried meat
The hydroxyproline quality dissociated in propylhomoserin colorimetric method for determining acid hydrolysis solution, the collagen quality that secondary indication is hydrolyzed.The numerical value
Be known as the degradation rate of collagen with the ratio of hydroxyproline total content in substrate collagen, can response matrix metalloproteinases collagen water
Solution vigor.
2.2 experimental method
With Tris-HCl buffer solutions (pH=7.4, CaCl containing 5mmol/ml2, 0.5mmol acetic acid -4- aminobenzenes mercury) and it is anti-
System is answered, addition substrate ox heel string collagen (Sigma C9879) to 2mg/ml adds enzyme 0.1mg/ml, in 15 DEG C of concussion reactions
30 it is small when, and periodically collect supernatant sample.After Supernatant samples filtering, isometric concentrated hydrochloric acid solution is added in acidolysis pipe, 110
It is heated overnight in DEG C baking oven, hydroxyproline content is measured with colorimetric method (561nm).
The enzyme that experimental group is added is 1 obtained low temperature matrix metalloproteinase (nrMMP14) of embodiment；Control group institute
The enzyme of addition is the type i collagen enzyme (MMP_from_Ch) from clostridium histolyticum (Clostridium histolyticum).
The result shows that the interior low temperature matrix metalloproteinase nrMMP14 of the present invention when 12 is small, 80% substrate collagen can be effectively hydrolyzed.
Meanwhile under the conditions of low temperature (15 DEG C), the average specific of nrMMP14 clostridiopetidase As is lived within entire reaction time, is control group (histolytica
Clostridium type i collagen enzyme MMP_from_Ch) average specific live 1.98 times (see Fig. 2).
By hot inactivation experiments, low temperature matrix metalloproteinase nrMMP14 thermal stability of the present invention, experiment condition are verified
For：0.5mg/ml enzyme stock solutions are configured, water-bath 30 minutes at 40 DEG C then measures enzyme after inactivation according to foregoing active assay method
Vigor.The result shows that through 40 DEG C of water bath processings 30 minutes, the collagenase activity complete deactivation of nrMMP14 is (see Fig. 2, nrMMP_
deactivated)。
Obviously, the above embodiment of the present invention is only intended to clearly illustrate example of the present invention, and is not pair
The restriction of embodiments of the present invention for those of ordinary skill in the art, may be used also on the basis of the above description
To make other variations or changes in different ways, all embodiments can not be exhaustive here, it is every to belong to this hair
The obvious changes or variations that bright technical solution is extended out is still in the row of protection scope of the present invention.
Sequence table
<110>Physical Chemistry Technology Inst., Chinese Academy of Sciences
<120>A kind of low temperature matrix metalloproteinase and its encoding gene and application
<130> JLC17I0835E
<160> 4
<170> SIPOSequenceListing 1.0
<210> 1
<211> 491
<212> PRT
<213> Notothenia rossii
<400> 1
Ala Thr Glu Arg Gln Val Asn Pro Gln Thr Trp Leu Gln Gln Tyr Gly
1 5 10 15
Tyr Leu Pro Pro Gly Asp Met Arg Ala His Ser Leu Arg Ser Pro His
20 25 30
Ser Val Thr Ser Ala Ile Ser Ala Met Gln Lys Phe Tyr Gly Leu Thr
35 40 45
Val Thr Gly Thr Phe Asp Pro Asn Thr Ile Glu Ala Met Lys Arg Pro
50 55 60
Arg Cys Gly Val Pro Asp Lys Phe Gly Ala Glu Leu Lys Ser Asn Leu
65 70 75 80
Arg Lys Lys Arg Tyr Ala Ile Gln Gly Leu Lys Trp Gly Lys Asn Glu
85 90 95
Ile Thr Phe Ser Ile Gln Asn Tyr Thr Pro Lys Ile Gly Glu Tyr Asn
100 105 110
Ser Tyr Glu Ala Ile Arg Arg Ala Phe Lys Val Trp Gln Gln Val Thr
115 120 125
Pro Leu Thr Phe Asp Glu Ile Pro Tyr Gln Glu Ile Lys Tyr Gly Arg
130 135 140
Arg Lys Glu Pro Asp Ile Met Ile Phe Phe Ala Ser Gly Phe His Gly
145 150 155 160
Asp Ser Ser Pro Phe Asp Gly Glu Gly Gly Phe Leu Ala His Ala Tyr
165 170 175
Phe Pro Gly Pro Gly Met Gly Gly Asp Thr His Phe Asp Ser Asp Glu
180 185 190
Pro Trp Thr Ile Gly Asn His Asn Val Gln Gly Asn Asp Leu Phe Leu
195 200 205
Val Ala Val His Glu Leu Gly His Ala Leu Gly Leu Glu His Ser Asn
210 215 220
Asn Pro Leu Ala Ile Met Ala Pro Phe Tyr Gln Trp Met Glu Thr Glu
225 230 235 240
Asn Phe Gln Leu Pro Asp Asp Asp Leu Arg Gly Ile Gln Gln Ile Tyr
245 250 255
Gly Ser Gly Ser Gly Pro Gln Pro Pro Pro Val Thr Thr Arg Thr Pro
260 265 270
Asn His Asp Pro Asp Val Glu Tyr Ser Pro Asp Lys Pro His Phe Gly
275 280 285
Pro Asn Ile Cys Asp Gly His Phe Asp Thr Ile Ala Ile Leu Arg Gly
290 295 300
Glu Met Phe Val Phe Lys Asp Lys Trp Phe Trp Arg Val Arg Asn Asn
305 310 315 320
His Val Leu Asp Gly Tyr Pro Met Pro Ile Gly His Phe Trp Arg Gly
325 330 335
Leu Pro Thr His Val Thr Ala Ala Phe Glu Arg Glu Asp Gly Lys Phe
340 345 350
Val Phe Phe Lys Gly Asp Lys Tyr Trp Val Phe Thr Glu Ser Leu Leu
355 360 365
Asp Pro Gly Phe Pro Lys Asn Ile Lys Glu Met Gly Thr Gly Leu Pro
370 375 380
Lys Asp Arg Ile Asp Ala Gly Leu Phe Tyr Thr Pro Thr Gly Gln Thr
385 390 395 400
Phe Tyr Phe Arg Ala Asn Lys Tyr Tyr Arg Phe Asn Glu Asp Met Arg
405 410 415
Ser Val Asp Glu Gly Tyr Pro Lys Ala Val Ser Val Trp Gln Gly Val
420 425 430
Pro Asp Asn Ile Lys Ala Ala Phe Met Ser Lys Asp Gln Glu His Thr
435 440 445
Tyr Phe Tyr Lys Ala Asn Lys Tyr Trp Lys Phe Asn Asn Gln Val Met
450 455 460
Arg Val Glu Pro Gly Tyr Pro Lys Ser Ala Leu Arg Asp Trp Met Gly
465 470 475 480
Cys Pro Asn Glu Asp Pro Lys Thr Asp Gly Gly
485 490
<210> 2
<211> 1473
<212> DNA
<213> Notothenia rossii
<400> 2
gcgacggagc gacaagtcaa tccacagaca tggctgcagc agtatggtta cctgcccccg 60
ggggacatgc gagcccactc cctccgctcc cctcactccg tcacctcggc tatcagcgcc 120
atgcagaagt tctacggcct caccgtcact ggcaccttcg accccaacac catcgaggcc 180
atgaagcgac cgcgctgtgg agtgccagat aagtttggtg ctgagttgaa aagcaacctg 240
aggaagaagc gatacgccat ccagggcctg aagtggggca agaatgaaat cactttcagt 300
atccaaaact acactcccaa gattggagag tataactcat acgaagccat ccgtcgggcg 360
tttaaagtct ggcagcaggt gaccccattg acctttgacg aaatccccta ccaggagatc 420
aaatatggac gccgcaagga gcccgacatt atgatctttt tcgcttcggg tttccatgga 480
gacagctctc cttttgatgg ggagggaggc ttcctagctc atgcctactt ccctggacct 540
ggaatgggcg gggacacaca ctttgactcc gatgaaccat ggaccatagg aaaccataac 600
gtacaaggta acgacctctt cctggttgca gtccatgagc tgggccacgc ccttggttta 660
gagcactcca acaacccact tgccatcatg gctccctttt accagtggat ggagacggag 720
aatttccaac tgccagatga cgacctgcga ggcatccagc agatctatgg ttctggatca 780
ggccctcagc cccctcctgt aacaactcgt acgccgaacc atgaccctga cgtcgaatat 840
tcaccagaca agcctcactt tggccccaac atctgtgatg gacacttcga cacaatcgcc 900
atcctcagag gagaaatgtt tgtgtttaag gataaatggt tctggagagt acggaacaac 960
catgttctgg atggatatcc aatgccgatt ggtcactttt ggaggggact gcccacacat 1020
gtgactgctg cttttgaaag ggaagatggg aaatttgttt tctttaaagg ggacaagtat 1080
tgggtgttta ccgaatcact tttagatcct ggtttcccga agaatataaa ggaaatgggc 1140
actggacttc ccaaggaccg aatagatgct ggtctcttct acacccccac tggacaaacg 1200
ttttacttca gagcaaacaa atattaccgt ttcaacgaag acatgcgaag cgttgatgag 1260
ggatatccaa aagctgtcag tgtgtggcaa ggagtgcctg acaatatcaa ggcagctttc 1320
atgagcaaag atcaagagca cacctacttc tacaaagcca acaagtattg gaagtttaac 1380
aaccaggtga tgcgtgtgga gcctggatat cctaaatcag cccttcgtga ctggatgggt 1440
tgtcccaacg aagaccccaa gactgatgga ggc 1473
<210> 3
<211> 23
<212> DNA
<213>Artificial sequence (Artificial Sequence)
<400> 3
ctcgaggcga cggagcgaca agt 23
<210> 4
<211> 28
<212> DNA
<213>Artificial sequence (Artificial Sequence)
<400> 4
gcggccgctt agcctccatc agtcttgg 28
Claims (9)
1. a kind of low temperature matrix metalloproteinase, which is characterized in that the low temperature matrix metalloproteinase is following (a) or (b)
Shown protein：
(a) protein being made of the amino acid sequence shown in sequence table SEQ ID NO.1；
(b) as the amino acid sequence shown in sequence table SEQ ID NO.1 by the substitution of one or more amino acid residues and/or
The protein with albumen degrading activity under cryogenic conditions that missing and/or insertion obtain.
2. the encoding gene of low temperature matrix metalloproteinase described in claim 1.
A kind of 3. encoding gene as claimed in claim 2, which is characterized in that the coding base of the low temperature matrix metalloproteinase
Because as shown in (a) or (b)：
(a) nucleotide sequence as shown in sequence table SED ID NO.2；
(b) nucleotide sequence of coding amino acid sequence as shown in sequence table SED ID NO.1.
4. expression vector, cell line, engineering bacteria or host strain containing the encoding gene described in Claims 2 or 3.
A kind of 5. method for expressing low temperature matrix metalloproteinase described in claim 1, which is characterized in that will contain and have the right to want
The recombinant expression carrier of the encoding gene of the low temperature matrix metalloproteinase described in 2 or 3 is asked to import host cell, expression obtains low
Warm matrix metalloproteinase.
6. according to the method described in claim 5, it is characterized in that, for build recombinant expression carrier set out carrier for pEB,
PPIC9K, pPIC9, pGAPza carrier.
7. according to the method described in claim 5, it is characterized in that, the host for Escherichia coli, saccharomycete, mammal,
Insect, hay bacillus, bacillus or lactobacillus.
8. the application of low temperature matrix metalloproteinase protein degradation in cryogenic conditions described in claim 1.
9. the application of the encoding gene of low temperature matrix metalloproteinase protein degradation in cryogenic conditions described in Claims 2 or 3.
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Cited By (1)
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| JP2021177752A (en) * | 2020-05-14 | 2021-11-18 | 中国農業科学院農産品加工研究所 | LOW-TEMPERATURE ACIDIC PROTEASE PsAPA, AND PREPARATION METHOD AND APPLICATION OF THE SAME |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20070015242A1 (en) * | 2005-02-01 | 2007-01-18 | Azar Dimitri T | Neostatins |
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2017
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| US20070015242A1 (en) * | 2005-02-01 | 2007-01-18 | Azar Dimitri T | Neostatins |
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| Title |
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| AUTOMATED COMPUTATIONAL ANALYSIS: "XP_010782392.1", 《GENBANK》 * |
| 曹敏杰 等: "鱼类基质金属蛋白酶研究进展", 《集美大学学报( 自然科学版)》 * |
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| JP2021177752A (en) * | 2020-05-14 | 2021-11-18 | 中国農業科学院農産品加工研究所 | LOW-TEMPERATURE ACIDIC PROTEASE PsAPA, AND PREPARATION METHOD AND APPLICATION OF THE SAME |
| JP7008767B2 (en) | 2020-05-14 | 2022-02-10 | 中国農業科学院農産品加工研究所 | Cold acidic protease PsAPA and its preparation method and application |
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