CN110295155A - Promote durothermic cellulase - Google Patents
Promote durothermic cellulase Download PDFInfo
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- CN110295155A CN110295155A CN201910635879.XA CN201910635879A CN110295155A CN 110295155 A CN110295155 A CN 110295155A CN 201910635879 A CN201910635879 A CN 201910635879A CN 110295155 A CN110295155 A CN 110295155A
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- Prior art keywords
- gly
- cellulase
- ser
- thr
- asn
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- JVGDAEKKZKKZFO-RCWTZXSCSA-N Val-Val-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)N)O JVGDAEKKZKKZFO-RCWTZXSCSA-N 0.000 description 1
- 108010084455 Zeocin Proteins 0.000 description 1
- 238000010669 acid-base reaction Methods 0.000 description 1
- 108010044940 alanylglutamine Proteins 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 108010008355 arginyl-glutamine Proteins 0.000 description 1
- 108010062796 arginyllysine Proteins 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- 108010047754 beta-Glucosidase Proteins 0.000 description 1
- 102000006995 beta-Glucosidase Human genes 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000008033 biological extinction Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 229920006184 cellulose methylcellulose Polymers 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 235000019628 coolness Nutrition 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000007599 discharging Methods 0.000 description 1
- 230000005611 electricity Effects 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000001952 enzyme assay Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 108010089804 glycyl-threonine Proteins 0.000 description 1
- 108010010147 glycylglutamine Proteins 0.000 description 1
- YMAWOPBAYDPSLA-UHFFFAOYSA-N glycylglycine Chemical compound [NH3+]CC(=O)NCC([O-])=O YMAWOPBAYDPSLA-UHFFFAOYSA-N 0.000 description 1
- 108010084389 glycyltryptophan Proteins 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 125000003835 nucleoside group Chemical group 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 238000003359 percent control normalization Methods 0.000 description 1
- CWCMIVBLVUHDHK-ZSNHEYEWSA-N phleomycin D1 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC[C@@H](N=1)C=1SC=C(N=1)C(=O)NCCCCNC(N)=N)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C CWCMIVBLVUHDHK-ZSNHEYEWSA-N 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000001012 protector Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 108010061238 threonyl-glycine Proteins 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
Classifications
-
- 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)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
-
- 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)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2445—Beta-glucosidase (3.2.1.21)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01021—Beta-glucosidase (3.2.1.21)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01091—Cellulose 1,4-beta-cellobiosidase (3.2.1.91)
Abstract
Durothermic cellulase is promoted the present invention relates to a kind of, its amino acid sequence system is the N-terminal of sequence number 2 to be added cysteine (Cysteine), and add glycine (Glycine) and cysteine (Cysteine) in C-terminal or add the sequence of proline (Proline) and cysteine (Cysteine).
Description
The application is application No. is 201510992464.X, and the applying date is on December 23rd, 2015, entitled " to be promoted
The divisional application of the Chinese patent application of durothermic cellulase ".
Technical field
The present invention relates to a kind of cellulases, espespecially a kind of to promote durothermic cellulase.
Background technique
Cellulose is the next of primary biological mass-energy (biomass) on one of main composition of plant cell wall and the earth
Source, therefore, the zymoproteins for capableing of effectively decomposition of cellulose many now are also very extensive in different industrial applications.Cellulose
Be by glucose be unit, long chain polysaccharides made of being bonded with β-Isosorbide-5-Nitrae-glycosidic bond (β-Isosorbide-5-Nitrae-glycosidic bond), this
A little polysaccharide bodies organize the decomposition for being arranged in close crystal type cellulose, and then resisting extraneous in concert.However, in living nature
Many plant-eating animals and microorganism etc. need to resolve into and can be inhaled in vivo by by the polysaccharide fiber element in plant cell wall
The grape monosaccharide of receipts, using as existence energy source.The catalyst mechanism of cellulase will connect two mainly by acid-base reaction
Effect is hydrolyzed in β-Isosorbide-5-Nitrae-glycosidic bond of a monosaccharide, and then decomposes polysaccharide fiber element.And cellulase substantially can be divided into three
Class, respectively endoglucanase (endo-glucanase), exoglucanase (cellobiohydrolase) and grape
Glycosidase (β-glucosidase).Long chain cellulose can be randomly cut into the oligosaccharides of many small fragments by endoglucanase；
And exoglucanase can then be decomposed from the reducing end or non-reducing end of long chain cellulose, primary product is fiber two
Sugar；Cellobiose can be then decomposed into the glucose of monosaccharide as glucuroide.
Cellulase industrially using very extensive, whether in food, feed or textile industry, or even can apply to
Biomass energy now of greatest concern.For the application of different industry, cellulase also needs to meet its different applicable item
Part and range.For example: being suitble to the zymoprotein of slant acidity and heatproof on feed industry, however be then preference in textile industry
The cellulase of meta-alkalescence.Therefore, can find out and be more in line with different industrial required zymoproteins is also whether to learn at present
Art or industrial circle are all in the target of effort.At present in many relevant researchs, more preferably enzyme in order to obtain, in addition in nature
In screen except, exactly existing zymoprotein is transformed.Mainly there are two big Reconstruc-tion policies now, one is random prominent
Become or by enzyme gene random alignment, under specific action condition, filters out the zymoprotein for more meeting its action condition.
The benefit of this strategy is need not to further investigate the structure or mechanism of action of enzyme, but directly go to find out at random under given conditions
Better zymoprotein；However, its disadvantage is that a large amount of manpower and time is needed to go largely to be screened or to have very well
A large amount of screening techniques cooperate.Another Reconstruc-tion policy is then by research enzymatic structure and mechanism of action to find out for enzyme activity
Property or characteristic there is critical amino acid, and be mutated and tested for these specific amino acids, and then obtain functionality
Stronger transformation zymoprotein.This advantage is to be not required to spend time and manpower the step of mass mutation is with screening, but need first
The protein structure and its mechanism of action for solving this enzyme can just find out the specific amino acids of tool transformation potentiality.
Different industrial process needs to meet the zymoprotein of its different role environment to cooperate and participate in.Even if cellulase
It is industrially widely used for a long time, however many industrial enzymes are from mesophilic bacteria, such as inner formula trichoderma (Trichoderma
Reesei it) is screened, therefore heat resistance is also poor.On the other hand, heat resistant fibre element enzyme can be effectively applied to
In the industry for needing high temperature action environment, it is made comprising beer or biomass energy industry etc..Has the albumen of heat resistance relatively
Its protein stabilized degree also can be higher, therefore can be stabilized in the high temperature environment, or even to make land used more preferable.Whether it is acting on
In environment or back segment treatment process, also it is not required to worry that zymoprotein can be destroyed because of high temperature itself.In addition, the work of zymoprotein
Property be also the big emphasis for improveing industrial enzyme, enzymatic activity is cured the decline of higher position representative cost and the raising of profit.
According to literature research, cystine linkage facilitates the stabilization of protein structure and promotes heat resistance.In formula trichoderma have permitted
Multi cellulose enzyme, wherein belonging to the Cel5A cellulase of GH family 5, protein structure (ID 3QR3) was sent out in 2011
Table, there are four cystine linkage positions for inside configuration tool in C16-C22, C92-C99, C232-C2683 and C273-C323, therefore has
There is higher solution temperature (Tm value), in addition, structure type (the Toni M of α/β TIM barrel is presented in the structure of Cel5A
Lee,Mary F Farrow,Frances H Arnold,and Stephen L Mayo.(2011)Protein Structure
Report,nov27；20(11):1935-40.).And in Simon R.Andrews in 2004 et al. the study found that
The CmXyn10B of Cellvibrio japonicas xylanase protein CjXyn10A and Cellvibrio mixtus, in its N-terminal
Increase that cystine linkage is bonded with C-terminal, further rock-steady structure and then the tolerance of temperature can be promoted, and CjXyn10A and CmXyn
Its structure of 10B is also to belong to α/β TIM barrel kenel (Andrews S.R., Taylor E.J., Pell G., Vincent
F.,Ducros V.M.,Davies G.J.,Lakey J.H.,and Gilbert H.J.,(2004)J.Biol.Chem.Dec
24；279(52):54369-79.).
Therefore, the present invention is intended to bonded to increase the cystine linkage of cellulase by modifying gene, promotes cellulase whereby
For the tolerance of temperature, to effectively increase the industrial value that cellulase is industrially applied.
Summary of the invention
It is an object of the invention to which existing cellulase is transformed, using structural analysis and point mutation technology, increase cellulose
The cystine linkage of enzyme is bonded, effectively to promote the temperature tolerance of cellulase, and then increases the industrial application value of cellulase.
In order to achieve the above object, a broader embodiment of the invention provides a kind of cellulase, amino acid sequence
It is by the N-terminal of sequence number 2 plus cysteine (Cysteine), and adds glycine (Glycine) and half Guang ammonia in C-terminal
Sour (Cysteine) or the sequence for adding proline (Proline) and cysteine (Cysteine).Wherein encode the sequence
The gene of number 2 is come out and optimized gene from inner formula trichoderma (Trichoderma reesei) is separated.
In one embodiment, the amino acid sequence of the cellulase is the amino acid sequence of sequence number 4.
In one embodiment, the amino acid sequence of the cellulase is the amino acid sequence of sequence number 6.
Also, another broader embodiment of the invention provide a kind of nucleic acid molecules for encoding the cellulase and comprising
The recombinant plasmid of the nucleic acid molecules.
Detailed description of the invention
Fig. 1 shows the nucleotide sequence and amino acid sequence of WT cellulase.
Fig. 2 shows the mutant primer sequence of primer one.
Fig. 3 shows the mutant primer sequence of primer two.
Fig. 4 shows the mutant primer sequence of primer three.
Fig. 5 shows the nucleotide sequence and amino acid sequence of improved CGC cellulase.
Fig. 6 shows the nucleotide sequence and amino acid sequence of improved CPC cellulase.
Fig. 7 shows that the temperature tolerance of WT cellulase and two kinds of mutains of CGC cellulase and CPC cellulase is analyzed.
The SDS-PAGE electrophoretic analysis that Fig. 8 display assessment cystine linkage connects.
Specific embodiment
The some exemplary embodiments for embodying feature of present invention and advantage will describe in detail in the explanation of back segment.It should be understood that
It is that the present invention there can be various variations in different embodiments, neither departs from the scope of the present invention, and therein
Illustrating and illustrate in itself should be illustrative, rather than to limit the present invention.
The cellulase that the present invention uses is separated from inner formula trichoderma (Trichoderma reesei) bacterial strain comes out
Gene, and it is optimized and remove 91 amino acid of N-terminal sequence, to promote its protein expression ability.This gene is not mutated
Processing, therefore (hereinafter referred to as WT cellulase) is referred to as with wild-type cellulose enzyme.The both ends of aforementioned WT cellulase are with EcoRI
It is engaged on pPICZ α A carrier with NotI restriction enzyme position, and carries out sequencing and protein expression.Fig. 1 shows WT cellulase
Nucleotide sequence and amino acid sequence, wherein WT cellulose enzyme gene includes that 984 bases (contain terminator codon, nucleosides
Acid sequence is with the mark of sequence number 1) and 327 amino acid (amino acid sequence is with the mark of sequence number 2).
Structure further is analyzed using PyMOL software, it is found that space length is about between the N-terminal and C-terminal of WT cellulaseGreater than the distance for forming cystine linkage.Therefore, the present invention attempts respectively to add N-terminal and C-terminal both ends into Cysteine (half
Cystine) except, increase a lesser Glycine of molecule (glycine) more before C-terminal Cysteine or long-chain is allowed to generate
The Proline (proline) of angular deflection generates cystine linkage and connects to reduce N-terminal with the space length of C-terminal, egg stable whereby
White N-terminal and C-terminal, and then promote the temperature tolerance of albumen.In other words, the present invention carries out two kinds of mutation transformations, and wherein the first is prominent
Become transformation be WT cellulase N-terminal plus Cysteine and in C-terminal plus Glycine and Cysteine, second of mutation
Transformation be WT cellulase N-terminal plus Cysteine and in C-terminal plus Proline and Cysteine.Improved albumen
Comprising 330 amino acid, the Cysteine of N-terminal is located at the 1st position of amino acid sequence, the Glycine or Proline of C-terminal
Positioned at the 329th position of amino acid sequence, the Cysteine of C-terminal is then located at the 330th position of amino acid sequence, therefore this hair
The first bright mutation transformation indicates with C1G329C330, abbreviation CGC cellulase, and second of mutation be transformed with
C1P329C330 expression, abbreviation CPC cellulase.
It will be described the method for the invention that cellulase is transformed and its obtained modified cellulose enzyme below.
The present invention carries out mutation transformation with point mutation technology.Firstly, using primer one (as shown in Figure 2) in cellulase
N-terminal increase Cysteine and then using primer two (as shown in Figure 3) in cellulase C-terminal increase Glycine and
Cysteine obtains the modifying gene of C1G329C330 (CGC), then uses primer three (as shown in Figure 4) again, will
329th amino acid Glycine point mutation of C1G329C330 modifying gene is Proline, obtains C1P329C330's (CPC)
Modifying gene.Fig. 5 is the nucleotide sequence and amino acid sequence for showing improved CGC cellulase, wherein CGC fiber
Plain enzyme gene includes 993 bases (containing terminator codon, nucleotide sequence is with the mark of sequence number 3) and 330 amino acid
(amino acid sequence is with the mark of sequence number 4).Fig. 6 then shows the nucleotide sequence and amino of improved CPC cellulase
Acid sequence, wherein CPC cellulose enzyme gene includes that 993 bases (contain terminator codon, nucleotide sequence is with the mark of sequence number 5
Show) and 330 amino acid (amino acid sequence is with the mark of sequence number 6).
After the DNA plasmid of two kinds of mutation transformations is linearized using Pme I restriction enzyme, turned with electricity
(electroporation) mode is sent into yeast Pichia pastoris X33, then by the bacterium solution after transition be coated onto containing
On the YPD plate of 100 μ g/ml zeocin antibiotic, it is placed in the culture of 30 DEG C of incubator progress two days.List is selected later
One bacterium colony is cultivated to 5ml YPD in 30 DEG C, is inoculated in 50ml BMGY and is cultivated one day for 30 DEG C；Next thallus is shifted to
The BMMY of 20ml carries out inducible protein expression in four days.Sample and add 0.5% methanol within every 24 hours, bacterium solution is with 3500rpm revolving speed
It is centrifuged and is collected supernatant, carries out albumen measurement and cellulase activity measurement.
The active testing mode of cellulase be take 1% carboxymethyl cellulose (Carboxymethyl cellulose,
CMC, pH 4.8,0.05M sodium citrate) (dilution buffer is 0.05M lemon for the cellulase protein liquid of 0.2ml and debita spissitudo
Lemon acid sodium；PH 4.8) 0.2ml, it is acted on 15 minutes at 50 DEG C after mixing, is subsequently added into the 1%DNS of 1.2ml and in 100
5 minutes are boiled in DEG C boiling water to stop reaction and colour generation, are then cooled down 10 minutes in cold water, in OD540Wavelength measures extinction
Value, then it is converted into unit of enzyme activity (unit).Wherein, the standard curve of enzymatic activity is by glucose standards solution 0-0.35 μ g/
It is formulated between ml, and the definition of 1unit is zymoprotein amount needed for discharging 1 μm of ole product per minute.
Heatproof test is then that (dilution buffer is 0.05M sodium citrate by the cellulase protein liquid of debita spissitudo；pH
4.8) it places and handles 2 minutes at different temperatures, 4 DEG C of coolings are placed on after taking-up place room temperature again within 10 minutes and rise again 10 minutes,
The Enzyme assay for carrying out 50 DEG C again later is calculated separately using the zymoprotein sample not through Overheating Treatment as 100% control
Opposite percentage remaining activity after Overheating Treatment out.
Fig. 7 shows that the temperature tolerance of WT cellulase and two kinds of mutains of CGC cellulase and CPC cellulase is analyzed,
Wherein the cellulase activity of not thermally treated sample is set as 100%.By Fig. 7 result it is found that at 75 DEG C, 80 DEG C and 85
DEG C after processing 2 minutes, the opposite residual activity of CPC cellulase is 94%, 70% and 74%, CGC cellulase it is opposite
Residual activity is 93%, 68% and 75%, and the two is much higher than 66%, 35% and the 43% of WT cellulase.In other words,
Residual activity after two kinds of mutains of CGC cellulase and CPC cellulase are handled 2 minutes at different temperatures is all higher than WT
Cellulase original protein, therefore temperature tolerance with higher, also illustrate that the industrial application value with larger potentiality.
On the other hand, the present invention is also directed to the evaluation test that mutain carries out cystine linkage.By the CGC fiber of debita spissitudo
Two kinds of mutains of plain enzyme and CPC cellulase and WT cellulase original protein liquid add 10mM dithiothreitol
(DTT), 12.5% sodium dodecyl sulfate polyacrylamide gel electrophoresis (sodium dodecyl sulfate is carried out
Polyacrylamide gel electrophoresis, SDS-PAGE), whether preliminary analysis mutain has cystine linkage
It connects.
The SDS-PAGE electrophoretic analysis that Fig. 8 display assessment cystine linkage connects, is the cystine linkage made in protein structure with DTT
Fracture, and observe movement speed of the albumen in electrophoresis colloid.By Fig. 8, as a result, it has been found that, the CGC cellulase after adding DTT is prominent
The white molecular weight and sizableness with the WT cellulase original protein of addition DTT of a kink of preserved egg, and it is not added with the CGC cellulose of DTT
Enzyme mutant protein positions are far below the WT cellulase original protein for being not added with DTT, indicate that CGC cellulase mutain generates
More cystine linkage, which connects, leads to protein molecular reduced space, and the movement speed in electrophoresis colloid less increases the original of cystine linkage
Beginning albumen it is fast.
In conclusion in order to increase the industrial application value of cellulase, the present invention designs by the mutation of logicality, makes
N-terminal and C-terminal generate cystine linkage and stablize protein structure to promote the temperature tolerance of cellulase.It is designed in two kinds of mutation of the invention
In, the first be WT cellulase N-terminal plus Cysteine and in C-terminal plus Glycine and Cysteine, obtain CGC
Cellulase；Second be WT cellulase N-terminal plus Cysteine and in C-terminal plus Proline and Cysteine,
Obtain CPC cellulase.According to heatproof test result it is found that two kinds of mutains of CGC cellulase and CPC cellulase are compared
In WT cellulase original protein, for high temperature tolerance more preferably, therefore can be more stable in the impact for facing temperature and can drop
Its low production cost can effectively increase the industrial value that cellulase is industrially applied.
Even if the present invention described in detail as above-described embodiment and can as be familiar with this those skilled in the art appoint apply craftsman think and be it is all as
Modification, it is so neither de- as attached claim is intended to Protector.
Sequence table
<110>Dongguan Fanyatai Biological Sci-Tech Co., Ltd.
<120>durothermic cellulase is promoted
<130> 158541TW01
<160> 12
<170> PatentIn version 3.3
<210> 1
<211> 984
<212> DNA
<213>inner formula trichoderma (Trichoderma reesei)
<400> 1
ggtgttagat ttgctggagt caatatcgca ggattcgatt ttggttgcac taccgatggt 60
acttgtgtca cctctaaggt ttacccacca ttgaagaatt tcactggttc taataactat 120
ccagacggta tcggacaaat gcaacatttt gttaacgatg atggtatgac aatcttcaga 180
ttgccagtcg gatggcaata cttggtcaat aacaatttgg gaggaaactt ggattctact 240
tctatttcta aatatgacca gttggttcag ggatgcttgt ctttgggtgc atactgtatt 300
gttgacattc ataactacgc tagatggaac ggtggtatca ttggacaggg tggtccaact 360
aatgctcaat tcacatcttt gtggtctcaa ttggcatcta agtatgcctc tcagtctaga 420
gtttggtttg gtattatgaa cgaaccacat gatgttaata tcaacacttg ggctgctact 480
gttcaagaag ttgttactgc tatcagaaac gctggtgcca cttctcagtt tatctctttg 540
ccaggtaacg attggcagtc tgccggtgct ttcatctctg acggttctgc cgctgcattg 600
tctcaggtta ccaaccctga cggatctact actaatttga tctttgacgt ccataagtat 660
ttggactctg acaactctgg tactcatgct gaatgtacaa ctaacaacat tgatggtgcc 720
ttttctcctt tggctacctg gttgagacag aacaacagac aggctatttt gaccgaaact 780
ggaggtggta atgttcagtc ttgtattcaa gatatgtgcc aacaaatcca gtacttgaat 840
caaaattctg atgtctattt gggttacgtt ggttggggtg ccggttcttt cgactctaca 900
tacgttttga ctgaaactcc aaccggatct ggtaactctt ggactgatac ttctttggtc 960
tcttcttgtt tggcaagaaa gtaa 984
<210> 2
<211> 327
<212> PRT
<213>inner formula trichoderma (Trichoderma reesei)
<400> 2
Gly Val Arg Phe Ala Gly Val Asn Ile Ala Gly Phe Asp Phe Gly Cys
1 5 10 15
Thr Thr Asp Gly Thr Cys Val Thr Ser Lys Val Tyr Pro Pro Leu Lys
20 25 30
Asn Phe Thr Gly Ser Asn Asn Tyr Pro Asp Gly Ile Gly Gln Met Gln
35 40 45
His Phe Val Asn Asp Asp Gly Met Thr Ile Phe Arg Leu Pro Val Gly
50 55 60
Trp Gln Tyr Leu Val Asn Asn Asn Leu Gly Gly Asn Leu Asp Ser Thr
65 70 75 80
Ser Ile Ser Lys Tyr Asp Gln Leu Val Gln Gly Cys Leu Ser Leu Gly
85 90 95
Ala Tyr Cys Ile Val Asp Ile His Asn Tyr Ala Arg Trp Asn Gly Gly
100 105 110
Ile Ile Gly Gln Gly Gly Pro Thr Asn Ala Gln Phe Thr Ser Leu Trp
115 120 125
Ser Gln Leu Ala Ser Lys Tyr Ala Ser Gln Ser Arg Val Trp Phe Gly
130 135 140
Ile Met Asn Glu Pro His Asp Val Asn Ile Asn Thr Trp Ala Ala Thr
145 150 155 160
Val Gln Glu Val Val Thr Ala Ile Arg Asn Ala Gly Ala Thr Ser Gln
165 170 175
Phe Ile Ser Leu Pro Gly Asn Asp Trp Gln Ser Ala Gly Ala Phe Ile
180 185 190
Ser Asp Gly Ser Ala Ala Ala Leu Ser Gln Val Thr Asn Pro Asp Gly
195 200 205
Ser Thr Thr Asn Leu Ile Phe Asp Val His Lys Tyr Leu Asp Ser Asp
210 215 220
Asn Ser Gly Thr His Ala Glu Cys Thr Thr Asn Asn Ile Asp Gly Ala
225 230 235 240
Phe Ser Pro Leu Ala Thr Trp Leu Arg Gln Asn Asn Arg Gln Ala Ile
245 250 255
Leu Thr Glu Thr Gly Gly Gly Asn Val Gln Ser Cys Ile Gln Asp Met
260 265 270
Cys Gln Gln Ile Gln Tyr Leu Asn Gln Asn Ser Asp Val Tyr Leu Gly
275 280 285
Tyr Val Gly Trp Gly Ala Gly Ser Phe Asp Ser Thr Tyr Val Leu Thr
290 295 300
Glu Thr Pro Thr Gly Ser Gly Asn Ser Trp Thr Asp Thr Ser Leu Val
305 310 315 320
Ser Ser Cys Leu Ala Arg Lys
325
<210> 3
<211> 993
<212> DNA
<213>artificial sequence (Artificial)
<220>
<221>
<222>
<223>mutant
<400> 3
tgtggtgtta gatttgctgg agtcaatatc gcaggattcg attttggttg cactaccgat 60
ggtacttgtg tcacctctaa ggtttaccca ccattgaaga atttcactgg ttctaataac 120
tatccagacg gtatcggaca aatgcaacat tttgttaacg atgatggtat gacaatcttc 180
agattgccag tcggatggca atacttggtc aataacaatt tgggaggaaa cttggattct 240
acttctattt ctaaatatga ccagttggtt cagggatgct tgtctttggg tgcatactgt 300
attgttgaca ttcataacta cgctagatgg aacggtggta tcattggaca gggtggtcca 360
actaatgctc aattcacatc tttgtggtct caattggcat ctaagtatgc ctctcagtct 420
agagtttggt ttggtattat gaacgaacca catgatgtta atatcaacac ttgggctgct 480
actgttcaag aagttgttac tgctatcaga aacgctggtg ccacttctca gtttatctct 540
ttgccaggta acgattggca gtctgccggt gctttcatct ctgacggttc tgccgctgca 600
ttgtctcagg ttaccaaccc tgacggatct actactaatt tgatctttga cgtccataag 660
tatttggact ctgacaactc tggtactcat gctgaatgta caactaacaa cattgatggt 720
gccttttctc ctttggctac ctggttgaga cagaacaaca gacaggctat tttgaccgaa 780
actggaggtg gtaatgttca gtcttgtatt caagatatgt gccaacaaat ccagtacttg 840
aatcaaaatt ctgatgtcta tttgggttac gttggttggg gtgccggttc tttcgactct 900
acatacgttt tgactgaaac tccaaccgga tctggtaact cttggactga tacttctttg 960
gtctcttctt gtttggcaag aaagggttgt taa 993
<210> 4
<211> 330
<212> PRT
<213>artificial sequence (Artificial)
<220>
<221>
<222>
<223>mutant
<400> 4
Cys Gly Val Arg Phe Ala Gly Val Asn Ile Ala Gly Phe Asp Phe Gly
1 5 10 15
Cys Thr Thr Asp Gly Thr Cys Val Thr Ser Lys Val Tyr Pro Pro Leu
20 25 30
Lys Asn Phe Thr Gly Ser Asn Asn Tyr Pro Asp Gly Ile Gly Gln Met
35 40 45
Gln His Phe Val Asn Asp Asp Gly Met Thr Ile Phe Arg Leu Pro Val
50 55 60
Gly Trp Gln Tyr Leu Val Asn Asn Asn Leu Gly Gly Asn Leu Asp Ser
65 70 75 80
Thr Ser Ile Ser Lys Tyr Asp Gln Leu Val Gln Gly Cys Leu Ser Leu
85 90 95
Gly Ala Tyr Cys Ile Val Asp Ile His Asn Tyr Ala Arg Trp Asn Gly
100 105 110
Gly Ile Ile Gly Gln Gly Gly Pro Thr Asn Ala Gln Phe Thr Ser Leu
115 120 125
Trp Ser Gln Leu Ala Ser Lys Tyr Ala Ser Gln Ser Arg Val Trp Phe
130 135 140
Gly Ile Met Asn Glu Pro His Asp Val Asn Ile Asn Thr Trp Ala Ala
145 150 155 160
Thr Val Gln Glu Val Val Thr Ala Ile Arg Asn Ala Gly Ala Thr Ser
165 170 175
Gln Phe Ile Ser Leu Pro Gly Asn Asp Trp Gln Ser Ala Gly Ala Phe
180 185 190
Ile Ser Asp Gly Ser Ala Ala Ala Leu Ser Gln Val Thr Asn Pro Asp
195 200 205
Gly Ser Thr Thr Asn Leu Ile Phe Asp Val His Lys Tyr Leu Asp Ser
210 215 220
Asp Asn Ser Gly Thr His Ala Glu Cys Thr Thr Asn Asn Ile Asp Gly
225 230 235 240
Ala Phe Ser Pro Leu Ala Thr Trp Leu Arg Gln Asn Asn Arg Gln Ala
245 250 255
Ile Leu Thr Glu Thr Gly Gly Gly Asn Val Gln Ser Cys Ile Gln Asp
260 265 270
Met Cys Gln Gln Ile Gln Tyr Leu Asn Gln Asn Ser Asp Val Tyr Leu
275 280 285
Gly Tyr Val Gly Trp Gly Ala Gly Ser Phe Asp Ser Thr Tyr Val Leu
290 295 300
Thr Glu Thr Pro Thr Gly Ser Gly Asn Ser Trp Thr Asp Thr Ser Leu
305 310 315 320
Val Ser Ser Cys Leu Ala Arg Lys Gly Cys
325 330
<210> 5
<211> 993
<212> DNA
<213>artificial sequence (Artificial)
<220>
<221>
<222>
<223>mutant
<400> 5
tgtggtgtta gatttgctgg agtcaatatc gcaggattcg attttggttg cactaccgat 60
ggtacttgtg tcacctctaa ggtttaccca ccattgaaga atttcactgg ttctaataac 120
tatccagacg gtatcggaca aatgcaacat tttgttaacg atgatggtat gacaatcttc 180
agattgccag tcggatggca atacttggtc aataacaatt tgggaggaaa cttggattct 240
acttctattt ctaaatatga ccagttggtt cagggatgct tgtctttggg tgcatactgt 300
attgttgaca ttcataacta cgctagatgg aacggtggta tcattggaca gggtggtcca 360
actaatgctc aattcacatc tttgtggtct caattggcat ctaagtatgc ctctcagtct 420
agagtttggt ttggtattat gaacgaacca catgatgtta atatcaacac ttgggctgct 480
actgttcaag aagttgttac tgctatcaga aacgctggtg ccacttctca gtttatctct 540
ttgccaggta acgattggca gtctgccggt gctttcatct ctgacggttc tgccgctgca 600
ttgtctcagg ttaccaaccc tgacggatct actactaatt tgatctttga cgtccataag 660
tatttggact ctgacaactc tggtactcat gctgaatgta caactaacaa cattgatggt 720
gccttttctc ctttggctac ctggttgaga cagaacaaca gacaggctat tttgaccgaa 780
actggaggtg gtaatgttca gtcttgtatt caagatatgt gccaacaaat ccagtacttg 840
aatcaaaatt ctgatgtcta tttgggttac gttggttggg gtgccggttc tttcgactct 900
acatacgttt tgactgaaac tccaaccgga tctggtaact cttggactga tacttctttg 960
gtctcttctt gtttggcaag aaagccatgt taa 993
<210> 6
<211> 330
<212> PRT
<213>artificial sequence (Artificial)
<220>
<221>
<222>
<223>mutant
<400> 6
Cys Gly Val Arg Phe Ala Gly Val Asn Ile Ala Gly Phe Asp Phe Gly
1 5 10 15
Cys Thr Thr Asp Gly Thr Cys Val Thr Ser Lys Val Tyr Pro Pro Leu
20 25 30
Lys Asn Phe Thr Gly Ser Asn Asn Tyr Pro Asp Gly Ile Gly Gln Met
35 40 45
Gln His Phe Val Asn Asp Asp Gly Met Thr Ile Phe Arg Leu Pro Val
50 55 60
Gly Trp Gln Tyr Leu Val Asn Asn Asn Leu Gly Gly Asn Leu Asp Ser
65 70 75 80
Thr Ser Ile Ser Lys Tyr Asp Gln Leu Val Gln Gly Cys Leu Ser Leu
85 90 95
Gly Ala Tyr Cys Ile Val Asp Ile His Asn Tyr Ala Arg Trp Asn Gly
100 105 110
Gly Ile Ile Gly Gln Gly Gly Pro Thr Asn Ala Gln Phe Thr Ser Leu
115 120 125
Trp Ser Gln Leu Ala Ser Lys Tyr Ala Ser Gln Ser Arg Val Trp Phe
130 135 140
Gly Ile Met Asn Glu Pro His Asp Val Asn Ile Asn Thr Trp Ala Ala
145 150 155 160
Thr Val Gln Glu Val Val Thr Ala Ile Arg Asn Ala Gly Ala Thr Ser
165 170 175
Gln Phe Ile Ser Leu Pro Gly Asn Asp Trp Gln Ser Ala Gly Ala Phe
180 185 190
Ile Ser Asp Gly Ser Ala Ala Ala Leu Ser Gln Val Thr Asn Pro Asp
195 200 205
Gly Ser Thr Thr Asn Leu Ile Phe Asp Val His Lys Tyr Leu Asp Ser
210 215 220
Asp Asn Ser Gly Thr His Ala Glu Cys Thr Thr Asn Asn Ile Asp Gly
225 230 235 240
Ala Phe Ser Pro Leu Ala Thr Trp Leu Arg Gln Asn Asn Arg Gln Ala
245 250 255
Ile Leu Thr Glu Thr Gly Gly Gly Asn Val Gln Ser Cys Ile Gln Asp
260 265 270
Met Cys Gln Gln Ile Gln Tyr Leu Asn Gln Asn Ser Asp Val Tyr Leu
275 280 285
Gly Tyr Val Gly Trp Gly Ala Gly Ser Phe Asp Ser Thr Tyr Val Leu
290 295 300
Thr Glu Thr Pro Thr Gly Ser Gly Asn Ser Trp Thr Asp Thr Ser Leu
305 310 315 320
Val Ser Ser Cys Leu Ala Arg Lys Pro Cys
325 330
<210> 7
<211> 34
<212> DNA
<213>artificial sequence (Artificial)
<220>
<221>
<222>
<223>synthetic primer
<400> 7
gctgaagctg aattctgtgg tgttagattt gctg 34
<210> 8
<211> 34
<212> DNA
<213>artificial sequence (Artificial)
<220>
<221>
<222>
<223>synthetic primer
<400> 8
cagcaaatct aacaccacag aattcagctt cagc 34
<210> 9
<211> 41
<212> DNA
<213>artificial sequence (Artificial)
<220>
<221>
<222>
<223>synthetic primer
<400> 9
ttgtttggca agaaagggtt gttaagcggc cgccagcttt c 41
<210> 10
<211> 41
<212> DNA
<213>artificial sequence (Artificial)
<220>
<221>
<222>
<223>synthetic primer
<400> 10
gaaagctggc ggccgcttaa caaccctttc ttgccaaaca a 41
<210> 11
<211> 35
<212> DNA
<213>artificial sequence (Artificial)
<220>
<221>
<222>
<223>synthetic primer
<400> 11
ttgtttggca agaaagccat gttaagcggc cgcca 35
<210> 12
<211> 35
<212> DNA
<213>artificial sequence (Artificial)
<220>
<221>
<222>
<223>synthetic primer
<400> 12
aaagctggcg gccgcttaac atggctttct tgcca 35
Claims (5)
1. a kind of cellulase, amino acid sequence is by the N-terminal of sequence number 2 plus cysteine (Cysteine), and
In C-terminal plus the sequence of proline (Proline) and cysteine (Cysteine).
2. cellulase as described in claim 1, wherein the gene for encoding the sequence number 2 is from inner formula trichoderma
(Trichoderma reesei) it is separated come out and optimized gene.
3. cellulase as described in claim 1, wherein the amino acid sequence of the cellulase is the amino acid of sequence number 6
Sequence.
4. a kind of nucleic acid molecules for encoding cellulase as described in claim 1.
5. a kind of recombinant plasmid, it includes nucleic acid molecules as claimed in claim 4.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201910635879.XA CN110295155A (en) | 2015-12-23 | 2015-12-23 | Promote durothermic cellulase |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510992464.XA CN106906198B (en) | 2015-12-23 | 2015-12-23 | Cellulase for improving temperature resistance |
| CN201910635879.XA CN110295155A (en) | 2015-12-23 | 2015-12-23 | Promote durothermic cellulase |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201510992464.XA Division CN106906198B (en) | 2015-12-23 | 2015-12-23 | Cellulase for improving temperature resistance |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN110295155A true CN110295155A (en) | 2019-10-01 |
Family
ID=59206304
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201910635879.XA Pending CN110295155A (en) | 2015-12-23 | 2015-12-23 | Promote durothermic cellulase |
| CN201510992464.XA Expired - Fee Related CN106906198B (en) | 2015-12-23 | 2015-12-23 | Cellulase for improving temperature resistance |
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201510992464.XA Expired - Fee Related CN106906198B (en) | 2015-12-23 | 2015-12-23 | Cellulase for improving temperature resistance |
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| Country | Link |
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| CN (2) | CN110295155A (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN111826367B (en) * | 2019-04-16 | 2022-01-14 | 湖北大学 | Enzyme activity enhanced cellulase |
Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101583712A (en) * | 2007-01-18 | 2009-11-18 | 丹尼斯科美国公司 | Modified endoglucanase II and methods of use |
| CN101809150A (en) * | 2007-05-31 | 2010-08-18 | 诺维信股份有限公司 | Methods of increasing the cellulolytic enhancing activity of a polypeptide |
| CN103237891A (en) * | 2010-09-30 | 2013-08-07 | 诺维信股份有限公司 | Variants of polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| CN103814129A (en) * | 2011-09-14 | 2014-05-21 | 杜邦营养生物科学有限公司 | Compositions comprising enzymes with endo-1,4-beta-xylanase activity and enzymes with endo-1,3(4)-beta-glucanase activity |
| US20140308713A1 (en) * | 2013-04-05 | 2014-10-16 | Toni M. Lee | Endoglucanase having enhanced thermostability and activity |
| US20150050701A1 (en) * | 2013-04-05 | 2015-02-19 | California Institute Of Technology | Cellulase compositions having improved thermostability and synergy |
| CN104870639A (en) * | 2012-12-14 | 2015-08-26 | 诺维信公司 | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102643789B (en) * | 2011-02-17 | 2013-08-21 | 东莞泛亚太生物科技有限公司 | Cellulase and application thereof |
| CN102676476B (en) * | 2011-03-09 | 2014-06-04 | 东莞泛亚太生物科技有限公司 | Dextranase with improved enzyme activity and thermal stability |
-
2015
- 2015-12-23 CN CN201910635879.XA patent/CN110295155A/en active Pending
- 2015-12-23 CN CN201510992464.XA patent/CN106906198B/en not_active Expired - Fee Related
Patent Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101583712A (en) * | 2007-01-18 | 2009-11-18 | 丹尼斯科美国公司 | Modified endoglucanase II and methods of use |
| CN101809150A (en) * | 2007-05-31 | 2010-08-18 | 诺维信股份有限公司 | Methods of increasing the cellulolytic enhancing activity of a polypeptide |
| CN103237891A (en) * | 2010-09-30 | 2013-08-07 | 诺维信股份有限公司 | Variants of polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| CN103814129A (en) * | 2011-09-14 | 2014-05-21 | 杜邦营养生物科学有限公司 | Compositions comprising enzymes with endo-1,4-beta-xylanase activity and enzymes with endo-1,3(4)-beta-glucanase activity |
| CN104870639A (en) * | 2012-12-14 | 2015-08-26 | 诺维信公司 | Polypeptides having cellulolytic enhancing activity and polynucleotides encoding same |
| US20140308713A1 (en) * | 2013-04-05 | 2014-10-16 | Toni M. Lee | Endoglucanase having enhanced thermostability and activity |
| US20150050701A1 (en) * | 2013-04-05 | 2015-02-19 | California Institute Of Technology | Cellulase compositions having improved thermostability and synergy |
Also Published As
| Publication number | Publication date |
|---|---|
| CN106906198B (en) | 2019-12-13 |
| CN106906198A (en) | 2017-06-30 |
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