CN103589697B - One group of cyclodextrin glucosyltransferase and encoding gene thereof and application - Google Patents
One group of cyclodextrin glucosyltransferase and encoding gene thereof and application Download PDFInfo
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- C12N9/1074—Cyclomaltodextrin glucanotransferase (2.4.1.19)
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Abstract
The invention discloses one group of cyclodextrin glucosyltransferase and encoding gene thereof and application.This cyclodextrin glucosyltransferase, from soft rotten bacillus cereus (Bacillus macerans).Its gene order is suddenlyd change by the present invention, has obtained four kinds of muteins.Said mutation protein degradation starch and production cyclodextrin are compared research.It is higher that result shows that the cyclodextrin glucosyl transferase that some site mutation obtains produces the specificity of α CD, and production efficiency is higher, has substantial worth in commercial production.
Description
Technical field
The present invention relates to one group of cyclodextrin glucosyltransferase and encoding gene thereof and application.
Background technology
The English of cyclodextrin is cyclodextrin, is called for short CD.Cyclodextrin is cyclodextrin transglucosylase
(CGTase) act on the product of starch, be the member cyclic oligosaccharides that links with α-Isosorbide-5-Nitrae glycosidic bond of more than six glucoses,
Common, most study is alpha-cyclodextrin (α-CD), beta-schardinger dextrin-(β-CD), gamma-cyclodextrin (γ-CD), respectively by six, seven
Individual and eight glucose molecules are constituted, and are relatively large and relative flexibility molecules.
Cyclohexaamylose is a high-valued product of class of starch deep processing, by six glucosyl groups by α-Isosorbide-5-Nitrae glucose
The cyclic oligosaccharide that glycosidic bond is formed by connecting.Structurally, α-CD presents the stereochemical structure of cylindrical shape (one end is big, and one end is little),
There is the special nature of " outer hydrophilic, interior hydrophobic ".By the stereochemical structure that it is special, functionally so that it is can be with multiple object
Compound uses proper method to carry out inclusion, thus changes by dissolubility, volatility and the chemical reactivity etc. of inclusion material
Physicochemical property, in addition its safety non-toxic so that it is there are some highly useful functions.
α-CD is a kind of potential food additive, especially as the cycloheptaamylose produced at present
The substitute products of (β-CD).The existing large-scale production of β-CD, but in use find the risk that it has internal organs to deposit, and
The problem of inclusion inefficiency.
Summing up, α-CD has following application prospect in food industry: (1) is by compound low to water-insoluble or dissolubility
Make the encapsulation compound that water solubility is high；(2) it is (as protected color, protecting perfume, resistance to that the compound making encapsulating has good stability
Hot, acidproof, hydrolysis, antioxidation, volatilization prevention etc.)；(3) shielding action (covers unhappy abnormal smells from the patient and bitterness in food)；(4) remove
Remove unwanted composition (such as caffeine, cholesterol etc.) in food；(5) there is emulsifying, foaming effect, emulsifying agent and foaming can be made
Agent；(6) liquid, oily, volatile material solidification is made.
At present, the biggest obstacle of α-CD development and application is a lack of the enzyme preparation with high alpha-cyclodextrin conversion activity, makes
The cost and price obtaining this product exceeds three times of β-CD, limits its large-scale application.
The generation of α-CD, mainly with starch as raw material, through cyclodextrin glucosyltransferase (cyclodextrin
Glucano-transferase is called for short CGTases) glycosyl transformation.The specificity of CGTases is relatively low, mostly
Produce α-CD, β-CD and three kinds of products of γ-CD in the case of number simultaneously.Use three kinds of proportion of products that different CGTases produces
Difference, the main converted product of existing CGTases is β-CD, also produces a certain amount of α-and γ-CD simultaneously.Existing research
Direction is mainly two aspects: the first seeks from natural resources that catalytic effect is more preferable or the higher enzyme of specificity；It two is
Existing pheron is oriented transformation thus obtains that catalytic effect is more preferable or the higher enzyme of specificity.
Summary of the invention
It is an object of the invention to provide one group of cyclodextrin glucosyltransferase and encoding gene thereof and application.
The cyclodextrin glucosyltransferase that the present invention provides, from soft rotten bacillus cereus (Bacillus macerans),
It is that protein shown in the sequence 1 of sequence table is carried out the protein that following (a) and (b), (c) and (d) four sudden changes obtain:
A the sequence 1 of sequence table is sported three continuous print groups from N-terminal the 167th amino acids residue by tyrosine by ()
Propylhomoserin
B the sequence 1 of sequence table is sported three continuous print groups from N-terminal the 167th amino acids residue by tyrosine by ()
Propylhomoserin, is sported phenylalanine by the 195th amino acids residue by tyrosine simultaneously；
C the sequence 1 of sequence table is sported arginine from N-terminal the 89th amino acids residue by tyrosine by (), will simultaneously
167th amino acids residue is sported three continuous print histidine by tyrosine, and by the 195th amino acids residue by cheese ammonia
Acid mutation is phenylalanine.
D the sequence 1 of sequence table is sported arginine from N-terminal the 89th amino acids residue by tyrosine by (), will simultaneously
167th amino acids residue is sported three continuous print histidine by tyrosine, simultaneously by the 180th amino acids residue by sweet ammonia
Acid mutation is leucine, and by tyrosine, the 195th amino acids residue is sported phenylalanine.
The gene of code for said proteins falls within protection scope of the present invention.
Protein shown in the sequence 2 of sequence table is concretely carried out following (e), (f), (g) and (h) four by described gene
The DNA molecular that sudden change obtains:
E the sequence 2 of sequence table is sported CACCACCAC from 5 ' end 499-501 position nucleotide by TAC by ()
F the sequence 2 of sequence table is sported CACCACCAC by TAC, simultaneously from 5 ' end 499-501 position nucleotide by ()
583-585 position nucleotide is sported CGA by TAT；
G the sequence 2 of sequence table is sported CGA from 5 ' end 265-267 position nucleotide by TAT by (), simultaneously by
499-501 position nucleotide is sported CACCACCAC by TAC, and by TAC, 583-585 position nucleotide is sported TTC.
H the sequence 2 of sequence table is sported CGA from 5 ' end 265-267 position nucleotide by TAT by (), simultaneously by
499-501 position nucleotide is sported CACCACCAC by TAC, and by GGG, 538-540 position nucleotide is sported CTC, and by
583-585 position nucleotide is sported TTC by TAC.
Recombinant expression carrier, expression cassette, transgenic cell line or recombinant bacterium containing described gene belong to the present invention's
Protection domain.
Described recombinant expression carrier concretely by described gene insertion vector pET-22b (+) multiple clone site obtain
Recombiant plasmid.Described recombinant expression carrier concretely by described gene insertion vector pET-22b (+) BamHI and XhoI
The recombiant plasmid obtained between restriction enzyme site.
The recombinant bacterium that described recombinant expression carrier importing escherichia coli are concretely obtained by described recombinant bacterium.Described large intestine
Bacillus concretely e. coli bl21 (DE3).
The present invention also protects the application of described protein, for as follows (I) or (II) or (III):
(I) cyclodextrin glucosyltransferase is prepared；
(II) degradable starch (such as soluble starch)；
(III) cyclohexaamylose is produced.
The protein that the present invention provides, the specificity producing α-CD is higher, and production efficiency is higher, has in commercial production
Substantial worth.
Accompanying drawing explanation
Fig. 1 is the structural representation of recombiant plasmid first.
Fig. 2 is α-CD standard curve.
Fig. 3 is β-CD standard curve.
Fig. 4 is γ-CD standard curve
Detailed description of the invention
Below example facilitates a better understanding of the present invention, but does not limit the present invention.Experiment in following embodiment
Method, if no special instructions, is conventional method.Test material used in following embodiment, if no special instructions, is certainly
Routine biochemistry reagent shop is commercially available.Quantitative test in following example, is respectively provided with three times and repeats experiment, and result is made even
Average.Soluble starch: Beijing modern times east fine chemicals company limited, lot number: 20070216.Carrier pET-22b (+):
Novagen, catalog number is 69744-3.E. coli bl21 (DE3): Beijing Quanshijin Biotechnology Co., Ltd, product
Catalog number (Cat.No.) is CD601-01.
TB culture medium (g/L): tryptone 12, yeast extract cream 24, glycerol 4mL, distilled water constant volume.
The discovery of embodiment 1, mutain and encoding gene thereof
Screen the soft rotten bacillus cereus (Bacillus macerans) of a strain from nature, cyclodextrin glycosyl can be produced
Transferring enzyme, the cyclodextrin glycosyl transferases gene in this bacterial strain as shown in the sequence 2 of sequence table, sequence 1 institute of polynucleotide
The protein shown.
By-CGTase-1 the albumen of the named α of protein shown in sequence 1, by its encoding gene named α-CGTase-1 base
Because of (as shown in sequence 2).By-CGTase-WT the albumen of the named α of protein shown in sequence 3 (sequence disclosed in NCBI), by it
Encoding gene named α-CGTase-WT gene (as shown in sequence 4).
Sequence 1 is only that the 590th amino acids residue (M/V) and the 677th amino acids residue (S/ with the difference of sequence 3
G).Sequence 2 is only that the 1768th nucleotide (A/G) and the 2029th nucleotide (A/G) with the difference of sequence 4.
With double-stranded DNA shown in the sequence 1 of sequence table as template, 167 amino acids are suddenlyd change, obtain a sudden change
Body；167 and 195 amino acids are carried out rite-directed mutagenesis simultaneously, obtains a mutant；Same to 89,167 and 195 amino acids
Shi Jinhang rite-directed mutagenesis, obtains a mutant；89,167,180 and 195 amino acids are suddenlyd change simultaneously, obtains one
Mutant.By carrying out the albumen of each gene expression in mutant library, enzyme is alive to be identified, it was found that the product of a series of enzymes is special
One property is different from mutain and the encoding gene thereof of α-CGTase-WT albumen shown in sequence 1.
Embodiment 2, enzyme are lived and are identified
One, the difference following double chain DNA molecule of synthetic:
(1) double chain DNA molecule 1: be from 5 ' end 499-with the difference of DNA molecular shown in the sequence 2 of sequence table
501 nucleotide are suddenlyd change for CACCACCAC by TAC；Accordingly by the 167th amino acids residue in sequence 1 by tyrosine
Sport three continuous print histidine.The named albumen of albumen 1 of double chain DNA molecule 1 coding.
(2) double chain DNA molecule 2: be from 5 ' end 499-with the difference of DNA molecular shown in the sequence 2 of sequence table
501 nucleotide are sported CACCACCAC by TAC, and will be sported CGA from 5 ' end 583-585 position nucleotide by TAT；
Accordingly the 167th amino acids residue in sequence 1 is sported three continuous print histidine by tyrosine, and by the 195th
Amino acid residue is sported phenylalanine by tyrosine.The named albumen of albumen 2 of double chain DNA molecule 2 coding.
(3) double chain DNA molecule 3: be from 5 ' end 265-with the difference of DNA molecular shown in the sequence 2 of sequence table
267 nucleotide are sported CGA by TAT, will sport by TAC from 5 ' end 499-501 position nucleotide simultaneously
CACCACCAC, and TTC will be sported from 5 ' end 583-585 position nucleotide by TAC；Corresponding by the 89th in sequence 1
Amino acid residue is sported arginine by tyrosine, the 167th amino acids residue is sported three continuously by tyrosine simultaneously
Histidine, and the 195th amino acids residue is sported phenylalanine by tyrosine.The albumen life of double chain DNA molecule 3 coding
Entitled albumen 3.
(4) double chain DNA molecule 4: be from 5 ' end 265-with the difference of DNA molecular shown in the sequence 2 of sequence table
267 nucleotide are sported CGA by TAT, will sport by TAC from 5 ' end 499-501 position nucleotide simultaneously
CACCACCAC, and CTC will be sported from 5 ' end 538-540 position nucleotide by GGG, and will be from 5 ' end 583-585 positions
Nucleotide is sported TTC by TAC；Accordingly the 89th amino acids residue in sequence 1 is sported arginine by tyrosine, with
Time the 167th amino acids residue is sported three continuous print histidine by tyrosine, by the 180th amino acids residue by sweet ammonia
Acid mutation is leucine, and by tyrosine, the 195th amino acids residue is sported phenylalanine.Double chain DNA molecule 3 coding
The named albumen of albumen 3.
(5) double chain DNA molecule 5: the i.e. double chain DNA molecule shown in sequence 2 of sequence table.
(6) double chain DNA molecule 6: the i.e. double chain DNA molecule shown in sequence 4 of sequence table.
Two, the structure (structural representation is shown in Fig. 1) of recombiant plasmid
1, design pair of primers, is made up of S2 and A3.
S2:5 '-CGCGGATCCG-3’；
A3:5'-CGGCTCGAG -3’。
In S2, underscore mark BamHI restriction endonuclease recognition sequence, the region that square frame labelling is corresponding with target sequence.In A3, lower stroke
Line mark XhoI restriction endonuclease recognition sequence, the region that square frame labelling is corresponding with target sequence.
2, respectively with each double chain DNA molecule of the 2-in-1 one-tenth of step as template, with the primer of S2 and A3 composition to carrying out PCR
Amplification, obtains pcr amplification product.
3, with restricted enzyme BamHI and the pcr amplification product of XhoI double digestion step (1), digestion products is obtained.
4, with restricted enzyme BamHI and XhoI double digestion carrier pET-22b (+), reclaim carrier framework (about
5.4kb).
5, the digestion products of step (3) and the carrier framework of step (4) are connected, obtain recombiant plasmid.
According to the numbering of double chain DNA molecule, the most named recombiant plasmid 1 to recombiant plasmid 6.
According to sequencing result, recombiant plasmid 1 is carried out structure to be described as follows: carrier pET-22b (+) BamHI and XhoI
Double chain DNA molecule 1 is inserted between restriction enzyme site.
According to sequencing result, recombiant plasmid 2 is carried out structure to be described as follows: carrier pET-22b (+) BamHI and XhoI
Double chain DNA molecule 2 is inserted between restriction enzyme site.
According to sequencing result, recombiant plasmid 3 is carried out structure to be described as follows: carrier pET-22b (+) BamHI and XhoI
Double chain DNA molecule 3 is inserted between restriction enzyme site.
According to sequencing result, recombiant plasmid 4 is carried out structure to be described as follows: carrier pET-22b (+) BamHI and XhoI
Double chain DNA molecule 4 is inserted between restriction enzyme site.
According to sequencing result, recombiant plasmid 5 is carried out structure to be described as follows: carrier pET-22b (+) BamHI and XhoI
Double chain DNA molecule 5 is inserted between restriction enzyme site.
According to sequencing result, recombiant plasmid 5 is carried out structure to be described as follows: carrier pET-22b (+) BamHI and XhoI
Double chain DNA molecule 6 is inserted between restriction enzyme site.
Three, the structure of recombinant bacterium
Each recombiant plasmid that step 2 builds is directed respectively into e. coli bl21 (DE3), obtains each recombinant bacterium.Press
According to the numbering of recombiant plasmid, the most named recombinant bacterium 1 to recombinant bacterium 6.
Four, the fermentation of recombinant bacterium
By step 3 build each recombinant bacterium be seeded to respectively in TB culture medium, 37 DEG C, 220rpm shaken cultivation extremely
OD600nm=0.6 (0.6-0.8)；Add IPTG so that it is the concentration in cultivating system is 0.01mM, then 16 DEG C, 220rpm
Shaken cultivation 96h；Cultivating system 4 DEG C, 8000rpm are centrifuged 10 minutes, collect supernatant.
According to the numbering of recombinant bacterium, the most named supernatant 1 to supernatant 6.
Five, enzyme is lived and is identified and product analysis
1, enzyme activity determination
(1) the soluble starch aqueous solution of 0.25g/100mL is prepared.
(2) experimental group: add 0.4mL soluble starch aqueous solution in test tube, is incubated 15min, then adds in 40 DEG C of water-baths
Enter 0.1mL solution to be measured；Matched group group: be initially charged 1.5mL0.1mol/L HCl/water solution before adding solution to be measured, other is same
Experimental group；Experimental group and matched group mixing are placed in 40 DEG C of waters bath with thermostatic control insulation 10min, and then experimental group is added
1.5mL0.1mol/L HCl/water solution；Add 3mL0.1mol/L I2Liquid (solvent is water) and addition 5mL distilled water, mixing, fast
Speed light-metering absorption value at 700nm, and record experimental data.
Enzyme (U/mL)=(a-b)/a × 100 × extension rate alive；A is the light absorption value of matched group, and b is the extinction of experimental group
Value.
2, product analysis
Each supernatant (solution to be measured) step 4 obtained respectively is tested as follows: solvable by 10g/100mL
Property amidin boils 10min；Take 2mL after cooling to add in new EP pipe, then press 400U/g substrate and add solution to be measured,
It is settled to 4mL with distilled water, then in 40 DEG C of water-baths, stands 24 hours；Then 10min, 12000rpm are boiled centrifugal
10min, takes supernatant；HPLC analysis is carried out by taking 20uL after supernatant 0.45um ultrafiltration membrance filter.
The parameter that HPLC analyzes: Waters600HPLC chromatograph, Waters manual injector, chromatographic column Lichrosorb
NH2 (4.6mm × 150mm), Waters2414 Composition distribution, flowing is made up of 73 parts by volume of acetonitrile and 27 parts by volume water,
Flow velocity 1mL/min, column temperature 40 DEG C.
Standard curve is made respectively with α-CD standard substance, β-CD standard substance and γ-CD standard substance.α-CD standard substance go out peak
Time is 8.5min, and standard curve is shown in that Fig. 2, standard curve equation are y=1081101x-3448, and R2=0.9999, x represent α-CD
Concentration (g/100ml), y represents peak area.The appearance time of β-CD standard substance is 9.8min, and standard curve is shown in Fig. 3, and standard is bent
Line equation is y=1080914x-4309, and R2=0.9998, x represent the concentration (g/100ml) of β-CD, and y represents peak area.γ-CD
The appearance time of standard substance is 10.7min, and standard curve is shown in that Fig. 4, standard curve equation are y=1040306x-7683, R2=
0.9982, the x concentration (g/100ml) representing γ-CD, y represents peak area.(α-CD's is dense for concentration ÷ of the concentration of α-CD=α-CD
The concentration of the concentration+γ-CD of degree+β-CD) × 100%.(content+β-CD's of α-CD is dense for concentration ÷ of the concentration of β-CD=β-CD
The concentration of degree+γ-CD) × 100%, concentration ÷ of the concentration of γ-CD=γ-CD be (concentration+γ-CD's of the content+β-CD of α-CD
Concentration) × 100%.
Using supernatant 1 to carry out step 5 and obtain in supernatant, the percentage composition of α-CD is 79.5 ± 3.7%, the percentage of β-CD
Content is 14.2 ± 3.2%, and the percentage composition of γ-CD is 6.1% ± 0.9%.The percentage composition ratio of α-CD and β-CD is 5.8 ±
0.5.(Y167HHH)
Using supernatant 2 to carry out step 5 and obtain in supernatant, the percentage composition of α-CD is 79.9 ± 0.7%, the percentage of β-CD
Content is 13.6 ± 0.9%, and the percentage composition of γ-CD is 6.5% ± 0.4%.The percentage composition ratio of α-CD and β-CD is 5.9 ±
0.4.(Y167HHH/Y195F)
Using supernatant 3 to carry out step 5 and obtain in supernatant, the percentage composition of α-CD is 83.2 ± 1.9%, the percentage of β-CD
Content is 12.8 ± 1.4%, and the percentage composition of γ-CD is 4.0% ± 0.6%.The percentage composition ratio of α-CD and β-CD is 6.6 ±
0.8。(Y89R/Y167HHH/Y195F)
Using supernatant 4 to carry out step 5 and obtain in supernatant, the percentage composition of α-CD is 72.1 ± 1.3%, the percentage of β-CD
Content is 23.9 ± 1.2%, and the percentage composition of γ-CD is 4.0% ± 0.2%.The percentage composition ratio of α-CD and β-CD is 3.0 ±
0.1%。(Y89R/Y167HHH/G180L/Y195F)
Using supernatant 5 to carry out step 5 and obtain in supernatant, the percentage composition of α-CD is 65.4 ± 1.5%, the percentage of β-CD
Content is 21.2 ± 0.2%, and the percentage composition of γ-CD is 13.1 ± 0.8%.The percentage composition ratio of α-CD and β-CD is 3.1 ±
0.7%.(Y167).
Claims (3)
1. protein shown in the sequence 1 of sequence table carries out following (c) suddenly change the protein obtained:
C the sequence 1 of sequence table is sported arginine from N-terminal the 89th amino acids residue by tyrosine by (), simultaneously by the 167th
Amino acids residue is sported three continuous print histidine by tyrosine, and is dashed forward by tyrosine by the 195th amino acids residue
Become phenylalanine.
2. the gene of protein described in coding claim 1.
3. gene as claimed in claim 2, it is characterised in that: described gene is by nucleotides sequence shown in the sequence 2 of sequence table
Arrange and carry out the DNA molecular that following (g) sudden change obtains:
G the sequence 2 of sequence table is sported CGA by TAT, simultaneously by 499-501 from 5 ' end 265-267 position nucleotide by ()
Position nucleotide is sported CACCACCAC by TAC, and by TAC, 583-585 position nucleotide is sported TTC.
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| CN103232981A (en) * | 2013-05-06 | 2013-08-07 | 中国科学院微生物研究所 | A group of cyclodextrine glucosyltransferases and encoding gene and application thereof |
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| CN103232981A (en) * | 2013-05-06 | 2013-08-07 | 中国科学院微生物研究所 | A group of cyclodextrine glucosyltransferases and encoding gene and application thereof |
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