CN105779420A - High temperature-resistant acid arabinfuranosidease AbfaHLB and gene and application thereof - Google Patents
High temperature-resistant acid arabinfuranosidease AbfaHLB and gene and application thereof Download PDFInfo
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Abstract
The invention relates to the field of gene engineering, in particular to a high temperature-resistant acid arabinfuranosidease AbfaHLB and a gene and an application thereof. The arabinfuranosidease AbfaHLB comes from bacillus badius HLB, an amino acid sequence is shown in SEQ ID No.1, and an encoding gene abfa HLB for encoding the arabinfuranosidease AbfaHLB is provided. The arabinfuranosidease has the advantages that the following properties are realized, the suitable pH (potential of hydrogen) value is 4.5, the suitable temperature is 50 DEG C, and the thermal stability at the temperature of 80 DEG C is good; the arabinfuranosidease is used as a new enzyme preparation, and can be widely applied to feeds, foods, energy source industry and the like.
Description
Technical field
The present invention relates to genetic engineering field, in particular it relates to a kind of high temperature resistant acidic arabinofuranosidase AbfaHLB and gene, the recombinant vector comprising this gene and application.
Background technology
The basic sugar unit of xylan is D-xylopyranose, and its main chain is formed with β-Isosorbide-5-Nitrae glycosidic bond connection by xylose, and side chain is modified by various different substituent groups, and meanwhile, these side substitution groups are cross-linked mutually by chemical bond, form complicated structure.Xylan is a class polysaccharose substance the abundantest in hemicellulose, is widely present in hardwood (15-30%), cork (7-10%) and draft class plant (less than 30%).The degraded of xylan needs backbone hydrolysis enzyme and the synergism of side chain hydrolytic enzyme, backbone hydrolysis enzyme includes β-Isosorbide-5-Nitrae-xylanase and xylobiase, and side-chain hydrolysis enzyme needs α-l-arabinofuranosidase, phlorose aldehydic acid, the coenzyme such as acetyl xylan esterase.Wherein, arabinofuranosidase (α-l-arabinofuranosidase, EC3.2.1.55) can be hydrolyzed from the non-reducing end of the polymer containing arabinose residues such as arabinan, araboxylan, arabinogalactan etc. and generate an arabinose molecule.At present, the α-l-arabinofuranosidase of antibacterial, fungus and plant origin has been easily separated purification or by, after gene clone, heterogenous expression, furtheing investigate the various character of enzyme by people.The optimal reaction pH deriving from the arabinofuranosidase of microorganism is acid between neutrality (pH3.0-7.0), and optimal reactive temperature is between 40-70 DEG C.
Arabinofuranosidase is also extensively used in food service industry, and L-arabinose can replace traditional sucrose as the sweeting agent of a kind of low intake, is suitable to old people and hyperglycemic patients eats.Arabinofuranosidase can also increase the concentration of terpenol in wine brewing process, improves the fragrance of wine.It can also increase the clarity of fruit juice, and is applied to juice production industry.As one of hemicellulose degrading enzymes system, α-l-arabinofuranosidase participates in the recycling of agricultural product residue at a low price, produces to can be used for fermentation and generates monosaccharide and other side-products of alcohol fuel.Producing in the process of alcohol fuel at cellulose fermentation, have the former material thing of about 70% can not be completely degraded generation monosaccharide, suitable cellulose preprocessing process can strengthen cellulosic utilization rate.The method utilizing enzyme pretreatment then decreases the generation of these problems.Arabinofuranosidase is the Side chain cleavage enzyme of hemicellulose, and it can promote the degradable of hemicellulose.It addition, Arabinofuranosidases is as a kind of feed additive, eliminate arabinose side chains on xylan, promote the degraded of xylan, it is easy to digested and assimilated by animal.Therefore, the production of arabinofuranosidase, purification, nature and characteristic and the application in fields such as feed manufacturing, brewing industry, fruit juice production and the energy thereof deepen continuously.
Commercial production needs enzyme to carry out Short-Term High Temperature process, and most arabinofuranosidase optimum temperatures are at about 50 degree at present, but the character of poor heat stability can not meet feed granulating, brewages the industrial requirements such as processing.Therefore the enzyme obtaining good heat stability can reduce production cost, meets the different industry requirement to enzymatic property.
Summary of the invention
It is an object of the invention to provide the high temperature resistant acidic arabinofuranosidase of a kind of energy efficient application.
Another object of the present invention is to provide the gene encoding above-mentioned high temperature resistant acidic arabinofuranosidase.
It is a further object of the present invention to provide the recombinant vector comprising said gene.
It is a further object of the present invention to provide the recombinant bacterial strain comprising said gene.
It is a further object of the present invention to provide a kind of gene engineering method preparing above-mentioned high temperature resistant arabinofuranosidase.
Another object of the present invention provides the application of above-mentioned high temperature resistant arabinofuranosidase.
The present invention separates from bacillus badius BacillusbadiusHLB and obtains a kind of new high temperature resistant arabinofuranosidase AbfaHLB.
The invention provides a kind of high temperature resistant acidic arabinofuranosidase AbfaHLB, its aminoacid sequence is such as shown in SEQIDNO.1:
Wherein, 502 aminoacid of this enzyme gene code, no signal peptide sequence.
The arabinofuranosidase AbfaHLB of the present invention has good enzyme activity in acidity and neutral range, and has good heat stability.The present invention screens the arabinofuranosidase AbfaHLB of bacillus badius BacillusbadiusHLB and has the property that optimum pH 4.5, and there is the enzyme activity of more than 60% within the scope of pH2.0-6.0, there is good pH stability, after acting on 1h at 37 DEG C, between pH2.0-8.0, residual enzyme activity is all more than 85%.Optimum temperature 50 DEG C, still has the activity of more than 60%, good heat stability at 60 DEG C, 80 DEG C have good stability.
The invention provides the Gene A bfaHLB encoding above-mentioned high temperature resistant acidic arabinofuranosidase.Specifically, the genome sequence of this gene is such as shown in SEQIDNO.2:
The present invention is the encoding gene of arabinofuranosidase AbfaHLB by the method separating clone of PCR, and DNA complete sequence analysis is it is shown that the encoding gene abfaHLB total length 1509bp of arabinofuranosidase.
Maturation protein theoretical molecular is 56.6kDa, the coding gene sequence of arabinofuranosidase AbfaHLB and the aminoacid sequence derived are carried out BLAST comparison in GenBank, and this gene is 77% with the arabinofuranosidase sequence identity deriving from Alicyclobacillushesperidum.Illustrate that AbfaHLB is a kind of new arabinofuranosidase.
Present invention also offers the recombinant vector comprising above-mentioned arabinofuranosidase gene abfaHLB, it is preferred to pPIC9-abfaHLB.The arabinofuranosidase gene of the present invention is inserted between the restriction enzyme site that expression vector is suitable so that it is nucleotide sequence is exercisable to be connected with expression regulation sequence.The most preferred embodiment as the present invention, it is preferred to be inserted between EcoRI and the NotI restriction enzyme site on plasmid pPIC9 by the arabinofuranosidase gene of the present invention, obtains expression of recombinant yeast plasmid pPIC9-abfaHLB.
Present invention also offers the recombinant bacterial strain comprising above-mentioned high temperature resistant arabinofuranosidase glucosides gene abfaHLB, preferred described bacterial strain is escherichia coli, yeast, bacillus cereus or lactobacillus, more preferably Pichia yeast, for instance, recombinant bacterial strain GS115/abfaHLB.
Present invention also offers a kind of method preparing high temperature resistant acidic arabinofuranosidase AbfaHLB, comprise the following steps:
1) with above-mentioned recombinant vector transformed host cell, recombinant bacterial strain is obtained；
2) cultivating recombinant bacterial strain, induction restructuring arabinofuranosidase is expressed；
3) the arabinofuranosidase AbfaHLB also expressed by purification is reclaimed.
Wherein, it is preferable that described host cell is Pichia sp., it is preferable that recombinant expression plasmid is converted Pichia pastoris GS115, obtains recombinant bacterial strain GS115/abfaHLB.
Present invention also offers the application of above-mentioned arabinofuranosidase AbfaHLB.Preferably, it is provided that above-mentioned arabinofuranosidase AbfaHLB application in feedstuff and food industry, it is preferred that the application of araboxylan of degrading in feedstuff and food industry.
The present invention first to be solved technical problem is that overcomes the deficiencies in the prior art, it is provided that a kind of good properties, be suitable at feedstuff, wine brewing, arabinofuranosidase that Applications in Food Industry is new.The arabinofuranosidase optimum pH of the present invention is 4.5, has higher enzymatic activity at pH2.0-6.0；PH good stability.Its high-temperature stability, can make it apply in the commercial production of demand hot environment.This arabinofuranosidase is applicable to feed industry, with xylanase synergism, can effectively eliminate or reduce the anti-oxidant action caused because viscosity increases.In brewing industry, the araboxylan of solubility and the insolubility of can effectively degrading, the viscosity effectively reducing beerwort improves filter efficiency clarifying beer.It addition, contribute to increasing the concentration of terpenol in wine brewing process in Chinese liquor, the brewageing of rice wine, tart up.Therefore, the application in the food industry of this arabinofuranosidase demonstrates its huge potentiality.
The arabinofuranosidase AbfaHLB deriving from bacillus badius BacillusbadiusHLB in the present invention has the property that optimum pH 4.5, and there is the enzyme activity of more than 60% within the scope of pH2.0-6.0, there is good pH stability, after acting on 1h at 37 DEG C, between pH2.0-8.0, residual enzyme activity is all more than 80%.Optimum temperature 50 DEG C, still has the activity of more than 60%, good heat stability at 60 DEG C, 80 DEG C have good stability.The characteristics such as good pH and heat stability make it have very big potentiality on feedstuff, food industry applications.
Accompanying drawing explanation
Fig. 1 is the optimum pH of the recombination high temperature-resistant acidity arabinofuranosidase of the present invention.
Fig. 2 is the pH stability of the recombination high temperature-resistant acidity arabinofuranosidase of the present invention.
Fig. 3 is the optimum temperature of the recombination high temperature-resistant acidity arabinofuranosidase of the present invention.
Fig. 4 is the heat stability of the recombination high temperature-resistant acidity arabinofuranosidase of the present invention.
Detailed description of the invention
Test material and reagent
1, bacterial strain and carrier
Yeast expression vector pPIC9 and bacterial strain GS115 is purchased from Invitrogen company.
2, enzyme and other biochemical reagents
Enzyme and other biochemical reagents: restriction endonuclease is purchased from TaKaRa company, and ligase is purchased from Invitrogen company.P-nitrophenyl-a-L-arabionfuranoside (pNPAf) available from Sigma, other is all domestic reagent (all can be commercially available from common biochemical Reagent Company).
3, culture medium
(1) Escherichia coli culture medium LB (1% peptone, 0.5% yeast extract, 1%NaCl, pH nature).
(2) BMGY culture medium: 1% yeast extract, 2% peptone, 1.34%YNB, 0.00004%Biotin, 1% glycerol (V/V).
(3) BMMY culture medium: replacing glycerol divided by 0.5% methanol, all the other compositions are all identical with BMGY, pH is natural.
Illustrate: following example are not made the experimental methods of molecular biology illustrated, all carry out with reference to concrete grammar listed in " Molecular Cloning: A Laboratory guide " (third edition) J. Pehanorm Brooker one book, or carry out according to test kit and product description.
The clone of arabinofuranosidase gene abfaHLB in embodiment 1 bacillus badius BacillusbadiusHLB
Extract bacillus badius BacillusbadiusHLB genomic DNA:
(1) take 0.5-2mL and cultivate bacterium solution, 10000rpm, centrifugal 30s, draw supernatant as much as possible, collect thalline；
(2) adding 200 μ L buffer RB in EP pipe resuspended, 10000rpm is centrifuged 30s, abandons supernatant；
(3) for gram positive bacteria: add 120 μ L lysozyme, reverse mixing, 37 DEG C of water-bath 30-60min；
(4) the centrifugal 2min of 12000rpm, is resuspended in cell oscillation or piping and druming after abandoning supernatant in 180 μ L buffer RB；
(5) adding RNaseA (25mg/mL) solution 20 μ L, vibration mixing, room temperature places 5-10min；
(6) adding in conjunction with liquid CB800 μ L, add 100 μ L isopropanols, vortex oscillation fully mixes at once, is now likely to occur flocculent deposit；
(7) being added in an adsorption column AC by previous step mixture (including presumable precipitation), adsorption column is put in collecting pipe, and 13000rpm is centrifuged 30-60s, discards waste liquid；
(8) add mortifier and remove the centrifugal 30s of liquid IR500 μ L, 12000rpm, abandon waste liquid；
(9) 700 μ L rinsing liquid WB, 12000rpm are added, centrifugal 30s, discard waste liquid；
(10) 500 μ L rinsing liquid WB, 12000rpm are added, centrifugal 30s, discard waste liquid；
(11) putting back in sky collecting pipe by adsorption column AC, 13000rpm is centrifuged 2min, removes rinsing liquid as far as possible, and in a rinsing liquid, residual ethanol suppresses downstream reaction；
(12) taking out adsorption column AC, put in a clean centrifuge tube, add 100 μ L elution buffer EB in the middle part of adsorbed film, room temperature places the centrifugal 1min of 3-5min, 12000rpm.Rejoining in centrifugal adsorbing column by the solution obtained, room temperature places the centrifugal 1min of 2min, 12000rpm；
(13) DNA obtained is in-20 DEG C of preservations.
From NCBI gene database, obtain bacillus cereus source arabinofuranosidase AbfaHLB gene order carry out sequence alignment analysis, design synthetic primer P1, P2:
P1:5'-ATGTCTATGGATGTAGATCCACGTTTA-3'；
P2:5'-TACATTTACACGTAAACGAATCCAAGA-3'。
Pcr amplification is carried out for template with bacillus badius BacillusbadiusHLB STb gene.PCR response parameter is: 94 DEG C of degeneration 5min；Then 94 DEG C of degeneration 30sec, 45 DEG C of annealing 30sec, 72 DEG C extend 2min, 30 rear 72 DEG C of insulation 10min of circulation, obtain the fragment of a treaty 1500bp size, after being attached conversion with pEASY-T3 carrier after this fragment being reclaimed, send the order-checking of the farsighted Bo Xinke Bioisystech Co., Ltd in Beijing.Obtained the genetic fragment of 1509bp by gene sequencing, encode 502 aminoacid and a termination codon.
The preparation of embodiment 2 arabinofuranosidase AbfaHLB
Primer is expressed in gene order design synthesis according to the arabinofuranosidase AbfaHLB obtained:
P3:5'-GATGAATTCATGTCTATGGATGTAGATCCACGTTTA-3'；
P4:5'-GCTGCGGCCGCTACATTTACACGTAAACGAATCCAAGA-3'。
Again pcr amplification is carried out with bacillus badius BacillusbadiusHLB STb gene for template, it is thus achieved that with the arabinofuranosidase AbfaHLB gene of restructuring restriction enzyme site.Expression vector pPIC9 is carried out double digestion (EcoRI+NotI), simultaneously by gene abfaHLB double digestion (EcoRI+NotI) of encoding arabinose furanoside enzyme, enzyme action goes out the genetic fragment of encoding mature arabinofuranosidase and is connected with expression vector pPIC9, obtain the recombiant plasmid pPIC-abfaHLB containing BacillusbadiusHLB arabinofuranosidase gene abfaHLB electroporated Pichia pastoris GS115, it is thus achieved that recombinant pichia yeast strain GS115/abfaHLB.
By the GS115 bacterial strain containing recombiant plasmid, it is inoculated in 400mLBMGY culture fluid, after 30 DEG C of 250rpm shaken cultivation 48h, centrifugal collection thalline.Then utilize 200mLBMMY culture medium resuspended, 30 DEG C of 250rpm shaken cultivation.After induction 72h, centrifugal collection supernatant.Measuring the vigor of arabinofuranosidase, the expression of restructuring arabinofuranosidase is 60U/mL.
Embodiment 3 is recombinated the activity analysis of arabinofuranosidase AbfaHLB
The mensuration of nofuranosidase activity: measure the amount of the enzyme hydrolysis substrate pNPAf product p-nitrophenol generated under 405nm.Reactions steps: 250 μ L2mMpNPAf substrates and the mixing of 150 μ L buffer, adds the 100 μ L enzyme liquid suitably diluted, reacts 10min in 40 DEG C, add 1.5mL1MNa2CO3Terminate reaction, measure OD value in 405nm place.
Embodiment 4 is recombinated the property testing of arabinofuranosidase AbfaHLB
1, the optimum pH of arabinofuranosidase AbfaHLB of recombinating and the mensuration of pH stability
The restructuring arabinofuranosidase AbfaHLB of embodiment 3 purification is carried out enzymatic reaction to measure its optimum pH under different pH.The substrate 0.1mol/L citrate-phosphate disodium hydrogen buffer configuration of different pH, carries out arabinofuranosidase vitality test under 37 DEG C of conditions.Result (Fig. 1) shows, the optimum pH of restructuring arabinofuranosidase is 4.5, has the relative activity of more than 50% at pH2.0-7.0.Restructuring arabinofuranosidase 37 DEG C of process 60min in the buffer of above-mentioned various different pH, then in pH4.5 buffer solution system, under 37 DEG C of conditions, measure enzymatic activity, to study the pH stability of recombinase.Result (Fig. 2) shows that restructuring arabinofuranosidase is all very stable between pH2.0-8.0, and after processing 60min within the scope of this pH, residual enzyme activity is more than 85%, and this illustrates that this enzyme pH toleration is comparatively wide in range.
2, recombinate the optimum temperature of arabinofuranosidase AbfaHLB and thermal stability determination
Being determined as of optimum temperature of restructuring arabinofuranosidase AbfaHLB carries out enzymatic reaction under citrate-phosphate disodium hydrogen buffer (pH4.5) buffer solution system and different temperatures.Temperature tolerance is determined as arabinofuranosidase AbfaHLB and processes different time at different temperatures, then carries out enzyme assay at 37 DEG C.Enzyme reaction optimum temperature measurement result (Fig. 3) shows that its optimum temperature is 50 DEG C, all keeps high enzyme to live at 20-65 DEG C.The heat stabilization test of enzyme shows (Fig. 4), restructuring arabinofuranosidase AbfaHLB has good heat stability, and incubation 2h at 70 DEG C can keep the enzymatic activity of more than 90%, and at 80 DEG C incubation 10min, the enzymatic activity of more than 80% can be remained.
3, the different chemical reagent impact on restructuring arabinofuranosidase AbfaHLB activity
Enzymatic reaction system adds different metal ions and the chemical reagent of variable concentrations, studies its impact on enzymatic activity, the final concentration of 1mmol/L of various materials.50 DEG C, pH4.5 when measure enzymatic activity.It is shown that most of ions and chemical reagent beta-mercaptoethanol and EDTA are recombinated when concentration is 1mmol, the vigor of arabinofuranosidase does not have significant change.But Ag+, Hg2+ almost can suppress its vigor completely, and SDS its vigor of also strong inhibition.
4, recombinate the antitrypsin of arabinofuranosidase AbfaHLB and the detection of pepsin ability
0.1mg/mL pepsin is configured, pH7.0 citrate-phosphate disodium hydrogen buffer configuration 0.1mg/mL trypsin with pH2.0Gly-HCl buffer.After the arabinofuranosidase AbfaHLB of purification is processed 120min in 10:1 (w/w) ratio in this protease buffer with protease, different time samplings, the residual enzyme detecting treatment enzyme by standard method is lived.It is shown that arabinofuranosidase AbfaHLB is with after pepsin 120min, residue enzyme activity is 96.9%, after trypsin treatment 120min, remains enzyme activity 94.7%.Illustrate that arabinofuranosidase AbfaHLB has the ability of good antipepsin and trypsin hydrolyzing.
Claims (8)
1. a high temperature resistant acidic arabinofuranosidase AbfaHLB, it is characterised in that its aminoacid sequence is such as shown in SEQIDNO.1.
2. a high temperature resistant acidic arabinofuranosidase gene abfaHLB, it is characterised in that coding arabinofuranosidase AbfaHLB described in claim 1.
3. high temperature resistant acidic arabinofuranosidase gene abfaHLB as claimed in claim 2, it is characterised in that its base sequence is such as shown in SEQIDNO.2.
4. comprise the recombinant vector of high temperature resistant acidic arabinofuranosidase gene abfaHLB described in Claims 2 or 3.
5. recombinant vector according to claim 4, it is characterised in that described recombinant vector is pPIC9-abfaHLB.
6. comprise the recombinant bacterial strain of high temperature resistant acidic arabinofuranosidase gene abfaHLB described in Claims 2 or 3.
7. the method preparing high temperature resistant acidic arabinofuranosidase AbfaHLB, it is characterised in that comprise the following steps:
1) with the recombinant vector transformed host cell of claim 4 or 5, recombinant bacterial strain is obtained；
2) cultivating recombinant bacterial strain, induction restructuring arabinofuranosidase AbfaHLB expresses；
3) the arabinofuranosidase AbfaHLB also expressed by purification is reclaimed.
8. the application of high temperature resistant acidic arabinofuranosidase AbfaHLB described in claim 1.
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109402089A (en) * | 2018-11-06 | 2019-03-01 | 江苏大学 | A kind of thermostable type arabinofuranosidase and its application |
| CN110484524A (en) * | 2019-09-02 | 2019-11-22 | 中国农业科学院饲料研究所 | Arabinofuranosidase BoAra43A and its encoding gene and application |
| CN116179516A (en) * | 2022-12-29 | 2023-05-30 | 云南师范大学 | alpha-L-arabinofuranosidase and application thereof |
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| CN102719417A (en) * | 2012-07-02 | 2012-10-10 | 武汉新华扬生物股份有限公司 | High-temperature resistance arabinfuranosidease Abf51B8, as well as gene and application thereof |
| CN103409397A (en) * | 2013-09-02 | 2013-11-27 | 南京林业大学 | High-temperature-resistant acid arabinosidase as well as coding gene and application thereof |
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| CN102719417A (en) * | 2012-07-02 | 2012-10-10 | 武汉新华扬生物股份有限公司 | High-temperature resistance arabinfuranosidease Abf51B8, as well as gene and application thereof |
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Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN109402089A (en) * | 2018-11-06 | 2019-03-01 | 江苏大学 | A kind of thermostable type arabinofuranosidase and its application |
| CN110484524A (en) * | 2019-09-02 | 2019-11-22 | 中国农业科学院饲料研究所 | Arabinofuranosidase BoAra43A and its encoding gene and application |
| CN116179516A (en) * | 2022-12-29 | 2023-05-30 | 云南师范大学 | alpha-L-arabinofuranosidase and application thereof |
| CN116179516B (en) * | 2022-12-29 | 2024-01-26 | 云南师范大学 | alpha-L-arabinofuranosidase and application thereof |
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