CN105602870A - Aminopeptidase producing strain bacillus axarquiensis SWJSX8 and application thereof - Google Patents

Aminopeptidase producing strain bacillus axarquiensis SWJSX8 and application thereof Download PDF

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CN105602870A
CN105602870A CN201610072276.XA CN201610072276A CN105602870A CN 105602870 A CN105602870 A CN 105602870A CN 201610072276 A CN201610072276 A CN 201610072276A CN 105602870 A CN105602870 A CN 105602870A
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aminopeptidase
swjsx8
producing strain
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bacterial strain
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CN105602870B (en
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赵谋明
雷芬芬
赵强忠
苏国万
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South China University of Technology SCUT
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    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/485—Exopeptidases (3.4.11-3.4.19)

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Abstract

The invention belongs to the technical field of microbiological screening and fermentation and discloses an aminopeptidase producing strain bacillus axarquiensis SWJSX8 and an application thereof. The aminopeptidase producing strain bacillus axarquiensis SWJSX8 is collected in the China General Microbiological Culture Collection Center (CGMCC) on June 10th, 2015, and the collection number is CGMCC No.10974. In the invention, the aminopeptidase producing strain bacillus axarquiensis SWJSX8 from deep sea is screened, the culture conditions are simple, the genetic properties are stable, and the produced aminopeptidase has relatively high primer specificity. The strain is likely to become a novel aminopeptidase producing strain or provide a new aminopeptidase coding gene and has a good prospect in study and application.

Description

A kind of product aminopeptidase bacterial strain Bacillus axarquiensis SWJSX8 and application thereof
Technical field
The invention belongs to microbe to screen and fermentation technical field, be specifically related to a kind of aminopeptidase bacterial strain Bacillus that producesAxarquiensisSWJSX8 and application thereof.
Background technology
Protease is the enzyme that a class can aminosal peptide bond, closely bound up with the mankind's life. Food protein warpProtease controlled enzymatic hydrolysis can improve nutritive peculiarity and the functional characteristic of protein, prepares biologically active peptide, thereby greatly improvesThe using value of protein. Had at present more rich commercial protease kind, as papain, neutral proteinase,Alkali protease, trypsase, compound protease, flavor protease etc. Alkali protease, papain are by more researchPerson's report has good hydrolysis effect to aquatic products, animal protein, but the hydrolysis effect of these protease to phytoproteinUnsatisfactory, there is the problems such as degree of hydrolysis is low, protein recovery is low, heavy bitter taste. These problems are mainly the enzymes by proteaseCut that the restriction in site causes. Protease can be divided into endo protease and exoproteinase according to its mode of action: inscribe albumenEnzyme mainly, from the inside cutting peptide bonds of peptide chain, generates micromolecular polypeptide; Exoproteinase is divided into aminopeptidase and carboxypeptidase, respectivelyFrom N end or the C end order hydrolysis amino acid of peptide chain, amino acid is discharged one by one. Above-mentioned commercial protease is except local flavor eggWhite enzyme, trypsase are outside the mixture of endo protease and exoproteinase, and major part is all endo protease, acts on and plantsOnly can be from inner cutting peptide bonds when thing protein, generate the polypeptide of larger molecular weight, and make hydrophobic grouping expose in a large number bitter taste to addHeavy. Therefore the exploitation of strengthening exoproteinase is significant to the application of raising phytoprotein.
Microbe-derived aminopeptidase has received researchers' concern always. Johnson equal 1936 first fromIn the metabolite of Aspergillusparasiticus, find aminopeptidase; 1996, the utilizations such as ChoiIt is 0.16LAPmL that Lactobacilluscaseissp.casei produces aminopeptidase level-1Left and right; The utilizations such as Zhang JinhuBacilluscereusCZ produces aminopeptidase and reaches 94.28UmL-1, the withered grass bud of the Tian Yaping of Southern Yangtze University professor team seed selectionSpore bacillus Zj016 produces aminopeptidase and reaches 5500UmL-1. The bacterial strain aminopeptidase diversity ratio of having reported is larger, this may with mensuration sideMethod and enzyme are lived definition unit are different and have certain relation, and also You compare great district of the zymologic property of aminopeptidase that different microorganisms is producedNot. The BacillusaxarquiensisSWJSX8 wild strain relating in the present invention separates and obtains from halmeic deposit,Through initial optimization condition of culture, the vigor that produces aminopeptidase is reaching 2.8LAPmL-1Left and right, stable hereditary property. PseudomonasThe relevant report of Bacillusaxarquiensis is also fewer, and the research of producing aminopeptidase about it is reported first herein,Can provide new production bacterial classification and theoretical foundation for the exploitation of aminopeptidase product.
Summary of the invention
Based on above prior art, primary and foremost purpose of the present invention is to provide source, a kind of deep-sea, micro-life of producing aminopeptidaseThing bacterial strain BacillusaxarquiensisSWJSX8.
Another object of the present invention is to provide mentioned microorganism bacterial strain BacillusaxarquiensisSWJSX8 to existLiquid fermentation produces the application in aminopeptidase.
The object of the invention is achieved through the following technical solutions:
A microbial strains BacillusaxarquiensisSWJSX8 for source, deep-sea, product aminopeptidase, this bacterial strainSeparate from South Sea absmal deposit matter sample, adopt casein plate primary dcreening operation and shake flask fermentation aminopeptidase activity to measure multiple sieve and obtain,Classification And Nomenclature is BacillusaxarquiensisSWJSX8. This bacterial strain has been preserved in Chinese micro-life on June 10th, 2015Thing culture presevation administration committee's common micro-organisms center, preservation address is the Yard 1, BeiChen xi Road, Chaoyang District, Beijing City Chinese Academy of SciencesInstitute of microbiology, deposit number is CGMCCNo.10974.
Through Morphological Identification and biological biochemistry characteristic research, the bacterial strain that deposit number is CGMCCNo.10974 is flat at caseinOn plate, colonial morphology is as follows: bacterium colony is rounded, and diameter is less, smooth moistening, and neat in edge is light yellow, sticky shape; (2) cellForm: Gram-positive, shaft-like, produce gemma; (3) physiological and biochemical property: aerobic growth, can utilize glucose, sucrose, wheatBud sugar, lactose, sweet mellow wine, D-glucitol and inositol, can not utilize rhamnose, the Starch Hydrolysis positive, the gelatin liquefaction positive, methylRed negative, the V-P test positive, indole negative, urease negative, oxidase positive, do not produce H2S。
The 16SrRNA gene that is CGMCCNo.10974 bacterial strain to deposit number carries out pcr amplification and sequencing, surveysObtaining 16SrDNA genetic fragment length is 1440bp, and concrete sequence is shown in sequence table. Listed in this gene order and GenbankGene order analysis learns, BacillusaxarquiensisstrainBPRIST011 phase in this bacterial strain and databaseThe highest like property, homology reaches 99%, identifies that this bacterial strain is Bacillusaxarquiensis.
Mentioned microorganism bacterial strain BacillusaxarquiensisSWJSX8 produces the application in aminopeptidase at liquid fermentation.
Tool of the present invention has the following advantages and beneficial effect:
The present invention's screening obtains the bacterial strain BacillusaxarquiensisSWJSX8 of the product aminopeptidase in source, deep-sea, itsCondition of culture is simple, stable hereditary property, and the aminopeptidase that produces has stronger substrate specificity. This bacterial strain may become novel ammonia peptideThe production bacterial classification of enzyme or new aminopeptidase encoding gene is provided, is worth continuing to strengthen theoretical research and base application research.
Brief description of the drawings
Fig. 1 is different fermentations temperature is produced aminopeptidase influence curve figure to bacterial strain SWJSX8;
Fig. 2 is the initial pH of different culture media produces aminopeptidase influence curve figure to bacterial strain SWJSX8;
Fig. 3 is different liquid amounts produce aminopeptidase influence curve figure to bacterial strain SWJSX8;
Fig. 4 is the influence curve figure that the different fermentations time bacterial strain SWJSX8 is produced to aminopeptidase;
Fig. 5 is the substrate specificity comparison diagram of bacterial strain aminopeptidase that SWJSX8 produces.
Detailed description of the invention
Below in conjunction with embodiment and accompanying drawing, the present invention is described in further detail, but embodiments of the present invention are not limitIn this.
Enrichment and seed culture medium: peptone 5g, dusty yeast 1g, artificial seawater 1L, pH7.4.
Casein culture medium: casein 10g, beef extract 3g, potassium dihydrogen phosphate 2g, agar powder 15g, artificial seawater 1L,PH7.2 left and right.
Fermentation medium: glycerine 3g, glucose 5g, dusty yeast 10g, potassium dihydrogen phosphate 0.5g, magnesium sulfate 0.3g, ammonium sulfate1g, calcium chloride 1g, sea salt 10g, pH7.2 left and right.
Produce the separation screening of the CGMCCNo.10974 of aminopeptidase:
Enrichment culture: take 2g deep-sea ooze sample sample in 50mL sterilizing centrifuge tube, add 15mL sterile distilled water, fullyMix, jolting 30min in shaking table, gets supernatant 1mL (25mL/250mL) in enriched medium after leaving standstill, and 37 DEG C,120rpm, cultivates 48h.
Primary dcreening operation: the nutrient solution 1mL getting after enrichment adds in 9mL sterile physiological water, is diluted to different gradients by multiple proportions method(10-1-10-7). Choose 10-4，10-5，10-6，10-7Dilution factor, respectively draws 0.1mL, adds in the casein culture medium having solidified,Coating evenly. Inversion is placed in 37 DEG C of incubators and cultivates 24-48h.
Separation and purification: select the bacterium colony that has obvious hydrolysis circle in above-mentioned casein plate, connect on new casein plateContinuous line separates more than three times, until be pure culture. Select the larger single bacterium colony of hydrolysis circle and be stored on test tube slant,Be preserved in 4 DEG C of refrigerators.
Shake flask fermentation sieves again: by the inoculation of above-mentioned preservation, in seed culture medium, 37 DEG C, 150rpm, activates 12h,Be inoculated in fermentation medium with 2% inoculum concentration, 37 DEG C, 150rpm, cultivates 48h. Zymotic fluid is at 4 DEG C, and 10000rpm is centrifugal10min, gets supernatant and is crude enzyme liquid. Adopt LNA method to measure aminopeptidase vigor, sift out again liquid fermentation aminopeptidase output highBacterial strain.
Aminopeptidase activity is measured: crude enzyme liquid is diluted to suitable concentration with the Tris-HCl cushioning liquid of pH8.0, gets80 μ L sample diluting liquids add in 96 orifice plates, add 20 μ LL-leucine paranitroanilinum (L-leu-pNA), accurately anti-at 40 DEG CAnswer after 10min, add 100 μ L absolute ethyl alcohol cessation reactions, measure the light absorption value under 405nm. With variable concentrations paranitroanilinumLight absorption value drawing standard curve under 405nm. 40 DEG C of enzymolysis L-Leu-paranitroanilinum per minute produce 1 μ mol to nitreThe required enzyme amount of base aniline is a Ge Meihuo unit.
Produce the qualification of the CGMCCNo.10974 of aminopeptidase:
The CGMCCNo.10974 of activation is inoculated in LB culture medium, and 37 DEG C, 150rpm cultivates 10h, gets 1.5mL new4 DEG C of fresh bacterium liquid, the centrifugal 5min of 10000rpm, collects thalline in 2mL centrifuge tube, adopts DNA to extract kit and extracts DNA. ElectricitySwimming detect after adopt universal primer carry out PCR (forward primer: 5 '-AGAGTTTGATCCTGGCTCAG-3 ', reverse primer: 5 '-GGTTACCTTGTTACGACTT-3’)。
Amplification overall reaction system is (20 μ L): templet gene DNA0.5 μ L; The each 1.0 μ L of upstream and downstream primer (20 μ mol/l);TaqDNA polymerase 0.2 μ L; 10 × buffer2.0 μ L; 4 kinds of deoxyribonucleoside acid blend dNTP (each 2.5mmol/L), 1.6 μL，25mmol/LMgCl21.6 μ L, distilled water (ddH2O) 12.1 μ L. Pcr amplification condition: 95 DEG C of 5min; 95 DEG C of 30s; 55 DEG C30s; 72 DEG C of 1.5min; 72 DEG C of 10min; 10 DEG C, totally 30 circulations. After PCR product purification, complete the 16SrRNA gene of mensurationGenetic fragment length is 1440bp, the highest with BacillusaxarquiensisstrainBPRIST011 similitude, homologyProperty reach 99%, concrete sequence is shown in sequence table, identifies that CGMCCNo.10974 is BacillusaxarquiensisSWJSX8.
BacillusaxarquiensisSWJSX8 liquid fermentation produces the condition optimizing of aminopeptidase:
The optimization of fermentation temperature: respectively at 25 DEG C, 30 DEG C, 37 DEG C, 40 DEG C bottom fermentations, the initial pH7 of culture medium, liquid amount10%, shaking speed 150rpm, cultivates 48h. The aminopeptidase vigor of measuring crude enzyme liquid at different fermentations temperature, the results are shown in Figure 1,37 DEG C of bottom fermentation aminopeptidase vigor are the highest.
The initial pH of culture medium optimizes: the initial pH that regulates respectively culture medium is 6.0,7.0,8.0,9.0,10.0, liquid amount10%, at 37 DEG C of bottom fermentations, shaking speed 150rpm, cultivates 48h. Measure the ammonia of crude enzyme liquid under the initial pH condition of different culture mediaPeptidase activity, the results are shown in Figure 2, and when the initial pH7-9 of culture medium, aminopeptidase vigor is higher, and wherein vigor is the highest when pH8.
The optimization of liquid amount: shake flask fermentation carries out in 250mL conical flask, liquid amount is respectively 10%, 20%, 30%,40%, at 37 DEG C, the initial pH8 of culture medium, 150rpm condition bottom fermentation 48h. Measure the ammonia peptide of crude enzyme liquid at different fermentations temperatureEnzyme activity, the results are shown in Figure 3, and liquid amount aminopeptidase vigor 10% time is all higher, and when liquid amount continues to increase, aminopeptidase output is fastPrompt drop is low.
The optimization of fermentation time: at 37 DEG C, the initial pH8 of culture medium, liquid amount 10%, 150rpm condition bottom fermentation, from 0-In 56h, in front 24h, get sample one time every 8h, in rear 48h, every 4h continuous sampling, measure aminopeptidase output and prolong with fermentation timeLong variation tendency. The results are shown in Figure 4, it is maximum that aminopeptidase accumulation in the time of 52h reaches, but growth compared with enzyme activity during with 48hNot remarkable, along with the time continues to extend, there is certain decline, therefore selection fermentation time is 48h.
The substrate specificity of aminopeptidase that BacillusaxarquiensisSWJSX8 produces:
Under identical condition, measure respectively different amino acid-paranitroanilinum AA-pNA (Leu-pNA, Phe-pNA,Ala-pNA, Arg-pNA, Glu-pNA, Lys-pNA, Pro-pNA and Met-pNA) vigor of aminopeptidase during as substrate, withThe vigor of Leu-pNA during as substrate is 100%, the results are shown in Figure 5. Aminopeptidase is to Leu-pNA and Arg-pNA as shown in Figure 5Substrate specificity is the strongest, and aminopeptidase vigor is higher, and Lys-pNA is had to stronger substrate specificity, to the specificity of other substratesA little less than.
BacillusaxarquiensisSWJSX8 genetic stability:
Its aminopeptidase vigor is cultivated and is measured in the BacillusaxarquiensisSWJSX8 continuous passage of preservation, withEnzyme activity is as the genetic stability of index comprehensive evaluation bacterial strain. The results are shown in Table 1, go down to posterity 8 times, aminopeptidase vigor remains on2.8LAP·mL-1Left and right, genetic stability is good.
Table 1
Above-described embodiment is preferably embodiment of the present invention, but embodiments of the present invention are not subject to above-described embodimentRestriction, other any do not deviate from change, the modification done under Spirit Essence of the present invention and principle, substitutes, combination, simplification,All should be equivalent substitute mode, within being included in protection scope of the present invention.

Claims (2)

1. produce an aminopeptidase bacterial strain, it is characterized in that: this bacterial strain is BacillusaxarquiensisSWJSX8, in 2015Be preserved in China Committee for Culture Collection of Microorganisms's common micro-organisms center on June 10, in, and deposit number is CGMCCNo.10974。
2. product aminopeptidase bacterial strain BacillusaxarquiensisSWJSX8 claimed in claim 1 produces ammonia peptide at liquid fermentationApplication in enzyme.
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Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN104651283A (en) * 2015-03-06 2015-05-27 华南理工大学 Bacillus cereus and applications thereof in production of aminopeptidase

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN104651283A (en) * 2015-03-06 2015-05-27 华南理工大学 Bacillus cereus and applications thereof in production of aminopeptidase

Non-Patent Citations (2)

* Cited by examiner, † Cited by third party
Title
MD. IFTEKHARUL WAHID ET AL.: "Purification and Characterization of Leucine Aminopeptidase from Marine Labyrinthulid Strain 00-Bat-05", 《AQUACULTURE SCI.》 *
向军: "产氨肽酶甲基营养型芽孢杆菌的鉴定、发酵优化及酶学性质研究", 《中国优秀硕士学位论文全文数据库 基础科学辑》 *

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