CN104651283A - Bacillus cereus and applications thereof in production of aminopeptidase - Google Patents

Bacillus cereus and applications thereof in production of aminopeptidase Download PDF

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CN104651283A
CN104651283A CN201510100394.2A CN201510100394A CN104651283A CN 104651283 A CN104651283 A CN 104651283A CN 201510100394 A CN201510100394 A CN 201510100394A CN 104651283 A CN104651283 A CN 104651283A
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aminopeptidase
bacillus cereus
cgmcc
swjs
vigor
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赵谋明
崔春
雷芬芬
赵强忠
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South China University of Technology SCUT
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    • 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
    • C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
    • C12N1/20—Bacteria; Culture media therefor
    • C12N1/205—Bacterial isolates
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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    • C12R2001/00—Microorganisms ; Processes using microorganisms
    • C12R2001/01—Bacteria or Actinomycetales ; using bacteria or Actinomycetales
    • C12R2001/07—Bacillus
    • C12R2001/085—Bacillus cereus
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/485—Exopeptidases (3.4.11-3.4.19)

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Abstract

The invention relates to a bacillus cereus and applications thereof in production of aminopeptidase. The Bacillus cereus SWJS 54 coming from deep sea and producing aminopeptidase is collected in China General Microbiological Culture Collection Center (CGMCC) at 23rd, September, 2014, with the collection number of CGMCC No.9697. The most appropriate temperature of the strain producing aminopeptidase is at 60DEG C, the activity is basically unchanged for 30 min at the temperature of no more than 55DEG C; the most appropriate pH is 9.5, and the bacillus cereus has better stability within the pH range of 5-10. The enzyme has strong hydrolysis capacity on peptide bond with N terminal of leucine and methionine, and belongs to leucine aminopeptidase. The bacillus cereus can be syngeneic with incision enzyme so as to improve the utilization rate of proteolysis, debitterize a proteolysis liquid, and prepare a biological active peptide and the like.

Description

One strain bacillus cereus and the application in product aminopeptidase thereof
Technical field
The present invention relates to one strain deep-sea source aminopeptidase produce bacterial strain, be specifically related to bacillus cereus ( bacillus cereussWJS 54) and the aminopeptidase that produces of liquid fermenting.
Background technology
Aminopeptidase is the excision enzyme that a class is held sequential hydrolysis amino acid from the N of polypeptide chain, amino acid is discharged one by one, is distributed widely in animal, plant and microorganism.Exopeptidase relates generally to signal transduction, the adjustment of peptide hormone, the process such as protein bound and digestion in vivo, so be the important topic in medical field always.On the other hand aminopeptidase also has important application in the food industry, as realize protein depth hydrolysis, weaken protein enzymatic hydrolyzate bitter taste, prepare biologically active polypeptides etc.The research of aminopeptidase starts from 1936, and Johnson etc. have found that three kinds derive from aspergillus parasiticuspeptase, through the development of decades, Chinese scholars has the report of the research about new aminopeptidase successively.But the product that the business aminopeptidase can found up till now in foodstuffs industry only has Rhodia Food and NOVO company to produce, aminopeptidase vigor is respectively 220 LAPg -1with 500 LAPg -1.Existing aminopeptidase product obviously can not meet foodstuffs industry heavy demand, and the exploitation of aminopeptidase product has important application prospect.
The source of current aminopeptidase mainly contains two aspects, and one is that extraction and isolation goes out some aminopeptidases from the pancreas of higher animal and intestinal juice, muscle, there is the problems such as extraction process complexity, extraction efficiency be low; Another one important sources is exactly the aminopeptidase that Institute of Micro-biology produces.The level that H.Choi equals to utilize milk-acid bacteria to produce aminopeptidase for 1996 is 0.16 LAPmL -1left and right, field sub-equal utilization subtilis Zj016 produces aminopeptidase and reaches 5500 UmL -1, Zhao Guangao etc. utilize mutagenesis aspergillus oryzae production aminopeptidase to reach 323.1 UmL -1deng.Bacterial strain mainly aspergillus oryzae, monascus, subtilis, the bacillus acidocldarius etc. of the product aminopeptidase reported at present.The present invention is separated and obtains the bacillus cereus that aminopeptidase is produced in a strain from abyssal sediment, and conducts a preliminary study its aminopeptidase character, is intended to for the exploitation of aminopeptidase product provides new production bacterial classification and theoretical basis.
Summary of the invention
The object of this invention is to provide a strain bacillus cereus and producing the application in aminopeptidase.
A strain bacillus cereus of the present invention is separated from South Sea pelagic deposit matter sample, adopts casein plate primary dcreening operation and shake flask fermentation amino-peptidase activity to measure multiple sieve and obtains, Classification And Nomenclature be bacillus cereus ( bacillus cereussWJS 54).This bacterial strain is preserved in China Committee for Culture Collection of Microorganisms's common micro-organisms center on September 23rd, 2014, and preservation address is Yard 1, BeiChen xi Road, Chaoyang District, Beijing City institute of microbiology of the Chinese Academy of Sciences, and deposit number is CGMCC No. 9697.
Carry out pcr amplification and sequencing to the 16S rRNA gene that deposit number is CGMCC No. 9697 bacterial strain, recording 16S rDNA gene fragment length is 1353bp, and concrete sequence is shown in sequence table.In this gene order and Genbank, listed gene order is carried out analysis and is learnt, in this bacterial strain and database bacillus cereusthe 16S rDNA sequentiality of different strains has the similarity of 99%, with bacillus cereusstrain B4 similarity is the highest, and homology reaches 99%, identify this bacterial strain be bacillus cereus ( bacillus cereussWJS 54).
The present invention is that the optimal reactive temperature of aminopeptidase, optimal reaction pH, temperature and pH stability are produced in the fermentation of CGMCC No.9697 strain liquid, substrate specificity is studied to deposit number.
Compared with prior art, tool of the present invention has the following advantages and effect: the present invention's screening obtains the bacterial strain bacillus cereus SWJS 54 of the product aminopeptidase in a source, strain deep-sea, and its aminopeptidase reaction conditions is gentle, has stronger specificity.This bacterial strain may become the production bacterial classification of novel aminopeptidase resource or provide new aminopeptidase encoding gene, has important subsequent development and industrial application value.
Accompanying drawing explanation
Fig. 1 is the optimal reactive temperature curve that bacillus cereus SWJS 54 produces aminopeptidase.
Fig. 2 is that temperature produces the influence curve of aminopeptidase stability to bacillus cereus SWJS 54.
Fig. 3 is the optimal reaction pH curve that bacillus cereus SWJS 54 produces aminopeptidase.
Fig. 4 is that pH produces the influence curve of aminopeptidase stability to bacillus cereus SWJS 54.
Fig. 5 is the comparing substrate specificity figure that bacillus cereus SWJS 54 produces aminopeptidase.
Embodiment
Below in conjunction with example, enforcement of the present invention is described further, but enforcement of the present invention and comprising is not limited thereto, if it is noted that following promising special detailed description part, be all that those skilled in the art can refer to existing techniques in realizing.
enrichment and seed culture medium:peptone 5g, yeast powder 1g, artificial seawater 1L, pH 7.4-7.6.
casein medium:casein 10g, beef extract powder 3g, potassium primary phosphate 2g, agar powder 15g, artificial seawater 1L, pH about 7.2.
fermention medium: glycerine 3g, glucose 5g, yeast powder 10g, potassium primary phosphate 0.5g, magnesium sulfate 0.3g, ammonium sulfate 1g, calcium chloride 1g, sea salt 10g, pH7.2.
produce the CGMCC No. of aminopeptidase9697 separation screening
Enrichment culture: take 2g deep-sea ooze sample sample in 50mL sterile centrifugation tube, add 15mL sterile distilled water, fully mix, jolting 30min in shaking table, gets supernatant liquor 1mL (25 mL/250mL) in enrichment culture, 37 DEG C after leaving standstill, 120rpm, cultivates 48h.
Primary dcreening operation: get the nutrient solution 1mL after enrichment and add in 9mL sterile physiological water, be diluted to different gradient (10 by multiple proportions method -1-10 -7).Choose 10 -4, 10 -5, 10 -6, 10 -7extent of dilution, respectively draws 0.1mL, adds in the casein medium solidified, and coating evenly.Inversion is placed in 37 DEG C of incubators and cultivates 24-48h.
Separation and purification: select in above-mentioned casein plate the bacterium colony having obviously hydrolysis circle, line separation more than three times continuously on new casein plate, until be pure growth.Selecting the larger single bacterium colony of hydrolysis circle is stored on test tube slant, is 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, and activation 12h, is inoculated in fermention medium with 2% inoculum size, 37 DEG C, and 150rpm cultivates 48h.Fermented liquid is at 4 DEG C, and the centrifugal 10min of 10000rpm, gets supernatant liquor and be crude enzyme liquid.Adopt LNA method to measure aminopeptidase vigor, sift out the bacterial strain that liquid fermenting aminopeptidase output is high again.
Amino-peptidase activity measures: the Tris-HCl buffered soln of crude enzyme liquid pH 8.0 is diluted to suitable concentration, gets 80 μ L sample diluting liquids and add in 96 orifice plates, add 20 μ L L-Leu p-Nitroaniline (L-leu- pnA), after 40 DEG C of accurate response 10 min, add 100 μ L dehydrated alcohol termination reactions, measure the light absorption value under 405nm.With the light absorption value drawing standard curve of different concns p-Nitroaniline under 405nm.40 DEG C of per minute enzymolysis L-Leu-p-Nitroaniline enzyme amount produced needed for 1 μm of ol p-Nitroaniline are a Ge Meihuo unit.
produce the CGMCC No. of proteolytic enzyme9697 qualification
be inoculated in LB substratum by the CGMCC No. 9697 of activation, 37 DEG C, 150rpm cultivates 10h, gets the fresh bacterium liquid of 1.5mL 4 DEG C, the centrifugal 5min of 10000rpm, collects thalline in 2mL centrifuge tube, adopts DNA extraction kit to extract DNA.Universal primer is adopted to carry out PCR(forward primer after electrophoresis detection: 5 '-AGAGTTTGATCCTGGCTCAG-3 ', reverse primer: 5 '-GGTTACCTTGTTACGACTT-3 ').
Amplification total reaction system is (20 μ L): templet gene DNA 0.5 μ L; Upstream and downstream primer (20 μm of ol/l) each 1.0 μ L; Taq archaeal dna polymerase 0.2 μ L; 10 × buffer 2.0 μ L; 4 kinds of deoxynucleotide mixture dNTP (each 2.5 mmol/L) 1.6 μ L, 25 mmol/L MgCl 21.6 μ L, distilled water (ddH 2o) 12.1 μ L.Pcr amplification condition: 95 DEG C of 5 min; 95 DEG C of 30 s; 55 DEG C of 30 s; 72 DEG C of 1.5 min; 72 DEG C of 10 min; 10 DEG C, totally 30 circulations.The 16S rRNA gene fragment length completing mensuration after PCR primer purifying is 1353bp, with bacillus cereusstrain B4 similarity is the highest, and homology reaches 99%, with other bacillus cereusthe 16S rDNA sequentiality of different strains reaches 99%, and concrete sequence is shown in sequence table, identify CGMCC No. 9697 for bacillus cereus ( bacillus cereussWJS 54).
bacillus cereus CGMCC No.9697 produce the zymologic property research of aminopeptidase
Optimal reactive temperature: crude enzyme liquid is by obtaining the pure enzyme of electrophoresis after ultrafiltration and concentration, gel filtration chromatography, the vigor of aminopeptidase is measured respectively at 25 DEG C, 30 DEG C, 35 DEG C, 40 DEG C, 45 DEG C, 50 DEG C, 60 DEG C, 65 DEG C, 70 DEG C, 75 DEG C, with the highest vigor for 100%, represent with the per-cent that the vigor of aminopeptidase at other temperature is lived with the highest enzyme, the results are shown in Figure 1.Aminopeptidase vigor at 60 DEG C is the highest, has higher vigor at 50-65 DEG C.Temperature is lower than 25 DEG C or higher than 75 DEG C of basic debilities.
The research of thermostability: by aminopeptidase after 25-75 DEG C of scope inside holding 30min, measures residual aminopeptidase vigor at 60 DEG C, and enzyme work during not to be incubated is 100%, the results are shown in Figure 2.Temperature is lower than 55 DEG C, and after insulation 30min, vigor is substantially constant, the vigor of 60-65 DEG C of insulation 30min residues about 50%, and temperature is higher than 65 DEG C of then very fast inactivations.
Optimal pH: with the damping fluid dilution enzyme liquid of pH 6.0-10.0, measure the vigor of aminopeptidase respectively at 60 DEG C, the results are shown in Figure 3.The optimal reaction pH of this aminopeptidase is 9.5, within the scope of pH 7.5-9.5, have higher vigor, and pH exceeds this scope survey vigor to be reduced, greatly lower than 50%.
PH stability: aminopeptidase is placed (4 DEG C) different time at different pH buffered soln (pH 3.0-10.0), then at pH9.5, measure aminopeptidase vigor at 60 DEG C, with vigor when placing 0h for 100%, the results are shown in Figure 4.This aminopeptidase has good stability within the scope of pH 5.0-10.0, places the vigor that still to keep more than 80% after 48h, pH lower than 5.0 time less stable.
Substrate specificity: at identical conditions, measures different amino acid-p-Nitroaniline (Leu-respectively pnA, Phe- pnA, Ala- pnA, Arg- pnA, Glu- pnA, Lys- pnA, Pro- pnA and Met- pnA) as the vigor of aminopeptidase during substrate, with Leu- pnA is 100% as vigor during substrate.Aminopeptidase is to Leu-as shown in Figure 5 pnA and Met- pnA has stronger substrate specificity, and aminopeptidase vigor is higher, to the poor specificity of other substrates.
Sequence table
TGTTACAAACTCTCGTGGTGTGACGGGCGGTGTGTACAAGGCCCGGGAACGTATTCACCGCGGCATGCTGATCCGCGATTACTAGCGATTCCAGCTTCATGTAGGCGAGTTGCAGCCTACAATCCGAACTGAGAACGGTTTTATGAGATTAGCTCCACCTCGCGGTCTTGCAGCTCTTTGTACCGTCCATTGTAGCACGTGTGTAGCCCAGGTCATAAGGGGCATGATGATTTGACGTCATCCCCACCTTCCTCCGGTTTGTCACCGGCAGTCACCTTAGAGTGCCCAACTTAATGATGGCAACTAAGATCAAGGGTTGCGCTCGTTGCGGGACTTACCCAACATCTCACGACACGAGCTGACGACAACCATGCACCACCTGTCACTCTGCTCCCGAAGGAGAAGCCCTATCTCTAGGGTTGTCAGAGGATGTCAAGACCTGGTAAGGTTCTTCGCGTTGCTTCGAATTAAACCACATGCTCCACCGCTTGTGCGGGCCCCCGTCAATTCCTTTGAGTTTCAGCCTTGCGGCCGTACTCCCCAGGCGGAGTGCTTAATGCGTTAACTTCAGCACTAAAGGGCGGAAACCCTCTAACACTTAGCACTCATCGTTTACGGCGTGGACTACCAGGGTATCTAATCCTGTTTGCTCCCCACGCTTTCGCGCCTCAGTGTCAGTTACAGACCAGAAAGTCGCCTTCGCCACTGGTGTTCCTCCATATCTCTACGCATTTCACCGCTACACATGGAATTCCACTTTCCTCTTCTGCACTCAAGTCTCCCAGTTTCCAATGACCCTCCACGGTTGAGCCGTGGGCTTTCACATCAGACTTAAGAAACCACCTGCGCGCGCTTTACGCCCAATAATTCCGGATAACGCTTGCCACCTACGTATTACCGCGGCTGCTGGCACGTAGTTAGCCGTGGCTTTCTGGTTAGGTACCGTCAAGGTGCCAGCTTATTCAACTAGCACTTGTTCTTCCCTAACAACAGAGTTTTACGACCCGAAAGCCTTCATCACTCACGCGGCGTTGCTCCGTCAGACTTTCGTCCATTGCGGAAGATTCCCTACTGCTGCCTCCCGTAGGAGTCTGGGCCGTGTCTCAGTCCCAGTGTGGCCGATCACCCTCTCAGGTCGGCTACGCATCGTTGCCTTGGTGAGCCGTTACCTCACCAACTAGCTAATGCGACGCGGGTCCATCCATAAGTGACAGCCGAAGCCGCCTTTCAATTTCGAACCATGCGGTTCAAAATGTTATCCGGTATTAGCCCCGGTTTCCCGGAGTTATCCCAGTCTTATGGGCAGGTTACCCACGTGTTACTCACCCGTCCGCCGCTAACTTCATAAGAGCA

Claims (2)

1. a strain bacillus cereus ( bacillus cereussWJS 54), this bacterial strain is preserved in China Committee for Culture Collection of Microorganisms's common micro-organisms center on September 23rd, 2014, and deposit number is CGMCC No. 9697.
2. bacillus cereus according to claim 1 ( bacillus cereussWJS 54) produce the application in aminopeptidase at liquid fermenting.
CN201510100394.2A 2015-03-06 2015-03-06 Bacillus cereus and applications thereof in production of aminopeptidase Pending CN104651283A (en)

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Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN105602870A (en) * 2016-02-02 2016-05-25 华南理工大学 Aminopeptidase producing strain bacillus axarquiensis SWJSX8 and application thereof
CN107400666A (en) * 2017-09-11 2017-11-28 广东轻工职业技术学院 A kind of aminopeptidase and its encoding gene and application

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
CUI,T.B: "JX544747.1", 《GENBANK》 *
吴庆勋: "氨肽酶高产菌株的选育及发酵条件优化", 《中国优秀硕士学位论文全文数据库 工程科技Ⅰ辑 》 *
张金虎: "蜡状芽孢杆菌CZ 发酵生产氨肽酶的过程调控", 《中国优秀硕士学位论文全文数据库基础科学辑》 *

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN105602870A (en) * 2016-02-02 2016-05-25 华南理工大学 Aminopeptidase producing strain bacillus axarquiensis SWJSX8 and application thereof
CN105602870B (en) * 2016-02-02 2019-05-14 华南理工大学 A kind of production aminopeptidase bacterial strain Bacillus axarquiensis SWJSX8 and its application
CN107400666A (en) * 2017-09-11 2017-11-28 广东轻工职业技术学院 A kind of aminopeptidase and its encoding gene and application
CN107400666B (en) * 2017-09-11 2019-11-22 广东轻工职业技术学院 A kind of aminopeptidase and its encoding gene and application

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Application publication date: 20150527