CN114277003B - Glutamine synthase mutant and application thereof - Google Patents
Glutamine synthase mutant and application thereof Download PDFInfo
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- CN114277003B CN114277003B CN202111530525.2A CN202111530525A CN114277003B CN 114277003 B CN114277003 B CN 114277003B CN 202111530525 A CN202111530525 A CN 202111530525A CN 114277003 B CN114277003 B CN 114277003B
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- Prior art keywords
- glu
- ala
- glutamine
- leu
- asp
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- 238000004519 manufacturing process Methods 0.000 claims abstract description 30
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 22
- 238000000855 fermentation Methods 0.000 claims abstract description 21
- 230000004151 fermentation Effects 0.000 claims abstract description 21
- 238000000034 method Methods 0.000 claims abstract description 15
- 244000005700 microbiome Species 0.000 claims abstract description 12
- 241000186226 Corynebacterium glutamicum Species 0.000 claims description 21
- 150000001413 amino acids Chemical group 0.000 claims description 8
- 239000012620 biological material Substances 0.000 claims description 6
- 241000588724 Escherichia coli Species 0.000 claims description 2
- 230000004913 activation Effects 0.000 claims description 2
- 239000002773 nucleotide Substances 0.000 claims description 2
- 125000003729 nucleotide group Chemical group 0.000 claims description 2
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- 108020004705 Codon Proteins 0.000 abstract description 10
- 239000002253 acid Substances 0.000 abstract description 7
- 230000009286 beneficial effect Effects 0.000 abstract description 5
- 238000002474 experimental method Methods 0.000 abstract description 4
- 238000005457 optimization Methods 0.000 abstract description 4
- 150000002308 glutamine derivatives Chemical class 0.000 abstract description 2
- 239000013612 plasmid Substances 0.000 description 19
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- MGBRZXXGQBAULP-DRZSPHRISA-N Phe-Glu-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CC1=CC=CC=C1 MGBRZXXGQBAULP-DRZSPHRISA-N 0.000 description 2
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Landscapes
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention relates to the technical field of recombinant microorganisms, in particular to a glutamine synthase mutant and application thereof. The invention strengthens the heterologous glutamine synthase by an error-prone PCR method and promotes the production of glutamine or glutamine derivatives. Specifically, the glutamine synthase mutants are obtained by codon optimization of glutamine synthase encoding genes of different sources and then constructing a mutant library by an error-prone PCR method. Fermentation experiments prove that the strain containing the glutamine synthase mutant provided by the invention is more beneficial to the production of glutamine; the yield of the glutamine can reach 32.7-33.5g/L, and the acid production is improved by 5.7-12.4%.
Description
Technical Field
The invention relates to the technical field of recombinant microorganisms, in particular to a glutamine synthase mutant and application thereof.
Background
Glutamine is a non-essential amino acid. The chemical name is 2-amino-4-carbamoyl butyric acid. Glutamine is an encoded amino acid in protein synthesis, can promote protein synthesis and inhibit protein decomposition, can be used for treating gastric and duodenal ulcers, and has an important role in the pharmaceutical industry.
At present, the most commonly used production method of glutamine is a fermentation method, and corynebacterium glutamicum (Corynebacterium glutamicum) is mainly used as a production bacterium for fermenting and producing the glutamine. Corynebacterium glutamicum is heterotrophic aerobic bacteria, is a gram-positive bacterium, and has the characteristics of high growth speed, non-pathogenicity and weak degradation capability on self metabolites. The fermentation method has the advantages of wide raw material sources, low production cost, controllable product quality, single product and the like. The glutamine synthase of corynebacterium glutamicum itself may undergo adenylation, resulting in a drastic decrease in enzyme activity, resulting in insufficient utilization of substrate glutamate. Therefore, finding a highly active glutaminase, which promotes the conversion of glutamate to glutamine, is of great importance.
Disclosure of Invention
The invention aims to strengthen heterologous glutamine synthase by an error-prone PCR method and promote the production of glutamine or glutamine derivatives.
The technical scheme provided by the invention is as follows: the coding gene of the glutamine synthase from lactobacillus acidophilus is subjected to codon optimization, then a mutant library is constructed by an error-prone PCR method, the screened plasmid is transformed into corynebacterium glutamicum MHZ-0513-3, the glutamine yield is compared by shake flask fermentation, the plasmid pXMJ19-L.a-glnA2 is selected, sequencing results show that the mutation sites of the amino acid sequence are F106L and Y305F respectively, meanwhile, the coding gene of the lactobacillus acidophilus from lactobacillus acidophilus reported in patent CN201711031742.0 is constructed into an expression plasmid pXMJ19-L.a-glnA0, and the expression plasmid is transformed into corynebacterium glutamicum MHZ-0513-3, so that the glutamine synthase mutant is more favorable for glutamine production by comparison.
The coding gene of the glutamine synthase from the corynebacterium crenatum is subjected to codon optimization, then a mutant library is constructed by an error-prone PCR method, the screened plasmid is transformed into corynebacterium glutamicum MHZ-0513-3, the glutamine yield is compared by shaking flask fermentation, the plasmid pXMJ19-C.c-glnA5 is selected, the sequencing result shows that the mutation site of the amino acid sequence is F211L, Q257T, F379S, meanwhile, the glutamine synthase from the corynebacterium crenatum reported by the patent CN201610574794.1 is imported into corynebacterium glutamicum MHZ-0513-3, and the glutamine synthase mutant is more favorable for glutamine production compared and found.
The coding gene of the glutamine synthase from bacillus subtilis is subjected to codon optimization, then a mutant library is constructed by an error-prone PCR method, and plasmids obtained through screening are introduced into the corynebacterium glutamicum MHZ-0513-3, so that the production of glutamine is facilitated compared with the fact that the glutamine synthase mutant containing the point mutations L299P and E378G is found.
Based on the above technical scheme, in a first aspect, the invention provides a glutamine synthase mutant, wherein the glutamine synthase mutant contains point mutations F106L and Y305F.
Alternatively, the glutamine synthase mutants provided by the present invention contain point mutations F211L, Q257T and F379S.
Alternatively, the glutamine synthase mutants provided by the present invention contain point mutations L299P and E378G.
The amino acid sequence of the glutamine synthase mutant provided by the invention is shown as SEQ ID No.2, SEQ ID No.4 or SEQ ID No. 6.
In a second aspect, the present invention provides a gene encoding a mutant glutamine synthase, wherein the nucleotide sequence of the encoding gene is shown as SEQ ID No.1, SEQ ID No.3 or SEQ ID No. 5.
In a third aspect, the present invention provides a biological material comprising the coding gene described above, said biological material being an expression cassette, a vector or a host cell.
In a fourth aspect, the present invention provides a recombinant microorganism expressing the above-described glutamine synthase mutant or comprising the above-described encoding gene.
The recombinant microorganism provided by the invention is corynebacterium glutamicum or escherichia coli.
The use of the above mutants or the above coding genes or the above biological materials or the above recombinant microorganisms for increasing glutamine production is also claimed, as will be appreciated by the person skilled in the art.
Specifically, the invention provides a method for improving the glutamine yield, which comprises the steps of activating the recombinant microorganism and inoculating the recombinant microorganism into a fermentation medium for fermentation production.
The invention has the beneficial effects that:
(1) The invention strengthens heterologous glutamine synthase by error-prone PCR to obtain a glutamine synthase mutant containing a plurality of point mutations.
(2) The strain containing the glutamine synthase mutant provided by the invention has the capability of high-yield glutamine and derivatives thereof.
(3) Corynebacterium glutamicum containing glutamine synthase point mutations F106L and Y305F has increased glutamine yield to 33.5g/L and increased acid production by 12.4%;
corynebacterium glutamicum containing glutamine synthase point mutations F211L, Q257T and F379S, the glutamine yield is improved to 33.2g/L, and the acid production is improved by 5.7%;
the corynebacterium glutamicum containing glutamine synthase point mutations L299P and E378G improves the glutamine yield to 32.7G/L and improves the acid production by 10.4 percent.
Detailed Description
The following examples are illustrative of the invention and are not intended to limit the scope of the invention.
The primers and sequences according to the present invention are shown in Table 1.
TABLE 1 primer sequences
The starting strain MHZ-0513-3 used in the examples was disclosed in CN106701649A, which was classified and named Corynebacterium glutamicum (Corynebacterium glutamicum), and was deposited in China general microbiological culture Collection center (China Committee) at 11 and 30 days of 2016: the collection number of the microbiological institute of China is CGMCC No.13405, and the collection number of the microbiological institute of China is China, national institute of sciences, no.1, no.3, north Chen West Lu, the Korean region of Beijing city.
The specific techniques or conditions are not identified in the examples and are described in the literature in this field or are carried out in accordance with the product specifications. The reagents or equipment used were conventional products available for purchase by regular vendors without the manufacturer's attention.
EXAMPLE 1 Lactobacillus acidophilus-derived Glutamine synthase mutant library
To ensure the normal expression of the Lactobacillus acidophilus-derived glutamine synthase in Corynebacterium glutamicum, the glutamine synthase was codon optimized, followed by gene synthesis at Jin Weizhi to obtain plasmid pUC-L.a-glnA, which was then used to construct a library of glutamine synthase mutants by error-prone PCR.
The error-prone PCR system adopted by the invention is as follows: mu.L of 10 Xerror-prone PCR buffer (100 mmol/L Tris-HCl pH 8.3, 500mmol/L KCl,1% Triton,20 mmol/LMgCl) was added per 50. Mu.L of system 2 mu.L of 10 XdNTP mixture (1 mmol/L dGTP,1mmol/L dATP,5mmol/L dCTP,5mmol/L dTTP); primer L.a-glnA-F/L.a-glnA-R50 pmol each, DNA template (pUC-L.a-glnA) 10ng, 5. Mu.L of 5mmol/L Mn 2+ 15U/. Mu.L Taq DNA polymerase 2.5. Mu.L, 5. Mu.L Mg 25mmol/L 2+ The sterilized ultrapure water was added to a total volume of 50. Mu.L.
The error-prone PCR procedure was 95℃for 5min;94℃1min,55℃1min,72℃1min 30s,30 cycles; and at 72℃for 10min. And (3) carrying out the next round of error-prone PCR by taking the first obtained PCR glue recovery product as a template, and repeating the 5 rounds of error-prone PCR to finally obtain the L.a-glnA mutant fragment.
Construction of L.a-glnA expression plasmid: the resulting L.a-glnA mutant fragment was purified by agarose gel recovery kit (Tiangen) and then digested with XmaI while pXMJ19 was digested with XmaI and dephosphorylated with FastAP, the fragment was ligated with vector using T4DNA ligase (TransGen Biotech), trans1T1 competent cells (TransGen Biotech) were transformed, the Canada resistant clone was picked up, xmaI restriction identified to give a positive clone of fragment insertion into pXMJ19, and further the correct inserted fragment was identified by sequencing with P1/P2 primers (Invitrogen). The resulting plasmid was designated pXMJ19-L.a-glnAX, X=1, 2,3 … n. The control plasmid was pXMJ19-L.a-glnA, i.e., plasmid insert L.a-glnA was codon optimized, but not mutated.
EXAMPLE 2 construction of the MHZ-0513-3/pXMJ19-L.a-glnA mutant Strain and Glutamine production Properties
The plasmid pXMJ19-L.a-glnAX was electrotransferred to MHZ-0513-3 to obtain strain MHZ-0513-3/pXMJ19-L.a-glnAX, followed by shaking fermentation to examine the glutamine yield. Through multiple experiments, a strain MHZ-0513-3/pXMJ19-L.a-glnA2 with higher glutamine yield is selected from the strain, the sequencing result of a glutamine synthase coding gene on an expression plasmid is shown as a sequence 1 (SEQ ID No. 1), the amino acid sequence is shown as a sequence 2 (SEQ ID No. 2), and 2 amino acids are subjected to point mutation in the sequencing, namely F106L and Y305F.
Meanwhile, the glutamine synthase from lactobacillus acidophilus reported in patent CN201711031742.0 is introduced into corynebacterium glutamicum MHZ-0513-3, and the mutant strain MHZ-0513-3/pXMJ19-L.a-glnA0 is obtained by the same construction method.
The strain MHZ-0513-3/pXMJ19-L.a-glnA, MHZ-0513-3/pXMJ19-L.a-glnA2 and MHZ-0513-3/pXMJ19-L.a-glnA0 were subjected to shaking fermentation, and the glutamine content was detected.
Method for verifying glutamine yield by fermentation: inoculating the strain frozen in-80 ℃ glycerol pipe into the slant culture medium for activation, culturing at 33 ℃ for 24 hours, growing a lawn, picking the lawn from the freshly activated slant, inoculating into the seed culture medium, culturing at 33 ℃ for 5 hours under 100rpm in a shaking way until the middle and later period of logarithmic growth, obtaining seed liquid, inoculating the seed liquid into a 500ml shaking bottle filled with 20ml fermentation culture medium with 10% inoculum size, and culturing at 33 ℃ for 48 hours under 150rpm in a shaking way. The results are shown in Table 3 (OD 562 The turbidity of the culture solution at 562nm and expressed the cell amount, and Gln (g/L) expressed the amount of accumulated L-glutamine.
The formula of the culture medium is as follows:
slant culture medium: 37g/L brain heart infusion, 1.8% agar, and sterilizing at 121deg.C under 0.1MPa for 20min;
the seed culture medium is as follows: glucose 50g/L, urea 5g/L, KH 2 PO 4 2.0g/L,MgSO 4 ·7H 2 O1.0 g/L, corn steep liquor 30g/L, pH 7.0;
the fermentation medium is as follows: glucose 90g/L, (NH 4) 2 SO 4 40g/L,KH 2 PO 4 2.0g/L,MgSO 4 ·7H 2 O1.0 g/L, corn steep liquor 10g/L, caCO 3 50g/L,pH 7.0。
Table 2 glutamine content assay of mutant strains
The shake flask fermentation result shows that MHZ-0513-3/pXMJ19-L.a-glnA and MHZ-0513-3/pXMJ19-L.a-glnA0 glutamine production are basically consistent, namely, codon optimized L.a-glnA and lactobacillus acidophilus-derived glutamine synthase reported in patent CN201711031742.0 are basically consistent in the glutamine production of the strain, but MHZ-0513-3/pXMJ19-L.a-glnA2 glutamine production is improved to 33.5g/L, acid production is improved by 12.4%, namely, the L.a-glnA2 point mutations F106L and Y305F are beneficial to glutamine production, and the glutamine synthase is superior to that reported in patent CN 201711031742.0.
EXAMPLE 3 construction of a library of Corynebacterium crenatum-derived glutamine synthase mutants
To ensure the normal expression of the glutamine synthase from Corynebacterium crenatum in Corynebacterium glutamicum, the glutamine synthase was codon optimized, followed by gene synthesis at Jin Weizhi to obtain plasmid pUC-C.c-glnA, and then an error-prone PCR method was used to construct a glutamine synthase mutant library. The primers used were C.c-glnA-F/C.c-glnA-R in the same manner as above.
Construction of C.c-glnA expression plasmid: the construction method was the same as above, and the resulting plasmid was designated pXMJ19-C.c-glnAX, X=1, 2,3 … n, and the control plasmid was pXMJ19-C.c-glnA, i.e., plasmid insert C.c-glnA was codon-optimized, but not mutated.
EXAMPLE 4 construction of the MHZ-0513-3/pXMJ19-C.c-glnA mutant Strain and Glutamine production Properties
The plasmid pXMJ19-C.c-glnAX was electrotransferred to MHZ-0513-3 to obtain strain MHZ-0513-3/pXMJ19-C.c-glnAX, followed by shaking fermentation to examine the glutamine yield. Through multiple experiments, a strain MHZ-0513-3/pXMJ19-C.c-glnA5 with higher glutamine yield is selected from the strain, the sequencing result of a glutamine synthase coding gene on an expression plasmid is shown as a sequence 3 (SEQ ID No. 3), the amino acid sequence is shown as a sequence 4 (SEQ ID No. 4), and the sequencing discovers point mutations F211L, Q257T and F379S. Meanwhile, the glutamine synthase from corynebacterium crenatum reported in patent CN201610574794.1 is introduced into corynebacterium glutamicum MHZ-0513-3, and the mutant strain MHZ-0513-3-C.c-glnA0 is obtained by the same construction method.
The strain MHZ-0513-3/pXMJ19-C.c-glnA, MHZ-0513-3/pXMJ19-C.c-glnA5 and MHZ-0513-3-C.c-glnA0 were subjected to shaking fermentation, and the glutamine content was detected.
TABLE 3 detection of glutamine content in mutant strains
The shake flask fermentation result shows that the MHZ-0513-3/pXMJ19-C.c-glnA and MHZ-0513-3/pXMJ19-C.c-glnA0 glutamine yield are basically consistent, namely, the codon optimized C.c-glnA and the corynebacterium crenatum-derived glutamine synthase reported in patent CN201610574794.1 are basically consistent, but the MHZ-0513-3/pXMJ19-C.c-glnA5 glutamine yield is improved to 33.2g/L, the acid production is improved by 5.7%, namely, the C.c-glnA5 midpoint mutation F211L, Q257T, F379S is beneficial to glutamine production, and is superior to the glutamine synthase reported in patent CN 201610574794.1.
EXAMPLE 5 construction of Bacillus subtilis-derived Glutamine synthase mutant library
To ensure the proper expression of the Bacillus subtilis-derived glutamine synthase in Corynebacterium glutamicum, the glutamine synthase was codon optimized, followed by gene synthesis at Jin Weizhi to obtain plasmid pUC-B.s-glnA, and then an error-prone PCR method was used to construct a glutamine synthase mutant library. The primers used were B.s-glnA-F/B.s-glnA-R in the same manner as above.
Construction of B.s-glnA expression plasmid: the resulting plasmid was designated pXMJ19-B.s-glnAX, X=1, 2,3 … n, as a control plasmid, i.e., B.s-glnA, which was codon-optimized but not mutated, as described above.
EXAMPLE 6 construction of the MHZ-0513-3/pXMJ19-B.s-glnA mutant Strain and Glutamine production Properties
The plasmid pXMJ19-B.s-glnAX was electrotransferred to MHZ-0513-3 to obtain strain MHZ-0513-3/pXMJ19-B.s-glnAX, followed by shaking fermentation to examine the glutamine yield. Through multiple experiments, a strain MHZ-0513-3/pXMJ19-B.s-glnA11 with higher glutamine yield is selected from the strain, the sequence of a glutamine synthase coding gene on an expression plasmid is shown as a sequence 5 (SEQ ID No. 5), the amino acid sequence is shown as a sequence 6 (SEQ ID No. 6), and the sequencing discovers point mutations L299P and E378G.
The strain MHZ-0513-3/pXMJ19-B.s-glnA and MHZ-0513-3-B.s-glnA11 were subjected to shaking fermentation, and the glutamine content was detected.
Table 4 glutamine content assay of mutant strains
The shake flask fermentation result shows that compared with MHZ-0513-3/pXMJ19-B.s-glnA11 and MHZ-0513-3/pXMJ19-B.s-glnA, the glutamine yield is improved to 32.7G/L, the acid production is improved by 10.4%, namely, the B.s-glnA11 midpoint mutation L299P, E378G is beneficial to the production of glutamine.
While the invention has been described in detail in the foregoing general description and with reference to specific embodiments thereof, it will be apparent to one skilled in the art that modifications and improvements can be made thereto. Accordingly, such modifications or improvements may be made without departing from the spirit of the invention and are intended to be within the scope of the invention as claimed.
Sequence listing
<110> gallery plum blossom biotechnology development Co., ltd
<120> glutamine synthase mutant and use thereof
<130> KHP211123997.5
<160> 14
<170> SIPOSequenceListing 1.0
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<211> 1338
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 1
atgtccaagc agtacaccgc agaagaaatc aagaccgaag tggaagataa gaacgtgcgc 60
ttcctgcgcc tgtgcttcac cgatatcaac ggcaccgaaa aggcagtgga agtgccaacc 120
tctcagctgg ataaggtgct gaccaacgat atccgcttcg atggctcctc catcgatggc 180
ttcgtgcgcc tggaagaatc cgatatggtg ctgtaccctg atttctccac ctggtccgtg 240
ctgccatggg gcgatgaaca cggcggcaag atcggccgcc tgatctgctc cgtgcacacc 300
accgatggca aggcactcgc cggcgatcca cgcaacaacc tgaagcgcgt gatcggcgaa 360
atggaaaacg ccggcttcga tgcattcgat atcggcttcg aaatggagtt ccacctgttc 420
aagctggatg ataacggcaa ctggaccacc gaagtgcctg atcacgcatc ctacttcgat 480
atgacctccg atgatgaagg cgcacgctgc cgccgcgaaa tcgtggaaac cctggaagat 540
atgggcttcg aagtggaagc agcacaccac gaagtgggcg atggtcagca agaaatcgat 600
ttccgcttcg ataacgcact ggcaaccgca gatcgctgtc agaccttcaa gatggtggca 660
cgcaccatcg cacgcaagca cggcctgttc gcaaccttca tggcaaagcc actggaaggc 720
caagccggca acggcatgca caacaacatg tccctgttca agggcaagaa gaacgtgttc 780
tacgataagg atggcgaatt tcacctgtcc gataccgcac tgtacttcct gaacggcatc 840
ctggaacacg cacgcgcaat caccgcaatc ggcaacccaa ccgtgaactc ctacaagcgc 900
ctgatccctg gcttcgaagc accatgctac atcgcatggg cagcaaagaa ccgctcccca 960
ctggtgcgca tcccatccgc cggcgaaatc aacacccgcc tggaaatgcg ctccgcagat 1020
ccaaccgcaa acccatacct gctcctggca gcatgcctga ccgccggcct gaatggtatc 1080
aaggagcaga agatgccaat gaagcctgtg gaagaaaaca tcttcgaaat gaccgaagag 1140
gaacgcgcaa agaagggcat caagccactg ccaaccaccc tgcacaacgc agtgaaggca 1200
ttcaaggaag atgatctgat caagtccgca ctgggcgatc acctgacccg ctccttcatc 1260
gaatccaagg aactggaatg gtccaagtac tctcagtccg tgtccgattg ggaacgtcag 1320
cgctacatga actggtaa 1338
<210> 2
<211> 445
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 2
Met Ser Lys Gln Tyr Thr Ala Glu Glu Ile Lys Thr Glu Val Glu Asp
1 5 10 15
Lys Asn Val Arg Phe Leu Arg Leu Cys Phe Thr Asp Ile Asn Gly Thr
20 25 30
Glu Lys Ala Val Glu Val Pro Thr Ser Gln Leu Asp Lys Val Leu Thr
35 40 45
Asn Asp Ile Arg Phe Asp Gly Ser Ser Ile Asp Gly Phe Val Arg Leu
50 55 60
Glu Glu Ser Asp Met Val Leu Tyr Pro Asp Phe Ser Thr Trp Ser Val
65 70 75 80
Leu Pro Trp Gly Asp Glu His Gly Gly Lys Ile Gly Arg Leu Ile Cys
85 90 95
Ser Val His Thr Thr Asp Gly Lys Ala Leu Ala Gly Asp Pro Arg Asn
100 105 110
Asn Leu Lys Arg Val Ile Gly Glu Met Glu Asn Ala Gly Phe Asp Ala
115 120 125
Phe Asp Ile Gly Phe Glu Met Glu Phe His Leu Phe Lys Leu Asp Asp
130 135 140
Asn Gly Asn Trp Thr Thr Glu Val Pro Asp His Ala Ser Tyr Phe Asp
145 150 155 160
Met Thr Ser Asp Asp Glu Gly Ala Arg Cys Arg Arg Glu Ile Val Glu
165 170 175
Thr Leu Glu Asp Met Gly Phe Glu Val Glu Ala Ala His His Glu Val
180 185 190
Gly Asp Gly Gln Gln Glu Ile Asp Phe Arg Phe Asp Asn Ala Leu Ala
195 200 205
Thr Ala Asp Arg Cys Gln Thr Phe Lys Met Val Ala Arg Thr Ile Ala
210 215 220
Arg Lys His Gly Leu Phe Ala Thr Phe Met Ala Lys Pro Leu Glu Gly
225 230 235 240
Gln Ala Gly Asn Gly Met His Asn Asn Met Ser Leu Phe Lys Gly Lys
245 250 255
Lys Asn Val Phe Tyr Asp Lys Asp Gly Glu Phe His Leu Ser Asp Thr
260 265 270
Ala Leu Tyr Phe Leu Asn Gly Ile Leu Glu His Ala Arg Ala Ile Thr
275 280 285
Ala Ile Gly Asn Pro Thr Val Asn Ser Tyr Lys Arg Leu Ile Pro Gly
290 295 300
Phe Glu Ala Pro Cys Tyr Ile Ala Trp Ala Ala Lys Asn Arg Ser Pro
305 310 315 320
Leu Val Arg Ile Pro Ser Ala Gly Glu Ile Asn Thr Arg Leu Glu Met
325 330 335
Arg Ser Ala Asp Pro Thr Ala Asn Pro Tyr Leu Leu Leu Ala Ala Cys
340 345 350
Leu Thr Ala Gly Leu Asn Gly Ile Lys Glu Gln Lys Met Pro Met Lys
355 360 365
Pro Val Glu Glu Asn Ile Phe Glu Met Thr Glu Glu Glu Arg Ala Lys
370 375 380
Lys Gly Ile Lys Pro Leu Pro Thr Thr Leu His Asn Ala Val Lys Ala
385 390 395 400
Phe Lys Glu Asp Asp Leu Ile Lys Ser Ala Leu Gly Asp His Leu Thr
405 410 415
Arg Ser Phe Ile Glu Ser Lys Glu Leu Glu Trp Ser Lys Tyr Ser Gln
420 425 430
Ser Val Ser Asp Trp Glu Arg Gln Arg Tyr Met Asn Trp
435 440 445
<210> 3
<211> 1434
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 3
gtggcattcg aaacccctga agaagtgacc aagttcatca aggatgaaaa cgtggaattc 60
atcgatgtgc gcttcaccga tctgcctggc accgaacagc acttctccat ccctgcagcc 120
gcattcgatg aagatgcaat cgaagaaggc ctggcattcg atggctcctc catccgcggc 180
ttcaccacca tcgatgaatc cgatatgaac ctgctgcctg atctgaccac cgcaaccctg 240
gatccattcc gcaaggcaaa gaccctgaac gtgaagttct tcgtgcacga tccattcacc 300
cgcgaagcat tctcccgcga tccacgcaac gtggcacgca aggcagaaca gtacctggca 360
tccaccggca tcgcagatac ctgcaacttc ggcgcagaag cagaattcta cctgttcgat 420
aaggtgcgct actccaccga aatcaacacc ggcttctacg aagtggatac caacgaaggc 480
tggtggaacc gcggccgcga aaccaacctg gatggcaccc caaacctggg ctccaagaac 540
cgcgtgaagg gcggctactt ccctgtggca ccatacgatc aagcagtgga tgtgcgcgat 600
gatatggtgc gcaacctgac ccaagccggc ctcaacctgg aacgcttcca ccacgaagtg 660
ggcggtggtc agcaagaaat caactaccgc ttcaacaccc tgctgcacgc agcagatgat 720
attcagacct tcaagtacat cgtgaagaac accgcacgtc agcacggtac gtccgcaacc 780
ttcatgccaa agccactggc cggcgataac ggctccggca tgcacgcaca tcagtccctg 840
tggaaggatg gcaagccact gttccacgat gaatccggct acgccggcct gtccgatatc 900
gcacgctact acatcggcgg catcctgcac cacgccggcg cagtgctggc attcaccaac 960
gcaaccctga actcctacca ccgcctggtg cctggcttcg aagcaccaat caacctggtg 1020
tactctcagc gcaaccgctc cgcagcagtg cgcatcccaa tcaccggctc caacccaaag 1080
gcaaagcgca tcgaattccg cgcacctgat ccatccggca acccatacct gggctcagca 1140
gcaatgatga tggccggcct ggatggcatc aagaaccgca tcgaaccaca cgcacctgtg 1200
gataaggatc tgtacgaact gccacctgaa gaagcagcat ccatcccaca agcaccaacc 1260
tccctggaag catccctgaa ggcactgcaa gaagataccg atttcctgac cgaatccgat 1320
gtgttcaccg aagatctgat cgaagcatac attcagtaca agtacgataa cgaaatctcc 1380
cctgtgcgcc tgcgcccaac cccacaagaa ttcgaactgt acttcgattg ctaa 1434
<210> 4
<211> 477
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 4
Val Ala Phe Glu Thr Pro Glu Glu Val Thr Lys Phe Ile Lys Asp Glu
1 5 10 15
Asn Val Glu Phe Ile Asp Val Arg Phe Thr Asp Leu Pro Gly Thr Glu
20 25 30
Gln His Phe Ser Ile Pro Ala Ala Ala Phe Asp Glu Asp Ala Ile Glu
35 40 45
Glu Gly Leu Ala Phe Asp Gly Ser Ser Ile Arg Gly Phe Thr Thr Ile
50 55 60
Asp Glu Ser Asp Met Asn Leu Leu Pro Asp Leu Thr Thr Ala Thr Leu
65 70 75 80
Asp Pro Phe Arg Lys Ala Lys Thr Leu Asn Val Lys Phe Phe Val His
85 90 95
Asp Pro Phe Thr Arg Glu Ala Phe Ser Arg Asp Pro Arg Asn Val Ala
100 105 110
Arg Lys Ala Glu Gln Tyr Leu Ala Ser Thr Gly Ile Ala Asp Thr Cys
115 120 125
Asn Phe Gly Ala Glu Ala Glu Phe Tyr Leu Phe Asp Lys Val Arg Tyr
130 135 140
Ser Thr Glu Ile Asn Thr Gly Phe Tyr Glu Val Asp Thr Asn Glu Gly
145 150 155 160
Trp Trp Asn Arg Gly Arg Glu Thr Asn Leu Asp Gly Thr Pro Asn Leu
165 170 175
Gly Ser Lys Asn Arg Val Lys Gly Gly Tyr Phe Pro Val Ala Pro Tyr
180 185 190
Asp Gln Ala Val Asp Val Arg Asp Asp Met Val Arg Asn Leu Thr Gln
195 200 205
Ala Gly Leu Asn Leu Glu Arg Phe His His Glu Val Gly Gly Gly Gln
210 215 220
Gln Glu Ile Asn Tyr Arg Phe Asn Thr Leu Leu His Ala Ala Asp Asp
225 230 235 240
Ile Gln Thr Phe Lys Tyr Ile Val Lys Asn Thr Ala Arg Gln His Gly
245 250 255
Thr Ser Ala Thr Phe Met Pro Lys Pro Leu Ala Gly Asp Asn Gly Ser
260 265 270
Gly Met His Ala His Gln Ser Leu Trp Lys Asp Gly Lys Pro Leu Phe
275 280 285
His Asp Glu Ser Gly Tyr Ala Gly Leu Ser Asp Ile Ala Arg Tyr Tyr
290 295 300
Ile Gly Gly Ile Leu His His Ala Gly Ala Val Leu Ala Phe Thr Asn
305 310 315 320
Ala Thr Leu Asn Ser Tyr His Arg Leu Val Pro Gly Phe Glu Ala Pro
325 330 335
Ile Asn Leu Val Tyr Ser Gln Arg Asn Arg Ser Ala Ala Val Arg Ile
340 345 350
Pro Ile Thr Gly Ser Asn Pro Lys Ala Lys Arg Ile Glu Phe Arg Ala
355 360 365
Pro Asp Pro Ser Gly Asn Pro Tyr Leu Gly Ser Ala Ala Met Met Met
370 375 380
Ala Gly Leu Asp Gly Ile Lys Asn Arg Ile Glu Pro His Ala Pro Val
385 390 395 400
Asp Lys Asp Leu Tyr Glu Leu Pro Pro Glu Glu Ala Ala Ser Ile Pro
405 410 415
Gln Ala Pro Thr Ser Leu Glu Ala Ser Leu Lys Ala Leu Gln Glu Asp
420 425 430
Thr Asp Phe Leu Thr Glu Ser Asp Val Phe Thr Glu Asp Leu Ile Glu
435 440 445
Ala Tyr Ile Gln Tyr Lys Tyr Asp Asn Glu Ile Ser Pro Val Arg Leu
450 455 460
Arg Pro Thr Pro Gln Glu Phe Glu Leu Tyr Phe Asp Cys
465 470 475
<210> 5
<211> 1335
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 5
atggcaaagt acacccgcga agatatcgaa aagctggtga aggaagaaaa cgtgaagtac 60
atccgcctgc agttcaccga tatcctgggc accatcaaga acgtggaaat ccctgtgtct 120
cagctgggca aggcactgga taacaaggtg atgttcgatg gctcctccat cgaaggcttc 180
gtgcgcatcg aagaatccga tatgtacctg taccctgatc tgaacacctt cgtgatcttc 240
ccatggaccg cagaaaaggg caaggtggca cgcttcatct gcgatatcta caaccctgat 300
ggcaccccat tcgaaggcga tccacgcaac aacctgaagc gcatcctgaa ggaaatggaa 360
gatctgggct tctccgattt caacctgggc cctgaacctg aattcttcct gttcaagctg 420
gatgaaaagg gcgaaccaac cctggaactg aacgataagg gcggctactt cgatctggca 480
ccaaccgatc tgggcgaaaa ctgccgccgc gatatcgtgc tggaactgga agaaatgggc 540
ttcgaaatcg aagcatccca ccacgaagtg gcacctggtc agcacgaaat cgatttcaag 600
tacgccggcg cagtgcgctc ctgcgatgat attcagacct tcaagctggt ggtgaagacc 660
atcgcacgca agcacggcct gcacgcaacc ttcatgccaa agccactgtt cggcgtgaac 720
ggctccggca tgcactgcaa cctgtccctg ttcaagaacg gcgtgaacgc attcttcgat 780
gaaaacgcag atctgcagct gtccgaaacc gcaaagcact tcatcgccgg catcgtgaag 840
cacgcaactt ccttcaccgc agtgaccaac ccaaccgtga actcctacaa gcgcccggtg 900
cctggctacg aagcaccatg ctacgtggca tggtccgcac agaaccgctc cccactgatc 960
cgcatccctg catcccgcgg catctccacc cgcgtggaag tgcgctccgt ggatcctgca 1020
gcaaacccat acctggcact gtccgtgctg ctggcagccg gcctggatgg catcaagaac 1080
aagctggaag cacctgcacc aatcgatcgc aacatctacg tgatgtccaa gggagaacgc 1140
atggaaaacg gcatcgtgga tctgcctgca accctggcag aagcactgga agaattcaag 1200
tccaacgaag tgatggtgaa ggcactgggc gaacacctgt tcgaacactt catcgaagca 1260
aaggaaatcg aatgggatat gttccgcacc caagtgcacc catgggaacg cgaacagtac 1320
atgtctcagt actaa 1335
<210> 6
<211> 444
<212> PRT
<213> Artificial sequence (Artificial Sequence)
<400> 6
Met Ala Lys Tyr Thr Arg Glu Asp Ile Glu Lys Leu Val Lys Glu Glu
1 5 10 15
Asn Val Lys Tyr Ile Arg Leu Gln Phe Thr Asp Ile Leu Gly Thr Ile
20 25 30
Lys Asn Val Glu Ile Pro Val Ser Gln Leu Gly Lys Ala Leu Asp Asn
35 40 45
Lys Val Met Phe Asp Gly Ser Ser Ile Glu Gly Phe Val Arg Ile Glu
50 55 60
Glu Ser Asp Met Tyr Leu Tyr Pro Asp Leu Asn Thr Phe Val Ile Phe
65 70 75 80
Pro Trp Thr Ala Glu Lys Gly Lys Val Ala Arg Phe Ile Cys Asp Ile
85 90 95
Tyr Asn Pro Asp Gly Thr Pro Phe Glu Gly Asp Pro Arg Asn Asn Leu
100 105 110
Lys Arg Ile Leu Lys Glu Met Glu Asp Leu Gly Phe Ser Asp Phe Asn
115 120 125
Leu Gly Pro Glu Pro Glu Phe Phe Leu Phe Lys Leu Asp Glu Lys Gly
130 135 140
Glu Pro Thr Leu Glu Leu Asn Asp Lys Gly Gly Tyr Phe Asp Leu Ala
145 150 155 160
Pro Thr Asp Leu Gly Glu Asn Cys Arg Arg Asp Ile Val Leu Glu Leu
165 170 175
Glu Glu Met Gly Phe Glu Ile Glu Ala Ser His His Glu Val Ala Pro
180 185 190
Gly Gln His Glu Ile Asp Phe Lys Tyr Ala Gly Ala Val Arg Ser Cys
195 200 205
Asp Asp Ile Gln Thr Phe Lys Leu Val Val Lys Thr Ile Ala Arg Lys
210 215 220
His Gly Leu His Ala Thr Phe Met Pro Lys Pro Leu Phe Gly Val Asn
225 230 235 240
Gly Ser Gly Met His Cys Asn Leu Ser Leu Phe Lys Asn Gly Val Asn
245 250 255
Ala Phe Phe Asp Glu Asn Ala Asp Leu Gln Leu Ser Glu Thr Ala Lys
260 265 270
His Phe Ile Ala Gly Ile Val Lys His Ala Thr Ser Phe Thr Ala Val
275 280 285
Thr Asn Pro Thr Val Asn Ser Tyr Lys Arg Pro Val Pro Gly Tyr Glu
290 295 300
Ala Pro Cys Tyr Val Ala Trp Ser Ala Gln Asn Arg Ser Pro Leu Ile
305 310 315 320
Arg Ile Pro Ala Ser Arg Gly Ile Ser Thr Arg Val Glu Val Arg Ser
325 330 335
Val Asp Pro Ala Ala Asn Pro Tyr Leu Ala Leu Ser Val Leu Leu Ala
340 345 350
Ala Gly Leu Asp Gly Ile Lys Asn Lys Leu Glu Ala Pro Ala Pro Ile
355 360 365
Asp Arg Asn Ile Tyr Val Met Ser Lys Gly Glu Arg Met Glu Asn Gly
370 375 380
Ile Val Asp Leu Pro Ala Thr Leu Ala Glu Ala Leu Glu Glu Phe Lys
385 390 395 400
Ser Asn Glu Val Met Val Lys Ala Leu Gly Glu His Leu Phe Glu His
405 410 415
Phe Ile Glu Ala Lys Glu Ile Glu Trp Asp Met Phe Arg Thr Gln Val
420 425 430
His Pro Trp Glu Arg Glu Gln Tyr Met Ser Gln Tyr
435 440
<210> 7
<211> 32
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 7
tccccccggg atgtccaagc agtacaccgc ag 32
<210> 8
<211> 30
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 8
tccccccggg ttaccagttc atgtagcgct 30
<210> 9
<211> 33
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 9
tccccccggg gtggcattcg aaacccctga aga 33
<210> 10
<211> 31
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 10
tccccccggg ttagcaatcg aagtacagtt c 31
<210> 11
<211> 33
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 11
tccccccggg atggcaaagt acacccgcga aga 33
<210> 12
<211> 32
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 12
tccccccggg ttagtactga gacatgtact gt 32
<210> 13
<211> 21
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 13
tgtgagcgga taacaatttc a 21
<210> 14
<211> 26
<212> DNA
<213> Artificial sequence (Artificial Sequence)
<400> 14
ttctgattta atctgtatca ggctga 26
Claims (7)
1. The glutamine synthase mutant is characterized in that the amino acid sequence of the glutamine synthase mutant is shown as SEQ ID No.2, SEQ ID No.4 or SEQ ID No. 6.
2. The coding gene of the glutamine synthase mutant as defined in claim 1, wherein the nucleotide sequence of the coding gene is shown as SEQ ID No.1, SEQ ID No.3 or SEQ ID No. 5.
3. A biological material comprising the coding gene of claim 2, wherein the biological material is an expression cassette, a vector or a host cell.
4. A recombinant microorganism expressing the glutamine synthase mutant of claim 1 or comprising the encoding gene of claim 2.
5. The recombinant microorganism according to claim 4, wherein the recombinant microorganism is Corynebacterium glutamicum or Escherichia coli.
6. Use of a mutant according to claim 1 or a coding gene according to claim 2 or a biomaterial according to claim 3 or a recombinant microorganism according to any one of claims 4 to 5 for increasing the production of glutamine or a derivative thereof.
7. A method for increasing glutamine production, characterized in that the recombinant microorganism according to any one of claims 4 to 5 is inoculated into a fermentation medium after activation, and fermentation production is performed.
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Citations (3)
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CN107603938A (en) * | 2017-10-30 | 2018-01-19 | 天津科技大学 | It is overexpressed the genetic engineering bacterium and its construction method of heterologous glutamyl amine synzyme |
CN112143751A (en) * | 2020-09-22 | 2020-12-29 | 廊坊梅花生物技术开发有限公司 | Bacillus subtilis engineering bacterium for high nucleoside yield, and construction method and application thereof |
CN113201524A (en) * | 2021-05-08 | 2021-08-03 | 廊坊梅花生物技术开发有限公司 | Inositol-3-phosphate synthase mutant and application thereof in constructing corynebacterium glutamicum capable of producing glutamine at high yield |
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CN107603938A (en) * | 2017-10-30 | 2018-01-19 | 天津科技大学 | It is overexpressed the genetic engineering bacterium and its construction method of heterologous glutamyl amine synzyme |
CN112143751A (en) * | 2020-09-22 | 2020-12-29 | 廊坊梅花生物技术开发有限公司 | Bacillus subtilis engineering bacterium for high nucleoside yield, and construction method and application thereof |
CN113201524A (en) * | 2021-05-08 | 2021-08-03 | 廊坊梅花生物技术开发有限公司 | Inositol-3-phosphate synthase mutant and application thereof in constructing corynebacterium glutamicum capable of producing glutamine at high yield |
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