WO2014193052A1 - Corynebacterium contenant un polynucléotide codant pour la psicose 3-épimérase et procédé de production de psicose l'utilisant - Google Patents

Corynebacterium contenant un polynucléotide codant pour la psicose 3-épimérase et procédé de production de psicose l'utilisant Download PDF

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WO2014193052A1
WO2014193052A1 PCT/KR2013/009641 KR2013009641W WO2014193052A1 WO 2014193052 A1 WO2014193052 A1 WO 2014193052A1 KR 2013009641 W KR2013009641 W KR 2013009641W WO 2014193052 A1 WO2014193052 A1 WO 2014193052A1
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fructose
microorganism
polynucleotide
microorganisms
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김선원
장희정
이현서
윤상활
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Gyeongsang National University GNU
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    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
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    • C12N1/00Microorganisms; 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
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    • C12N15/00Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09Recombinant DNA-technology
    • C12N15/11DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
    • C12N15/52Genes encoding for enzymes or proenzymes
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    • C12N15/00Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09Recombinant DNA-technology
    • C12N15/63Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
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    • C12N15/00Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09Recombinant DNA-technology
    • C12N15/63Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/74Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora
    • C12N15/77Vectors or expression systems specially adapted for prokaryotic hosts other than E. coli, e.g. Lactobacillus, Micromonospora for Corynebacterium; for Brevibacterium

Definitions

  • the present invention relates to a Corynebacterium comprising a polynucleotide encoding a Pycos 3-epimerase enzyme and a method of producing Pycos using the same.
  • D-psicose is an epimer of carbon number 3 of fructose (D-fructose), which is sweet like ordinary sugars, but is not metabolized in the human body. It is a functional sugar that can be used as a sugar substitute functional sweetener. In addition, it has the function of reducing the abdominal obesity by inhibiting the enzyme activity involved in lipid synthesis in the liver, and is a sugar currently being studied as a therapeutic agent for diabetes and atherosclerosis.
  • Ken Izumori et al Used galacitol, D-tagatose or D-talitol by utilizing microbial cell reactions. It has been shown that it is possible to produce psychocos from. However, these substrates also have the disadvantage that they are relatively rare in nature and have a high cost.
  • D-tagatose-3-epimerase of isolated microorganism Pseudomonas cichorii ST-24 is produced and purified from recombinant E. coli.
  • Korean Laid-Open Patent Publication No. 2006-125971 discloses a method for producing a psychos by a psychos epimerase.
  • a Corynebacterium microorganism comprising a polynucleotide encoding an enzyme having an activity catalyzing the conversion of fructose to a psychose, wherein the polynucleotide encodes the amino acid sequence of SEQ ID NO: 1.
  • microorganism of 1 above wherein the microorganism is the polynucleotide introduced into a Corynebacterium glutamicum strain.
  • microorganism according to any one of the preceding items, wherein the polynucleotide is introduced into the microorganism by itself or using a vector.
  • the microorganisms of the present invention are capable of mass production of psychoses from fructose with high efficiency while being safe.
  • Figure 1 shows the results of measuring the amount of psychos from the Corynebacterium glutamicum transformants incorporating cyclose 3-epimerase.
  • the gray bar is the result of 24 hours of psychos production
  • the dark gray bar is the result of 48 hours of psychos production.
  • Figure 2 is a result of measuring the amount of Pseudopsis while recovering and cultured four times the Corynebacterium glutamicum transformed cells incorporating Pycos 3-epimerase.
  • Panel A shows the results of the cycle production
  • panel B shows the concentration of the cells
  • Panel C shows the results of dividing the cycles produced by the cell concentration.
  • the present invention includes a polynucleotide encoding an enzyme having an activity of catalyzing the conversion of fructose to a psychocos, wherein the polynucleotide encodes the amino acid sequence of SEQ ID NO: 1, thereby safely and efficiently purifying the fructose from fructose.
  • the present invention relates to a Corynebacterium microorganism capable of mass production, and a method for producing a psychosis using the same.
  • Corynebacterium microorganism of the present invention comprises a polynucleotide encoding an enzyme having an activity that catalyzes the conversion of fructose to the psychos, the polynucleotide encodes the amino acid sequence of SEQ ID NO: 1.
  • Amino acid sequence of SEQ ID NO: 1 is a MKHGIYYSYW EHEWSAKFGP YIEKVAKLGF DIIEVAAHHI NEYSDAELAT IRKSAKDNGI ILTAGIGPSK TKNLSSEDAA VRAAGKAFFE RTLSNVAKLD IHTIGGALHS YWPIDYSQPV DKAGDYARGV EGINGIADFA NDLGINLCIE VLNRFENHVL NTAAEGVAFV KDVGKNNVKV MLDTFHMNIE EDSFGDAIRT AGPLLGHFHT GESNRRVPGK GRMPWHEIGL ALRDINYTGA VIMEPFVKTG GTIGSDIKVW RDLSGGADIA KMDEDARNAL AFSRFVLGG.
  • Corynebacterium microorganism of the present invention is not particularly limited as long as it contains the polynucleotide, for example, Corynebacterium glutamicum, preferably Corynebacterium glutamicum ATCC13032 (Corynebacterium glutamcium ATCC13032, taxid GenBank NID: NC_003450, ATCC13032) may be introduced into the polynucleotide.
  • Corynebacterium glutamicum preferably Corynebacterium glutamicum ATCC13032 (Corynebacterium glutamcium ATCC13032, taxid GenBank NID: NC_003450, ATCC13032) may be introduced into the polynucleotide.
  • Corynebacterium glutamicum ATCC13032 has been deposited with ATCC (American Type Culture Collection, Manassas, USA).
  • Corynebacterium glutamicum is a GRAS (Generally Recognized as Safe) strain, and in particular, Corynebacterium glutamicum ATCC13032 is an enzyme having an activity that catalyzes the conversion of fructose to psychos, when the polynucleotide comprises the polynucleotide. Can be produced with excellent efficiency, and the conversion rate of fructose to psychos is very excellent.
  • the enzyme may be an enzyme derived from Agrobacterium tumefaciens.
  • the polynucleotide encodes the amino acid sequence of SEQ ID NO: 1.
  • the polynucleotide may be introduced by any method known in the art.
  • the polynucleotide may be introduced into the polynucleotide itself or by a vector, for example.
  • vector refers to a nucleic acid molecule capable of delivering other nucleic acids to which it is linked. From the standpoint of nucleic acid sequences that mediate the introduction of specific genes, in the present invention, a vector is interpreted to be used interchangeably with a nucleic acid construct and a cassette.
  • Vectors include, for example, plasmids or viral derived vectors. Plasmid refers to a circular double stranded DNA ring to which additional DNA can be linked. Vectors used in the present invention include, for example, a plasmid expression vector, a plasmid shuttle vector, a virus expression vector (e.g., a replication defective retrovirus vector, a retrovirus vector, an adenovirus vector, a herpes simplex virus vector, a poxvirus vector, a lenti Viral vectors, adeno-associated viral vectors, etc.) and viral vectors capable of performing equivalent functions thereof are included, but are not limited to these.
  • virus expression vector e.g., a replication defective retrovirus vector, a retrovirus vector, an adenovirus vector, a herpes simplex virus vector, a poxvirus vector, a lenti Viral vectors, adeno-associated viral vectors, etc.
  • viral vectors capable of performing equivalent functions thereof are included, but
  • the polynucleotide may be operably linked with one or more elements consisting of a promoter and a transcription terminator.
  • the polynucleotide may be operably linked with a regulatory element.
  • the regulatory element may be selected from the group consisting of chemical inducible elements and temperature sensitive elements.
  • the chemical inducible element may be selected from the group consisting of lac operon and arabinose operon.
  • the microorganism of the genus Corynebacterium according to the present invention is a ptsF (EII Fru , fruA, NCgl1861, GI: 19553141, GI: 19553141, EC 2.7), which is a PTS transport system that transports into cells while converting endogenous di-fractose into di-fractose 1-phosphate. .1.69) may be missing or inactivated gene having a homology of 80% or more, preferably the same gene may be missing or inactivated.
  • Psychoses are generated from D-fructose, so depletion or inactivation of the gene can inhibit the phosphorylation of fructose, which can significantly improve the production efficiency of psychos.
  • the ptsF gene may be encoding the amino acid sequence of SEQ ID NO: 2.
  • Amino acid sequence of SEQ ID NO: 2 is MNSVNNSSLV RLDVDFGDST TDVINNLATV IFDAGRASSA DALAKDALDR EAKSGTGVPG QVAIPHCRSE AVSVPTLGFA RLSKGVDFSG PDGDANLVFL IAAPAGGGKE HLKILSKLAR SLVKKDFIKA LQEATTEQEI VDVVDAVLNP APKTTEPAAA PAAAAVAESG AASTSVTRIV AITACPTGIA HTYMAADSLT QNAEGRDDVE LVVETQGSSA VTPVDPKIIE AADAVIFATD VGVKDRERFA GKPVIESGVK RAINEPAKMI DEAIAASKNP NARKVSGSGV AASAETTGEK LGWGKRIQQA VMTGVSYMVP FVAAGGLLLA LGFAFGGYDM ANGWQAIATQ FSLTNLPGNT VDVDGVAMTF ERSGFLLYFG AVLFATGQAA MGFIVAALSG YTA
  • the microorganism of the genus Corynebacterium according to the present invention has a homology of 80% or more with mtlD (NCgl0108, GI: 19551360, EC 1.1.1.67) encoding mannitol 2-dehydrogenase
  • the gene may be deleted or inactivated, and preferably, the same gene may be deleted or inactivated.
  • fructose is converted to D-mannitol by mannitol 2-dihydrogenase
  • deletion or inactivation of the gene can suppress the reduction of fructose, thereby significantly improving the production efficiency of psychos. can do.
  • the mtlD gene may be encoding the amino acid sequence of SEQ ID NO: 3.
  • Amino acid sequence of SEQ ID NO: 3 is MNTPLQLNTE NLQEIASTSG VQIPAFNRAD VAPGIVHFGV GGFHRAHQAM YLNELMNEGK ALDWGIIGMG VMPSDVRMRD ALASQDHLYT LTTKAPDGTL DQKIIGSIID YVFAPEDPAR AVATLAQDSI RIVSLTVTEG GYNIDPATED FDHTNPRIVA DREALQAGDT STLQTFFGLI TAALISRKES GSTPFTIMSC DNIQGNGDLA KRFFLAFAHS VSSELGEWVE NNVAFPNSMV DRITPETTDG DRDDIKEIGY IDAWPVVSED FTQWVLEDAF TQGRPAYEEV GVQVVSDVEP YELMKLRLLN ASHQGLCYFG HLAGHHMVHD VMADTRFQDF LLAYMEREAT PTLKELPGVD LDAYRRQLIA RFGNAAVKDT VPRLCAESSD RIPKWLLPVV
  • the term “deleted” or “inactivated” means that the expression of the gene is reduced or not expressed.
  • the “inactivation” can be made by methods known in the art. For example, it may be inactivated by homologuous recombination. The homologous recombination may be mediated by, for example, transposon mutagenesis or P1 transduction.
  • the microorganism itself can obtain advantages such as enzyme immobilization as an enzyme carrier or a container containing the enzyme.
  • enzyme immobilization as an enzyme carrier or a container containing the enzyme.
  • the enzyme requires a secondary process of immobilization on the carrier in order to create an environment in which the activity can be maintained for a long time, but in the case of microorganisms, it is possible to reuse it by preventing the enzyme activity from rapidly degrading by sufficiently serving as a carrier. Do it.
  • the present invention shows a remarkably improved effect compared to the conventional method for producing a psychos using an enzyme or the like.
  • the present invention also provides a method for producing a psychos.
  • the microorganism is cultured in a medium containing fructose.
  • the culture conditions of the microorganisms are not particularly limited, and conditions used for culturing the transformant of the genus Corynebacterium known in the art may be used.
  • the culture temperature may be 26 to 38 °C.
  • the medium may be a nutrient medium containing yeast extract and nitrogen sources, such as 2YT medium, LB medium, TB medium.
  • carbon sources including glucose, glycerol and the like
  • Nitrogen sources including ammonia, urea, and the like
  • Essential metal ions such as sodium, potassium, calcium, magnesium, and manganese
  • It may be a life medium (defined medium) commonly used in the art including vitamins and the like.
  • the fructose concentration contained in the medium is not particularly limited, and may be included, for example, at a concentration of 1% (w / v) to 80% (w / v), preferably 1% (w / v) to 50%. (w / v).
  • the culture can be continuous, semi-continuous, or batch type culture.
  • the culturing may be carried out by further adding a substance that induces the expression of a polynucleotide encoding an enzyme having an activity of catalyzing the conversion of fructose to sicose.
  • the substance inducing the expression of the polynucleotide is not particularly limited and may be a substance commonly used in the art.
  • the cycos is recovered from the culture of the microorganism.
  • the method for recovering the psychocos is not particularly limited and may be based on methods known in the art, and examples thereof include centrifugation, filtration, crystallization, ion exchange chromatography, and the like.
  • the culture may be carried out by centrifugation to separate the culture from the microorganism, and by separating the psychose from the culture by the recovery method.
  • the method for producing a psychos of the present invention before the step of culturing the microorganisms in the medium containing fructose, the enzyme having an activity that catalyzes the conversion of fructose to psychos by culturing the microorganisms in a medium not containing fructose Expressing a polynucleotide encoding a nucleotide; And recovering the microorganisms from the culture of the microorganisms.
  • the medium not containing fructose may be the same category of medium as the medium containing fructose, except that the fructose is not included.
  • the method for recovering the microorganism from the culture of the microorganism is not particularly limited, and a method known in the art may be used, and examples thereof include centrifugation and filtration.
  • the microorganisms recovered by this method can be used at a desired concentration, for example in a concentrated state.
  • the transformant of Corynebacterium glutamicum can be inoculated and cultured in a medium containing the fructose at high concentration. Therefore, the microorganism used in the culturing in the medium containing fructose may be the recovered microorganism.
  • the recovered microorganism has a turbidity (measured at 600 nm absorbance, OD 600 ) of cells in a medium containing fructose in a range of 0.01 to 300, for example, 1 to 300, 10 to 300, 20 to 300, 5 to 300, or It can be inoculated at a concentration such that 40 to 300.
  • a cell containing a high concentration of the enzyme it is possible to efficiently convert fructose to a psychos in a medium containing high concentration of fructose in the medium.
  • the fructose when the recovered cells are used, the fructose may be included in the medium at a concentration of, for example, 1% (w / v) to 80% (w / v). Within this range, for example, 1% (w / v) to 35% (w / v), 10% (w / v) to 80% (w / v), 20% (w / v) to 80% (w / v), 30% (w / v) to 80% (w / v), 30% (w / v) to 80% (w / v) and the like.
  • the method for producing a psychosis of the present invention may further include recovering the microorganism from the culture of the microorganism, and culturing the separated microorganism in a medium containing fructose again.
  • the isolated microorganisms can be used for the production of 2 to 10 times, preferably 3 to 10 times, more preferably 4 to 10 times.
  • the isolated microorganism may be inoculated at a concentration such that, for example, OD 600 is 5 to 150 in the medium. Within this range, for example, 5 to 150, 10 to 150, 20 to 150, 10 to 100, 20 to 100, 20 to 80, 20 to 40, 40 to 100, and the like.
  • a microorganism containing a high concentration of the enzyme can inhibit the growth of microorganisms in a high concentration of fructose, it is possible to efficiently convert fructose to a psychos in a medium containing a high concentration of fructose in the medium.
  • the fructose is 1% (w / v) to 80% (w / v), 1% (w / v) to 35% (w / v) , 10% (w / v) to 80% (w / v), 20% (w / v) to 80% (w / v), or 30% (w / v) to 80% (w / v) or It may be included in the medium at a concentration of 30% (w / v) to 50% (w / v).
  • the pCES208 J. Microbiol. Biotechnol., 18: 639-647, 2008
  • E. coli-Corinebacterium shuttle vector was modified and used to construct a pSGT208 shuttle vector in which a terminator and a lac promoter were inserted.
  • the primers 1 and 2 were used to amplify the dpe gene from the Agrobacterium tumefaciens genome, cut it with restriction enzymes KpnI and BamHI, insert the same site of the pSGT208 shuttle vector, and then synthesize the Pycos 3-epimerase.
  • a pS208-dpe recombinant shuttle vector was constructed.
  • Recombinant vectors pS208-dpe, pS208cT-dpe and pSGT208 vector as a negative control thereof were introduced into the wild type Corynebacterium glutamicum ATCC 13032 and transformed into fructose. It was used for the production of the psychos. Transformation followed the method specified in the Handbook of Corynebacterium glutamicum (Lothar Eggeling et al., ISBN 0-8493-1821-1, 2005 by CRC press).
  • the primers used are listed in Table 1 below.
  • the Corynebacterium glutamicum transformant prepared in Example 1 was inoculated in 5 ml of LB medium (Difco) containing 20 ⁇ g / ml of kanamycin and subjected to 30 ° C. and 250 rpm conditions.
  • the main culture was incubated for 36 hours at 30 ° C. and 180 rpm at a volume of 50 ml in a slotted 300 ml Erlenmeyer flask to induce sufficient cell mass and sufficient expression of protein.
  • the obtained culture solution was centrifuged to remove the supernatant and the cells were recovered, and the cell concentration was resuspended at 65 OD 600 in the same medium as above containing 40% (w / v) fructose as a substrate.
  • the cells were cultured at 180 rpm.
  • the measurement result is shown in FIG.
  • the gray bar is the result of 24 hours of psychos production
  • the dark gray bar is the result of 48 hours of psychos production.
  • the cells were incubated for 24 hours in the presence of fructose, and the cells were separated from the culture. Then, the process of culturing the cells for 24 hours in the presence of fructose was repeated four times.
  • Panel A shows the results of the cycle production
  • panel B shows the concentration of the cells
  • Panel C shows the results of dividing the cycles produced by the cell concentration.
  • the cell concentration (Panel B of FIG. 2) tended to decrease as the number of reactions increased, which was caused by the centrifugation of the cell reaction solution to separate the reaction supernatant and the cell. This is because of the loss.

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Abstract

La présente invention concerne une bactérie Corynebacterium comprenant un polynucléotide codant pour la psicose 3-épimérase, ainsi qu'un procédé de production du psicose l'utilisant. Plus spécifiquement, l'invention concerne : une bactérie Corynebacterium comprenant un polynucléotide codant pour la psicose 3-épimérase ayant une activité de catalyse de la conversion du fructose en psicose, ledit polynucléotide permettant de produire à grande échelle, en toute sécurité et avec efficacité, du psicose à partir de fructose en codant la séquence d'acides aminés représentée par SEQ ID nº : 1 ; et un procédé de production du psicose l'utilisant.
PCT/KR2013/009641 2013-05-28 2013-10-28 Corynebacterium contenant un polynucléotide codant pour la psicose 3-épimérase et procédé de production de psicose l'utilisant Ceased WO2014193052A1 (fr)

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KR1020130060703A KR20140140215A (ko) 2013-05-28 2013-05-28 사이코스 3-에피머라제 효소를 코딩하는 폴리뉴클레오티드를 포함하는 코리네박테리움 및 이를 이용한 사이코스의 생산 방법

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Cited By (2)

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CN108559747A (zh) * 2016-08-31 2018-09-21 Cj第制糖株式会社 新型启动子及其应用
CN113801833A (zh) * 2021-09-08 2021-12-17 福州大学 一种产d-阿洛酮糖的重组菌单细胞工厂及其构建与应用

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CN107109443B (zh) 2014-11-06 2021-11-02 庆尚大学校产学协力团 阿洛酮糖的制备方法
KR101677368B1 (ko) 2015-04-02 2016-11-18 씨제이제일제당 (주) 신규 프로모터 및 이의 용도
EP3663397A4 (fr) * 2017-07-31 2021-04-28 CJ Cheiljedang Corporation Nouvelle psicose-6-phosphate phosphatase, composition pour la production de psicose comprenant ladite enzyme, procédé pour la production de psicose au moyen de ladite enzyme
KR101965509B1 (ko) * 2017-11-15 2019-04-03 씨제이제일제당 (주) 신규한 d-사이코스 3-에피머화 효소 및 이를 이용한 d-사이코스의 제조 방법
WO2019112368A1 (fr) * 2017-12-08 2019-06-13 씨제이제일제당 (주) Nouvelle psicose-6-phosphate phosphatase, composition de production de psicose comprenant celle-ci, et procédé de production de psicose faisant appel à celle-ci

Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US7332310B2 (en) * 1999-12-16 2008-02-19 Kyowa Hakko Kogyo Co., Ltd. Mutant of homoserine dehydrogenase from Corynebacterium and DNA encoding thereof
US20090081740A1 (en) * 2007-09-26 2009-03-26 Binder Thomas P Production of amino acids from sucrose in corynebacterium glutamicum
KR20110035805A (ko) * 2009-09-30 2011-04-06 씨제이제일제당 (주) 사이코스-에피머화 효소의 고정화 및 이를 이용한 사이코스의 제조방법
KR20110041910A (ko) * 2009-10-16 2011-04-22 경상대학교산학협력단 사이코스 3-에피머라제 효소를 코딩하는 폴리뉴클레오티드를 포함하는 대장균 및 그를 이용하여 사이코스를 생산하는 방법

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US7332310B2 (en) * 1999-12-16 2008-02-19 Kyowa Hakko Kogyo Co., Ltd. Mutant of homoserine dehydrogenase from Corynebacterium and DNA encoding thereof
US20090081740A1 (en) * 2007-09-26 2009-03-26 Binder Thomas P Production of amino acids from sucrose in corynebacterium glutamicum
KR20110035805A (ko) * 2009-09-30 2011-04-06 씨제이제일제당 (주) 사이코스-에피머화 효소의 고정화 및 이를 이용한 사이코스의 제조방법
KR20110041910A (ko) * 2009-10-16 2011-04-22 경상대학교산학협력단 사이코스 3-에피머라제 효소를 코딩하는 폴리뉴클레오티드를 포함하는 대장균 및 그를 이용하여 사이코스를 생산하는 방법

Non-Patent Citations (2)

* Cited by examiner, † Cited by third party
Title
DATABASE GENBANK 12 April 2012 (2012-04-12), accession no. 55915.1 *
MOON, MIN-WOO ET AL.: "Analyses of enzyme Il gene mutants for sugar transport and heterologous expression of fructokinase gene in Corynebacterium gluiamicum ATCC 13032", FEMS MICROBIOLOGY LETTERS, vol. 244, no. 2, 15 March 2005 (2005-03-15), pages 259 - 266 *

Cited By (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CN108559747A (zh) * 2016-08-31 2018-09-21 Cj第制糖株式会社 新型启动子及其应用
EP3508580A4 (fr) * 2016-08-31 2020-03-18 CJ Cheiljedang Corporation Nouveau promoteur et utilisation associée
CN108559747B (zh) * 2016-08-31 2021-08-31 Cj第一制糖株式会社 新型启动子及其应用
CN113801833A (zh) * 2021-09-08 2021-12-17 福州大学 一种产d-阿洛酮糖的重组菌单细胞工厂及其构建与应用
CN113801833B (zh) * 2021-09-08 2023-04-11 福州大学 一种产d-阿洛酮糖的重组菌单细胞工厂及其构建与应用

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