WO2016064146A1 - 타가토스 제조용 조성물 및 과당으로부터 타가토스를 제조하는 방법 - Google Patents

타가토스 제조용 조성물 및 과당으로부터 타가토스를 제조하는 방법 Download PDF

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WO2016064146A1
WO2016064146A1 PCT/KR2015/011007 KR2015011007W WO2016064146A1 WO 2016064146 A1 WO2016064146 A1 WO 2016064146A1 KR 2015011007 W KR2015011007 W KR 2015011007W WO 2016064146 A1 WO2016064146 A1 WO 2016064146A1
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seq
amino acid
kda
fructose
protein
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French (fr)
Korean (ko)
Inventor
이영미
김양희
양성재
박일향
김성보
조현국
박승원
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CJ CheilJedang Corp
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CJ CheilJedang Corp
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Priority to UAA201703549A priority Critical patent/UA119791C2/uk
Priority to CN201580057200.3A priority patent/CN107109394B/zh
Priority to RU2017113926A priority patent/RU2701669C2/ru
Priority to ES15852026T priority patent/ES2721309T3/es
Priority to EP15852026.2A priority patent/EP3211078B1/en
Priority to JP2017521088A priority patent/JP6518761B2/ja
Priority to US15/521,243 priority patent/US10544438B2/en
Publication of WO2016064146A1 publication Critical patent/WO2016064146A1/ko
Anticipated expiration legal-status Critical
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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
    • 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
    • C12N1/00—Microorganisms; 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
    • 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
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • 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
    • C12N9/90—Isomerases (5.)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P19/00—Preparation of compounds containing saccharide radicals
    • C12P19/02—Monosaccharides
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P19/00—Preparation of compounds containing saccharide radicals
    • C12P19/24—Preparation of compounds containing saccharide radicals produced by the action of an isomerase, e.g. fructose
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y501/00—Racemaces and epimerases (5.1)
    • C12Y501/03—Racemaces and epimerases (5.1) acting on carbohydrates and derivatives (5.1.3)
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2250/00—Food ingredients
    • A23V2250/60—Sugars, e.g. mono-, di-, tri-, tetra-saccharides
    • A23V2250/634—Tagatose

Definitions

  • the present invention provides a composition for preparing tagatose and a method for preparing tagatose from fructose, and more specifically, a gene encoding thermophilic fructose 4-epimerase derived from a pyrobacterial microorganism and tagatose from fructose using the enzyme. It relates to a method of manufacturing.
  • Tagatose is an epimer of fructose (D-fructose). Tagatose has a natural sweetness that is almost indistinguishable from sugar, and its physical properties are similar to sugar. Tagatose is a natural sweetener present in foods such as milk, cheese, cacao, and sweet fruits such as apples and tangerines.It is 1.5 kcal / g, 1/3 of sugar, GI (Glycemic index) Index) is 3, which is about 5% of sugar, but has a variety of health functions with a sweet taste similar to that of sugar, and can be used as an alternative sweetener that can satisfy both health and taste simultaneously when applying multiple products.
  • D-fructose D-fructose
  • Tagatose has a natural sweetness that is almost indistinguishable from sugar, and its physical properties are similar to sugar.
  • Tagatose is a natural sweetener present in foods such as milk, cheese, cacao, and sweet fruits such as apples and tangerines.It
  • the representative basic raw material for obtaining galactose is lactose, and there is instability of the price of lactose or lactose-containing products according to the production, demand, and supply of crude oil and lactose in the international market, thus producing stable tagatose. There is a limit to the supply and demand of raw materials.
  • tagatose was produced using galactose decomposed from various biological resources such as whey permeate, whey permeate, and lactic acid, a plant-based biomass, as a food ingredient.
  • an object of the present invention is to provide a composition for producing tagatose and a method for producing tagatose for producing tagatose from common sugar suitable for industrial application compared to the conventional method for producing tagatose from galactose. .
  • the present invention is a protein of which the function is not known in the prior art, having a D-fructose 4-epimerase activity, a novel enzyme protein capable of producing tagatose with high yield from fructose, genes encoding the same and the same
  • An object of the present invention is to provide a composition for producing tagatose and a method for producing tagatose from fructose.
  • a protein comprising the amino acid sequence of any one of SEQ ID NO: 1 to SEQ ID NO: 7 of the present invention or a strain for expressing the protein, provides a composition for producing tagatose from fructose. .
  • a method of preparing tagatose from fructose comprising reacting the composition of an embodiment of the present invention with fructose.
  • the present invention develops a novel D-fructose 4-epimerase enzyme, an enzyme having the activity of producing tagatose by epimerizing the fourth carbon position of fructose, thereby reducing production costs by using fructose, a common raw material. This enables the production of tagatose with high yield.
  • the present invention can provide an economical and high yield tagatose manufacturing method by reducing the manufacturing cost using fructose as a general raw material rather than lactose having a large price fluctuation.
  • fructose can be industrially manufactured from glucose or sugar
  • the raw materials of the process according to the present invention are used in the form of whole or part of fructose for cheaper production in addition to fructose. It can be extended to include. That is, the present invention includes the production of tagatose through enzymatic conversion from starch, raw sugar or sugar.
  • the present invention can produce tagatose using fructose to efficiently mass-produce tagatose, which has been spotlighted as an important food material today.
  • 1A-1G are cleavage maps of recombinant vectors for expressing seven D-fructose 4-epimerases derived from each thermophilic microorganism.
  • FIGS. 2A to 2G are HPLC graphs showing the production of seven tagatose derived from each of the thermophilic microorganisms by D-fructose 4-epimerase reaction using fructose as a substrate.
  • 3A to 3G are graphs showing the temperature-dependent activity of the seven D-fructose 4-epimerases from each of the thermophilic microorganisms.
  • 4A to 4G are graphs showing the activity according to the pH change for each of the 7 D-fructose 4-epimerases derived from each thermophilic microorganism.
  • Figures 5a to 5g is a graph comparing the activity of the activity of the seven D-fructose 4-epimerase derived from each thermophilic microorganism according to the type of metal ion.
  • 6A-6G show the amino acid sequence (SEQ ID NO: 1 to SEQ ID NO: 7) of proteins derived from each of the seven thermophilic microorganisms.
  • n-th carbon position means a carbon position determined according to the carbon numbering rule defined by IUPAC, which may be expressed as Cn.
  • n is an integer of 1 or more.
  • epimerized at carbon position 4" may be referred to as "C4-epimerized”.
  • composition for producing tagatose for producing tagatose from fructose comprising a protein consisting of the amino acid sequence of any one of SEQ ID NO: 1 to SEQ ID NO: 7 or a strain expressing the protein. do.
  • aldohexose is an aldose consisting of six carbon atoms, which means that it has an aldehyde group at one end.
  • Non-limiting examples include glucose, galactose, allose, and gulose. , Altrose, mannose, talos and idose.
  • ketohexose herein means a monosaccharide having six carbon atoms and having a ketone group, and non-limiting examples include fructose, tagatose, psicose, and sorbose. And specifically, may be fructose.
  • the fructose and the tagatose refer to D-type fructose or D-type tagatose unless otherwise specified herein.
  • the amino acid sequence of any one of SEQ ID NO: 1 to SEQ ID NO: 7 may be an enzyme having the activity of producing tagatose by epimerizing the fourth carbon position of fructose.
  • thermophilic microorganism also sseomeoseu (Rhodothermus) genus Thermococcus frozen error in bakteo (Thermoanaerobacter), A write motto is (Thermotoga), A mousse (Dictyoglomus) a dithiol Ogle.
  • Enzyme produced by thermophilic microorganism has the same function as enzyme produced by mesophilic microorganism (mesophile) and can stably react under extreme reaction conditions (high temperature, etc.). Because of its many advantages, such as increased solubility of substances with low solubility and increased reaction rate, it is possible to overcome the industrial shortcomings using mesophilic enzymes.
  • the first polynucleotide expressing an enzyme capable of converting fructose to tagatose among the genes of each microorganism was first identified, thereby effectively overexpressing the protein (
  • a polynucleotide sequence optimized for overexpression) is synthesized and inserted into and expressed in a recombinant vector to provide an enzyme having an activity of converting fructose into tagatose.
  • amino acid sequence of any one of SEQ ID NO: 1 to SEQ ID NO: 7 may be transformed with a recombinant vector containing a gene encoding each of the protein consisting of the sequence.
  • Escherichia . coli As the strain for transformation, Escherichia . coli , Corynebacterum glutamicum , Aspergillus oryzae , or Bacillus subtilis, and the like.
  • the strain transformed into E. coli is, for example, Escherichia coli BL21 (DE3) -pET21a-RM (Accession No .: KCCM11576P), Escherichia coli BL21 (DE3) -pET21a-TAM (Accession No .: KCCM11577P), Escherichia coli BL21 (DE3) -pET21a-TAS (Accession No .: KCCM11578P), Escherichia coli BL21 (DE3) -pET21a-TAX (Accession No .: KCCM11579P), Escherichia coli BL21 (DE3) -pET21a-TP (Accession No .: KCCM115
  • the protein consisting of the amino acid sequence of SEQ ID NO: 1 of one embodiment of the present invention is Rhodothermus ( Rhodothermus) marinus ).
  • the protein may have a molecular weight of 55 kDa to 60 kDa, an optimum activity temperature of 50 ° C. to 90 ° C., and an optimum activity pH of 6.0 to 9.0.
  • the optimum active temperature may be 60 °C to 80 °C
  • the optimum active pH may be 7.0 to 9.0.
  • the protein consisting of the amino acid sequence of SEQ ID NO: 2 of one embodiment of the present invention is Thermotoga Petrophy ( Thermotoga petrophila ) .
  • the protein may have a molecular weight of 55 kDa to 58 kDa, an optimum activity temperature of 50 ° C to 90 ° C, and an optimum activity pH of 7.0 to 9.0.
  • the optimum active temperature may be 70 °C to 90 °C.
  • the protein consisting of the amino acid sequence of SEQ ID NO: 3 of one embodiment of the present invention may be an enzyme derived from Thermomotoga lettingae .
  • the protein may have a molecular weight of 55 kDa to 58 kDa, an optimum activity temperature of 50 ° C to 90 ° C, and an optimum activity pH of 7.0 to 9.0.
  • the optimum active temperature may be 60 °C to 80 °C.
  • the protein consisting of the amino acid sequence of SEQ ID NO: 4 of one embodiment of the present invention is Thermoanaerobacter ( Thermoanaerobacter may be an enzyme derived from mathranii ) .
  • the protein may have a molecular weight of 55 kDa to 58 kDa, an optimum activity temperature of 50 ° C to 90 ° C, and an optimum activity pH of 7.0 to 10.0.
  • the optimum active temperature may be 70 °C to 90 °C
  • the optimum active pH may be 8.0 to 10.0.
  • a protein consisting of an amino-acid sequence of SEQ ID NO: 5 of the present invention to Dick mousse pop bonus thio article (Dictyoglomus turgidum ) .
  • the protein may have a molecular weight of 55 kDa to 58 kDa, an optimum activity temperature of 50 ° C to 90 ° C, and an optimum activity pH of 7.0 to 9.0.
  • the optimum active temperature may be 60 °C to 80 °C.
  • the protein consisting of the amino acid sequence of SEQ ID NO: 6 of one embodiment of the present invention is Thermoaneromakterium xylorytum ( Thermoanaerobacterium xylanolyticum ).
  • the protein may have a molecular weight of 53 kDa to 58 kDa, an optimum activity temperature of 50 ° C to 90 ° C, and an optimum activity pH of 6.0 to 9.0.
  • the optimum active temperature may be 60 °C to 80 °C
  • the optimum pH may be 6.0 to 8.0.
  • the protein consisting of the amino acid sequence of SEQ ID NO: 7 of one embodiment of the present invention is Thermoanaerobacter ( Thermoanaerobacter siderophilus ).
  • the protein may have a molecular weight of 55 kDa to 58 kDa, an optimum activity temperature of 50 ° C. to 80 ° C., and an optimum activity pH of 7.0 to 10.0.
  • the optimum active temperature may be 60 °C to 80 °C
  • the optimum pH may be 8.0 to 10.0.
  • it may be a method for producing tagatose from fructose, comprising the step of reacting the composition of any one of the embodiments of the present invention with fructose.
  • reaction may be made at 50 °C to 80 °C.
  • reaction may be performed at pH 6.0 to 9.0.
  • reaction may further comprise magnesium ions, zinc ions, nickel ions, cobalt ions, iron ions, manganese ions, or mixtures thereof.
  • fructose serving as a substrate may be in a concentration of 5% (w / v) to 60% (w / v).
  • fructose can be obtained from sugar or glucose.
  • the step of reacting the composition of any one of the embodiments of the present invention with fructose the step of hydrolyzing sugar or isomerizing glucose to further obtain the fructose.
  • the enzyme used for the hydrolysis is ⁇ -D-fructosidase including ⁇ -fructofuranosidase, invertase, saccharase, and the like; It may be one or more selected from the group consisting of sucrase, ⁇ -glucosidase and ⁇ -D-glucohydrolase, but is not limited thereto.
  • the glucose isomerization enzyme may be, but is not limited to, glucose isomerase or phosphoglucois isomerase.
  • the polynucleotide encoding the amino acid sequence of SEQ ID NO: 1 to SEQ ID NO: 7 (Figs. 6A to 6G) derived from seven thermophilic microorganisms using pET21a (the expression vectors NdeI and XhoI)
  • the recombinant vector pET21a-RM, pET21a-TAM, pET21a-TAS, pET21a-TAX, pET21a-TP, pET21a-TL, pET21a-DT were prepared by insertion into the same restriction enzyme site of Novagen) (FIGS. 1A-1G).
  • the recombinant vector was transformed into E. coli BL21 (DE3) (invitrogen) by heat shock (Sambrook and Russell: Molecular Cloning.) To prepare a recombinant strain.
  • Example 1 A total of 7 cells recovered in Example 1 was turbid in a lysis buffer (50mM K-phosphate) and then disrupted for 10 minutes at 4 °C using an ultrasonic wave processor (Ultrasonic processor). The crushed liquid was heat-treated for 30 minutes at 60 °C shake incubator, centrifuged for 10 minutes at 13,000 rpm to ensure only the supernatant. The obtained supernatant was applied to Q-Sepharose DEAE, previously equilibrated with lysis buffer, and the target protein was purified by sequentially flowing a buffer solution containing 50 mM K-phosphate 200 mM NaCl. .
  • the eluted protein was converted to a buffer for measuring enzyme activity (50 mM K-phosphate, pH 7) and used in the next experiment after dialysis.
  • the purified seven D-fructose 4-epimerase enzymes RM, TAM, TAS, TAX, TP, TL, and DT have molecular weights of about 58kDa, 56kDa, 56kDa, 55kDa, 56kDa, 57kDa, It confirmed that it was 57 kDa.
  • Example 2-1 In order to confirm the activity of the D-fructose 4-epimerase according to the pH and temperature change of the seven enzymes purified in Example 2-1, the enzyme and the fructose substrate were reacted at various pH and temperature and the activity was confirmed.
  • the activity was measured in each pH and temperature range of 50Mm fructose, enzyme 1mg / ml, 0.1mM NiSO 4 , and the reaction was stopped on ice and analyzed by HPLC.
  • the HPLC analysis was performed using a SUGAR SP0810 (Shodex) column at 80 ° C. while flowing water into the mobile phase at a flow rate of 0.6 ml / min, and detecting tagatose with a differential index detector to increase tagatose productivity. Analyzed.
  • the maximum conversion rate was shown at 80 ° C. for TAM and TP, two of the seven enzymes. In the case of five species RM, TAS, TAX, TL, DT, the maximum conversion was shown at 70 °C (Fig. 3a to 3g).
  • TAX showed a particularly high activity at pH7, TP, TL, RM, and DT at pH8, TAS, and TAM at pH9.
  • the maximum activity in the Tris-HCl buffer solution was confirmed to show the highest activity in the buffer solution (FIGS. 4A to 4G).
  • Example 2-1 As shown in Figures 5a to 5g, it was confirmed that the enzyme of Example 2-1 can be produced tagatose from fructose.
  • Example 2-1 As shown in Figure 5a to 5g, the enzyme of Example 2-1 was found to increase the activity by the addition of nickel ions and cobalt ions it can be seen that there is a metal ion requirement. In particular, when NiSO 4 was added, it was confirmed to show the maximum activity.
  • Example 2 Tagatose productivity was confirmed under the optimum enzyme reaction conditions selected in Example 2. Specifically, the D-fructose 4-epimerase purified in Example 2-1 Using a concentration of 1mg / ml, the reaction temperature was 50m Tris-Cl at 80 ° C for two of the seven enzymes, at 80 ° C for five species, RM, TAS, TAX, TL, and DT for 70%. Each buffer was prepared for each pH, and TAX reacted with 20g / L (about 110mM concentration) fructose under the conditions of pH7, TP, TL, RM, DT for pH8, TAS and TAM for pH9 and 0.1mM of nickel sulfate.
  • 20g / L about 110mM concentration
  • HPLC analysis was performed in the same manner as in Example 2-2 (FIGS. 2A to 2G).
  • the conversion rate from fructose to tagatose was measured. The results are shown in Table 2.
  • reaction completion liquid (tagatose and fructose mixed solution) can be secured through decolorization (using activated carbon), ion purification, chromatography, crystallization, and final crystal tagatose.

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PCT/KR2015/011007 2014-10-22 2015-10-19 타가토스 제조용 조성물 및 과당으로부터 타가토스를 제조하는 방법 Ceased WO2016064146A1 (ko)

Priority Applications (7)

Application Number Priority Date Filing Date Title
UAA201703549A UA119791C2 (uk) 2014-10-22 2015-10-19 Композиція для одержання тагатози та спосіб одержання тагатози з фруктози
CN201580057200.3A CN107109394B (zh) 2014-10-22 2015-10-19 用于制备塔格糖的组合物以及从果胶制备塔格糖的方法
RU2017113926A RU2701669C2 (ru) 2014-10-22 2015-10-19 Композиция для получения тагатозы и способ получения тагатозы из фруктозы
ES15852026T ES2721309T3 (es) 2014-10-22 2015-10-19 Composición para preparar tagatosa y método para preparar tagatosa a partir de fructosa
EP15852026.2A EP3211078B1 (en) 2014-10-22 2015-10-19 Composition for preparing tagatose and method for preparing tagatose from fructose
JP2017521088A JP6518761B2 (ja) 2014-10-22 2015-10-19 タガトース製造用の組成物とフルクトースからタガトースを製造する方法
US15/521,243 US10544438B2 (en) 2014-10-22 2015-10-19 Composition for preparing tagatose and method for preparing tagatose from fructose

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KR1020140143703A KR101638024B1 (ko) 2014-10-22 2014-10-22 타가토스 제조용 조성물 및 과당으로부터 타가토스를 제조하는 방법
KR10-2014-0143703 2014-10-22

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Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2018526011A (ja) * 2016-07-29 2018-09-13 シージェイ チェルジェダン コーポレイション Ｄ−タガトース転換活性が高められたヘキスロン酸ｃ４−エピメラーゼ変異体及びこれを用いたｄ−タガトースの製造方法
WO2020081959A1 (en) 2018-10-19 2020-04-23 Bonumose Llc Enzymatic production of tagatose
CN113272439A (zh) * 2018-09-28 2021-08-17 Cj第一制糖株式会社 新型果糖-4-差向异构酶以及使用其制备塔格糖的方法
US20220372534A1 (en) * 2018-10-19 2022-11-24 Cj Cheiljedang Corporation Novel fructose-4-epimerase and method for preparing tagatose using same

Families Citing this family (14)

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Publication number Priority date Publication date Assignee Title
PL3322803T3 (pl) 2015-10-02 2021-09-27 Bonumose, Inc. Enzymatyczne wytwarzanie d-tagatozy
CN111344405B (zh) 2017-03-31 2023-12-22 Cj第一制糖株式会社 用于制备塔格糖的组合物和利用其制备塔格糖的方法
CA3057595C (en) * 2017-03-31 2024-11-12 Cj Cheiljedang Corporation Composition for the production of tagatose and process for the production of tagatose employing it
WO2019004702A2 (ko) * 2017-06-28 2019-01-03 주식회사 삼양사 기능성 감미료의 제조방법
EP3677675A4 (en) * 2017-08-31 2021-06-09 CJ Cheiljedang Corporation FRUCTOSE-4-EPIMERASE AND METHOD FOR MANUFACTURING TAGATOSE USING THE SAME
CN109750024B (zh) 2017-11-02 2021-12-14 中国科学院天津工业生物技术研究所 一种6磷酸塔格糖4位差向异构酶及其应用
CN108774636A (zh) * 2018-06-25 2018-11-09 嘉兴欣贝莱生物科技有限公司 一种酿酒酵母发酵生产d-塔格糖的方法
US11060119B2 (en) 2018-07-03 2021-07-13 Arzeda Corp. Methods and compositions for preparing tagatose from fructose
KR102328650B1 (ko) * 2018-09-27 2021-11-19 씨제이제일제당 주식회사 신규 과당-4-에피머화 효소 및 이를 이용한 타가토스의 제조 방법
KR102219195B1 (ko) * 2019-08-14 2021-02-24 씨제이제일제당 주식회사 신규 과당-4-에피머화 효소 및 이를 이용한 타가토스의 제조 방법
KR102362873B1 (ko) * 2020-06-05 2022-02-11 건국대학교 산학협력단 타카투론산 에피머화 효소 변이체 및 이를 이용한 과당으로부터 타카토스의 생산방법
EP4464785A1 (de) 2023-05-15 2024-11-20 Annikki GmbH Verfahren zur herstellung von d-talitol, d-tagatose und d-psicose
EP4713470A1 (de) 2023-05-15 2026-03-25 Annikki GmbH Verfahren zur herstellung von d-talitol, d-tagatose und d-psicose
CN119932003B (zh) * 2024-12-19 2025-11-14 浙江工业大学 一种塔格糖-4-差向异构酶突变体及其在制备d-塔格糖中的应用

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR20040035683A (ko) * 2001-07-16 2004-04-29 아를라 푸즈 에이엠비에이 타가토스의 제조 방법
KR20080053708A (ko) * 2006-12-11 2008-06-16 씨제이제일제당 (주) 높은 전환율의 갈락토스 이성화 반응을 이용한 타가토스의제조방법

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR100964091B1 (ko) 2008-01-28 2010-06-16 씨제이제일제당 (주) 대두 올리고당을 이용한 타가토스의 제조 방법
MX374397B (es) * 2013-06-05 2025-03-06 Cj Cheiljedang Corp Metodo de produccion para tagatosa.
KR101868194B1 (ko) 2013-11-19 2018-06-18 씨제이제일제당 (주) 호열균 유래 당 에피머화효소를 포함하는, 비인산헥소오스의 에피머화용 조성물

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR20040035683A (ko) * 2001-07-16 2004-04-29 아를라 푸즈 에이엠비에이 타가토스의 제조 방법
KR20080053708A (ko) * 2006-12-11 2008-06-16 씨제이제일제당 (주) 높은 전환율의 갈락토스 이성화 반응을 이용한 타가토스의제조방법

Non-Patent Citations (9)

* Cited by examiner, † Cited by third party
Title
DATABASE NCBI 16 May 2013 (2013-05-16), Database accession no. WP_011943119.1 *
DATABASE NCBI 16 May 2013 (2013-05-16), Database accession no. WP_012002872.1 *
DATABASE NCBI 17 May 2013 (2013-05-17), Database accession no. WP_012582608.1 *
DATABASE NCBI 18 May 2013 (2013-05-18), Database accession no. WP_012844026.1 *
DATABASE NCBI 18 May 2013 (2013-05-18), Database accession no. WP_013150657.1 *
DATABASE NCBI 18 May 2013 (2013-05-18), Database accession no. WP_013788787.1 *
DATABASE NCBI 28 May 2013 (2013-05-28), Database accession no. WP_006569468.1 *
KIM, HYE-JUNG ET AL.: "Novel activity of UDP-galactose-4-epimerase for free monosaccharide and activity improvement by active site-saturation mutagenesis", APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, vol. 163, no. 3, 2011, pages 444 - 451, XP055300273 *
See also references of EP3211078A4 *

Cited By (14)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2018526011A (ja) * 2016-07-29 2018-09-13 シージェイ チェルジェダン コーポレイション Ｄ−タガトース転換活性が高められたヘキスロン酸ｃ４−エピメラーゼ変異体及びこれを用いたｄ−タガトースの製造方法
CN108884454A (zh) * 2016-07-29 2018-11-23 Cj第制糖株式会社 具有改良的d-塔格糖转化活性的己糖醛酸酯c4-差向异构酶变异体和用它制造d-塔格糖的方法
JP2018536425A (ja) * 2016-07-29 2018-12-13 シージェイ チェルジェダン コーポレイション Ｄ−タガトース転換活性が高められたヘキスロン酸ｃ４−エピメラーゼ変異体及びこれを用いたｄ−タガトースの製造方法
JP2018536422A (ja) * 2016-07-29 2018-12-13 シージェイ チェルジェダン コーポレイション Ｄ−タガトース転換活性が高められたヘキスロン酸ｃ４−エピメラーゼ変異体及びこれを用いたｄ−タガトースの製造方法
JP2019507601A (ja) * 2016-07-29 2019-03-22 シージェイ チェルジェダン コーポレイション Ｄ−タガトース転換活性が高められたヘキスロン酸ｃ４−エピメラーゼ変異体及びこれを用いたｄ−タガトースの製造方法
US20190112589A1 (en) * 2016-07-29 2019-04-18 Cj Cheiljedang Corporation Hexuronate c4-epimerase variant having improved d-tagatose conversion activity, and d-tagatose production method using same
CN108884454B (zh) * 2016-07-29 2022-08-30 Cj第一制糖株式会社 己糖醛酸酯c4-差向异构酶变异体、核酸和制造d-塔格糖的方法
US10801020B2 (en) * 2016-07-29 2020-10-13 Cj Cheiljedang Corporation Hexuronate C4-epimerase variant having improved d-tagatose conversion activity, and d-tagatose production method using same
EP3492589A4 (en) * 2016-07-29 2020-11-04 Cj Cheiljedang Corporation C4-EPIMERASE HEXURONATE VARIANT WITH ENHANCED D-TAGATOSE CONVERSION ACTIVITY, AND PROCESS FOR PRODUCING D-TAGATOSE USING THIS VARIANT
CN113272439A (zh) * 2018-09-28 2021-08-17 Cj第一制糖株式会社 新型果糖-4-差向异构酶以及使用其制备塔格糖的方法
CN113272439B (zh) * 2018-09-28 2023-10-20 Cj第一制糖株式会社 新型果糖-4-差向异构酶以及使用其制备塔格糖的方法
WO2020081959A1 (en) 2018-10-19 2020-04-23 Bonumose Llc Enzymatic production of tagatose
US20220372534A1 (en) * 2018-10-19 2022-11-24 Cj Cheiljedang Corporation Novel fructose-4-epimerase and method for preparing tagatose using same
US12098401B2 (en) * 2018-10-19 2024-09-24 Cj Cheiljedang Corporation Fructose-4-epimerase and method for preparing tagatose using same

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JP2017531438A (ja) 2017-10-26
CN107109394B (zh) 2021-01-15
UA119791C2 (uk) 2019-08-12
RU2017113926A3 (https=) 2018-11-22
KR20160047361A (ko) 2016-05-02
ES2721309T3 (es) 2019-07-30
KR101638024B1 (ko) 2016-07-20
CN107109394A (zh) 2017-08-29
JP6518761B2 (ja) 2019-05-22
US20170306370A1 (en) 2017-10-26
RU2017113926A (ru) 2018-11-22
RU2701669C2 (ru) 2019-09-30

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