WO2014122005A1 - Culture autotrophique - Google Patents

Culture autotrophique Download PDF

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Publication number
WO2014122005A1
WO2014122005A1 PCT/EP2014/051074 EP2014051074W WO2014122005A1 WO 2014122005 A1 WO2014122005 A1 WO 2014122005A1 EP 2014051074 W EP2014051074 W EP 2014051074W WO 2014122005 A1 WO2014122005 A1 WO 2014122005A1
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WO
WIPO (PCT)
Prior art keywords
cells
enzyme
coenzyme
activity
wild
Prior art date
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Ceased
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PCT/EP2014/051074
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German (de)
English (en)
Inventor
Thomas Haas
Markus PÖTTER
Martin DEMLER
Eva-Maria Eckl
Simon PRZYBILLA
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Evonik Industries AG
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Evonik Industries AG
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
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Publication date
Application filed by Evonik Industries AG filed Critical Evonik Industries AG
Priority to EP14701509.3A priority Critical patent/EP2954052A1/fr
Priority to BR112015019156A priority patent/BR112015019156A2/pt
Priority to CA2900293A priority patent/CA2900293A1/fr
Priority to CN201480007955.8A priority patent/CN104955945A/zh
Priority to RU2015137939A priority patent/RU2015137939A/ru
Priority to MX2015009925A priority patent/MX2015009925A/es
Priority to KR1020157024127A priority patent/KR20150115905A/ko
Publication of WO2014122005A1 publication Critical patent/WO2014122005A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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    • 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
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/40—Preparation of oxygen-containing organic compounds containing a carboxyl group including Peroxycarboxylic acids
    • C12P7/42—Hydroxy-carboxylic acids
    • 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

Definitions

  • the invention relates to a method comprising an autotrophic cultivation of cells.
  • PRIOR ART In the fermentative production of products, efforts are always made to avoid or minimize the formation of undesirable by-products as far as possible. In general, one can thus increase the product yield and also the purification of the
  • Organisms producing polyhydroxyalkanoate use as precursor 3-hydroxyalkanyl-CoA.
  • This metabolic product can serve as an excellent starting substance, in particular to be metabolized by artificially inserted metabolic pathways to other, high-quality organic substances.
  • the object of the invention was to provide a process which reduces by-product formation in fermentation processes and thus increases the yield of monomer units of the polyhydroxyalkanoate reduced in the biosynthesis.
  • Precultivation which in particular serves for the generation of cell mass, is carried out under autotrophic conditions, followed by a further autotrophic cultivation, which preferably serves for product formation over at least a part-time range of the cultivation.
  • An advantage of the present invention is that unwanted by-products such as acetate, lactate, pyruvate, succinate, alanine, valine, butanol, butyrate, malate, acetone, 2-methyl-propionic acid or 3-methyl-butyrate, especially acetate, pyruvate and acetone, are formed significantly reduced.
  • the present invention advantageously increases the space-time yield.
  • Yet another advantage of the present invention is that the desired product can be more easily isolated.
  • Yet another advantage of the present invention is that one can operate completely independently of complex carbon sources, such as sugars.
  • Yet another advantage of the present invention is that it binds carbon dioxide, which could otherwise be problematic as a greenhouse gas.
  • the method according to the invention comprises the method steps
  • under autotrophic conditions in the context of the present invention is to be understood as culturing conditions in which the carbon source available to the cells contains at least 90% by weight, based on carbon atoms, of inorganic carbon.
  • a wild-type cell is preferably referred to as a cell whose genome is in a state as naturally produced by evolution, and is used for both the entire cell and for individual genes. fall therefore in particular not such cells or genes whose Gene sequences have been altered at least in part by humans by recombinant methods.
  • reduced polyhydroxyalkanoate synthesis compared to wild-type in the context of the present invention is meant that the cultured cells, when cultured under the same conditions as the wild-type, produce less polyhydroxyalkanoate per cell than the wild-type.
  • the cells used in the method according to the invention are genetically engineered, therefore recombinant cells. They can be prokaryotes or eukaryotes. These may be mammalian cells (such as human cells), plant cells, or microorganisms such as yeasts, fungi or bacteria, with microorganisms being most preferred and bacteria and yeasts being most preferred. It is preferred according to the invention that the cells used are selected from acetogenic bacteria or oxyhydrogen bacteria.
  • explosive gas bacterium a bacterium capable of growing chemolithoautotrophically and of H 2 and C0 2 in the presence of oxygen
  • Oxy-gas bacteria preferably used according to the invention are selected from the genera Achromobacter, Acidithiobacillus, Acidovorax, Alcaligenes, Anabena, Ancyclobacter, Aquifex, Arthrobacter, Azospirillum, Bacillus, Bradyrhizobium, Cupriavidus, Derxia, Helicobacter,
  • Mycobacterium Nocardia, Oligotropha, Paracoccus, Pelomonas, Polaromonas, Pseudomonas, Pseudonocardia, Rhizobium, Rhodococcus, Rhodopseudomonas, Rhodospirillum, Seliberia, Streptomyces, Thiocapsa, Variovorax, Xanthobacter, Wautersia, cupriavidus being particularly preferred especially from the species Cupriavidus necator (also known as Ralstonia eutropha, Wautersia eutropha, Alcaligenes eutrophus, Hydrogenomonas eutropha), Achromobacter ruhlandii, Acidithiobacillus ferrooxidans, Acidovorax facilis, Alcaligenes hydrogenophilus, Alcaligenes latus, Anabena cylindrica, Anabena oscillaroides, Ana
  • Herbaspirillum autotrophicum Hydrogenobacter hydrogenophilus, Hydrogenobacter thermophilus, Hydrogenobaculum acidophilum, Hydrogenophaga flava, Hydrogenophaga palleronii, Hydrogenophaga pseudoflava, Hydrogenophaga taeniospirales, Hydrogeneophilus thermoluteolus, Hydrogenothermus marinus, Hydrogenovibrio marinus, Ideonella sp. 0-1, Kyrpidia tusciae, Metallosphaera sedula, Myobacterium gordonae, Nocardia autotrophica, Oligotropha carboxidivorans, Paracoccus denitrificans, Pelomonas saccharophila,
  • Polaromonas hydrogenivorans Pseudomonas hydrogenovora, Pseudomonas thermophila, Rhizobium japonicum, Rhodococcus opacus, Rhodopseudomonas palustris, Seliberia carboxydohydrogena, Thiocapsa roseopersicina, Variovorax paradoxus, Xanthobacter autrophicus, Xanthobacter flavus, Cupriavidus necator is particularly preferred, in particular from the strains Cupriavidus necator H 16, Cupriavidus necator H1 or Cupriavidus necator Z-1.
  • polyhydroxyalkanoate Preferably, the polyhydroxyalkanoate whose synthesis is reduced, polyhydroxybutyrate.
  • the reduced compared to the wild type polyhydroxyalkanoate synthesis can preferably be achieved by a genetic modification, so that compared to the wild-type cell reduced activity of at least one enzyme, which is the conversion of 3-hydroxyalkanyl coenzyme A to polyhydroxyalkanoate, preferably 3-hydroxybutyryl Coenzyme A too
  • this is preferably a factor reduced by a factor of at least 0.5, more preferably of at least 0.1, more preferably of at least 0.01, even more preferably of at least 0.001, and most preferably of at least 0.0001.
  • the phrase "decreased activity” also does not include any detectable activity ("zero activity”).
  • the reduction of the activity of a particular Enzyme can be carried out, for example, by targeted mutation or by other measures known in the art for reducing the activity of a particular enzyme. Methods for reducing enzymatic activities in microorganisms are known to the person skilled in the art, these include insertion of foreign DNA into the gene coding for the target enzyme, deletion of at least parts of the gene coding for the target enzyme,
  • RNA interference siRNA
  • antisense RNA modification (insertion, deletion or point mutations) of
  • regulatory sequences such as promoters and terminators or of
  • foreign DNA is to be understood as any DNA sequence which is "foreign” to the gene (and not to the organism), that is to say endogenous DNA sequences may also function as “foreign DNA” in this connection.
  • Polyhydroxyalkanoate is preferably a polyhydroxyalkanoate synthase, more preferably a polyhydroxybutyrate synthase.
  • this enzyme is preferably encoded by the genes phbC or phaC, with phaC being particularly preferred.
  • the method is used in method step A) under autotrophic conditions, thus under conditions in which the carbon source available to the cells to at least 90 wt .-%, preferably 95 wt .-%, particularly preferably 99 wt .-% based on carbon atoms, inorganic carbon ,
  • inventive method step A) is used, in particular in the form of substances supplied, selected from the group comprising, preferably consisting of carbonates, carbon dioxide and carbon monoxide, carbon dioxide being particularly preferred. It is also possible to use mixtures of the carbon sources in process step A).
  • the medium in which the cells are contained is containing a gas
  • the cells are preferably multiplied by at least 10-fold, more preferably by at least 100-fold, in particular by at least 1000-fold, based on the number of cells per volume of the total culture.
  • the cell density X in method step A is preferably at least 1 ⁇ 10 5 , more preferably at least 1 ⁇ 10 7 , in particular at least 1 ⁇ 10 8 cells / ml of total culture.
  • step B) of the method according to the invention dilution of the cells with medium takes place.
  • the medium used can be the same as used in process step 1, but it can also be a different one.
  • the cells are under autotrophic conditions, thus under conditions in which the carbon source available to the cells to at least 90 wt .-%, preferably 95 wt .-%, particularly preferably 99 wt .-% based on carbon atoms , inorganic carbon contains, increased.
  • Carbon which is used in process step C) according to the invention is supplied in particular in the form of substances selected from the group comprising, preferably consisting of carbonates, carbon dioxide and carbon monoxide, carbon dioxide being particularly preferred.
  • carbonates preferably consisting of carbonates, carbon dioxide and carbon monoxide, carbon dioxide being particularly preferred.
  • Carbon sources are used.
  • Process step C) is advantageously and thus preferably used for at least part of the time range for product production.
  • Process step C) synthesized by the cells target products whose formation on the
  • the desired product can be reacted, wherein as a "chemical compound" those with or without coenzyme A thioester functionalization should be considered equivalent and thus the thioester forming or cleaving enzymes are not counted.
  • a preferred target product is 2-hydroxyisobutyric acid.
  • the cell used in the method according to the invention has an increased compared to their wild type activity of the enzyme egg, which catalyzes the conversion of 3-hydroxybutyryl-coenzyme A to 2-hydroxyisobutyryl-coenzyme A.
  • the enzyme Ei is preferably a hydroxyl isobutyryl-CoA mutase, an isobutyryl-CoA mutase (EC 5.4.99.13) or a
  • Methylmalonyl-CoA mutase (EC 5.4.99.2), each preferably a coenzyme B12-dependent mutase.
  • the enzyme Ei is preferably those enzymes which are derived from the
  • DQ436456.1 of at least 60%, preferably of at least 80%, more preferably of at least 95%, most preferably at least 99% at the amino acid level, determined according to the blastp algorithm with an expect threshold of 10, a word size of 3, a blosum62 matrix with gap costs of existence: 1 1 and extension: 1 and a conditional compositional score matrix adjustment.
  • enhanced activity of an enzyme as used above in connection with the enzyme Ei and in the following statements in connection with the enzymes E 2 , etc., is preferably to be understood as an increased intracellular activity the enzyme activity in cells apply both to the increase in the activity of the enzyme E- ⁇ and for all the enzymes mentioned below, the activity of which may optionally be increased.
  • an increase in enzymatic activity can be achieved by increasing the copy number of the gene sequence or gene sequences which code for the enzyme, using a strong promoter, changing the codon usage of the gene, in various ways the half-life of the mRNA or of the enzyme that increases
  • the gene coding for the enzyme E x overexpressed, resulting in increased activity through overexpression.
  • Genetically modified cells according to the invention are produced, for example, by transformation, transduction, conjugation or a combination of these methods with a vector which contains the desired gene, an allele of this gene or parts thereof and a promoter which enables the expression of the gene.
  • Heterologous expression is particularly by integration of the gene or alleles in the chromosome of the cell or a
  • Protein separations between wild type and genetically engineered cell can be determined.
  • a common method for preparing the protein gels in coryneform bacteria and for identifying the proteins is that described by Hermann et al. (Electrophoresis, 22: 1712.23 (2001).) Protein concentration can also be assessed by Western blot hybridization with an antibody specific for the protein to be detected (Sambrook et al., Molecular Cloning: a laboratory manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY USA, 1989) and subsequent optical evaluation with appropriate software for concentration determination (Lohaus and Meyer (1989) Biospektrum, 5: 32-39; Lottspeich (1999), Angewandte Chemie 1 1 1: 2630-2647)
  • the activity of DNA-binding proteins can be measured by DNA band shift assays (also referred to as gel retardation) (Wilson et al., (2001) Journal of Bacteriology, 183: 2151-2155.)
  • the intracellular enzymatic activities can be determined by various methods described (Donahue et al., (2000) Journal of Bacteriology 182 (19): 5624-5627, Ray et al., (2000) Journal of Bacteriology 182 (8): 2277-2284, Freedberg et (1973) Journal of Bacteriology 1 15 (3): 816-823).
  • mutations can be generated either undirected by classical methods, such as by UV irradiation or by mutagenic chemicals, or specifically by genetic engineering methods such as deletion (s), insertion (s) and or
  • Nucleotide substitution results in altered cells.
  • Particularly preferred mutants of enzymes are, in particular, also those enzymes which are no longer or at least less feedback-inhibitable in comparison with the wild-type enzyme.
  • RNA polymerase For example, one increases the copy number of the corresponding genes or mutates the promoter and regulatory region or the ribosome binding site, which is located upstream of the structural gene.
  • expression cassettes act, which are installed upstream of the structural gene.
  • Inducible promoters also make it possible to increase expression at any time.
  • the enzyme gene can be assigned as regulatory sequences but also so-called “enhancers", which have an improved interaction between RNA polymerase and
  • DNA also cause increased gene expression. Measures to extend the lifetime of mRNA also improve expression. Furthermore, by
  • genes or gene constructs are either present in plasmids with different copy numbers or are integrated and amplified in the chromosome. Alternatively, a further
  • episomal plasmids are used, for example. In principle, all embodiments which are available to the person skilled in the art for this purpose are suitable as plasmids or vectors. Such plasmids and
  • Vectors can, for. B. the brochures of the companies Novagen, Promega, New England Biolabs, Clontech or Gibco BRL be removed. Further preferred plasmids and vectors can be found in: Glover, D.M. (1985), DNA cloning: a practical approach, Vol. I-Ill, IRL Press Ltd. , Oxford; Rodriguez, R.L. and Denhardt, D.T (eds) (1988), Vectors: a survey of molecular cloning vectors and their uses, 179-204, Butterworth, Stoneham; Goeddel, D.V. (1990), Systems for heterologous gene expression, Methods Enzymol. 185, 3-7; Sambrook, J .; Fritsch, E.F. and Maniatis, T. (1989), Molecular cloning: a laboratory manual, 2nd ed., Cold Spring Harbor Laboratory Press, New York.
  • the plasmid vector containing the gene to be amplified is then passed through
  • Conjugation or transformation into the desired strain is described, for example, in Schwarzerbach et al., Applied and Environmental Microbiology 60: 756-759 (1994). Methods for transformation are described, for example, in Thierbach et al., Applied Microbiology and Biotechnology 29: 356-362 (1988), Dunican and Shivnan, Bio / Technology 7: 1067-1070 (1989), and Tauch et al., FEMS Microbiology Letters 123: 343-347 (1994). After homologous recombination by means of a cross-over event, the resulting strain contains at least two copies of the gene of interest.
  • an increased activity of an enzyme E x which is increased in comparison with its wild type, is preferably always a factor greater than or equal to at least 2, particularly preferably at least 10, more preferably at least 100, moreover even more preferably of at least 1, 000 and most preferably of at least 10,000 increased activity of the respective enzyme E x
  • the cell according to the invention comprises "an activity of an enzyme E x increased compared to its wild type, in particular also a cell whose wild type has no or at least no detectable activity of this enzyme E x and which only after increasing the enzyme activity, for example by overexpression, a
  • the term "overexpression” or the expression “increase in expression” used in the following also encompasses the case that a starting cell, for example a wild-type cell, has no or at least no detectable expression and only by recombinant methods a detectable Synthesis of the enzyme E x is induced. It can furthermore be advantageous if the cells used in the method according to the invention have an increased activity of an enzyme E 2 compared to their wild-type, which inhibits the Reaction of acetoacetyl-coenzyme A catalyzed to 3-hydroxybutyryl-coenzyme A have.
  • the enzyme E 2 is preferably an enzyme selected from the group comprising:
  • This enzyme is preferably encoded by the genes selected from the group consisting of phaB, phbB, fabG, phbN1, phbB2 or, with phaB, phbB being particularly preferred.
  • the nucleotide sequence of these genes may be, for example, the "Kyoto
  • the process according to the invention preferably has a process step D) purification of the target product.
  • a process step D purification of the target product.
  • Embodiments should be limited.
  • Cupriavidus necator H16 PHB1 pBBR1 MCS-2 :: icmA-icmB (lac) (hereinafter called RITA).
  • the RITA strain is transformed with an expression vector for icmA and icmB from Aquincola tertiaricarbonis. A detailed generation of the strain is described in Example 2 of WO2009156214.
  • the medium was used according to Vollbrecht, consisting of 2 g / l (NH 4 ) 2 HP0 4 , 2.1 g / l KH 2 P0 4 , 0.2 g / l MgS0 4 , 0.01 g / l CaCl 2 , 6 mg / l FeCl 3 , 0.05 mg / l Titriplex III, 0.02 mg / l FeSO 4 ⁇ 7 H 2 O, 1 g / l ZnSO 4 ⁇ 7 H 2 O, 0.3 g / l MnCl 2 x 4 H 2 0, 3 g / l H 3 B0 3 , 2 Mg / l CoCl 2 x 6 H 2 O, 0.1 pg / l CuCl 2 x 2 H 2 O, 0.2 Mg 1 NiCl 2 x 6 H 2 0 and 0.3 Mg l Na 2 M04 x 2 H 2 0.
  • Heterotrophic preculture (method step A) but heterotrophic, not according to the invention):
  • the preculture was carried out in 500 ml shake flasks with 50 ml of medium per strain in duplicate.
  • the preculture was inoculated with a single colony from an agar plate.
  • the incubation was carried out at 30 ° C and 150 rpm for 28.5 hours.
  • the cultures were centrifuged for 10 min at 4500 x g.
  • pellets were resuspended in 2 ml of medium and added to the main autotrophic culture (see there).
  • the preculture was carried out in 250 ml pressure-resistant coated Schott bottles with 50 ml of medium.
  • Bottle cap had a gassing frit, an exhaust filter and a sampling tube.
  • the bottles were rinsed 3 times with N 2 and 3 times with oxyhydrogen before seeding.
  • the experiment took place at 0.8 bar overpressure, 28 ° C and 150 rpm.
  • the fumigation took place with oxyhydrogen gas
  • Composition 4% 0 2 , 6% C0 2 and 90% H 2 Composition 4% 0 2 , 6% C0 2 and 90% H 2 .
  • the preculture was inoculated with a single colony from an agar plate.
  • the cultivation period was 143 hours.
  • the cultures were centrifuged for 10 min at 4500 x g.
  • the pellets were resuspended in 2 ml of medium and added to the main autotrophic culture (see there).
  • the main culture was carried out in pressure-resistant coated 250 ml Schott bottles with 50 ml of medium.
  • the bottle cap had a gassing frit, an exhaust filter and a sampling tube.
  • the bottles were rinsed 3 times with N 2 and 3 times with oxyhydrogen before seeding.
  • the experiment took place at 0.8 bar overpressure, 28 ° C and 150 rpm, each strain in duplicate. It is inoculated to a start OD of 0.5.
  • the fumigation was carried out with oxyhydrogen of composition 4% 0 2 , 6% C0 2 and 90% H 2 .
  • the sampling took place after 25 hours.
  • the cultures were centrifuged off at 4500 ⁇ g for 10 min and the supernatant was analyzed by means of NMR. Observations:

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Abstract

L'invention concerne un procédé comprenant les étapes consistant à A) multiplier les cellules qui ont été génétiquement modifiées de manière à présenter par rapport à leur type sauvage une synthèse de polyhydroxyalcanoate réduite dans un milieu dans des conditions autotrophiques allant jusqu'à une densité cellulaire de X cellules/Litre, B) diluer au moins une partie des cellules à une densité cellulaire de 0,001 X à 0,5 X, de préférence de 0,01 X à 0,3 X, idéalement de 0,05 X à 0,2 X dans un milieu et C) multiplier ladite au moins une partie de cellules dans des conditions autotrophiques.
PCT/EP2014/051074 2013-02-08 2014-01-21 Culture autotrophique Ceased WO2014122005A1 (fr)

Priority Applications (7)

Application Number Priority Date Filing Date Title
EP14701509.3A EP2954052A1 (fr) 2013-02-08 2014-01-21 Culture autotrophique
BR112015019156A BR112015019156A2 (pt) 2013-02-08 2014-01-21 cultivo autotrófico
CA2900293A CA2900293A1 (fr) 2013-02-08 2014-01-21 Culture autotrophique
CN201480007955.8A CN104955945A (zh) 2013-02-08 2014-01-21 自养培养
RU2015137939A RU2015137939A (ru) 2013-02-08 2014-01-21 Автотрофное культивирование
MX2015009925A MX2015009925A (es) 2013-02-08 2014-01-21 Cultivo autotrofico.
KR1020157024127A KR20150115905A (ko) 2013-02-08 2014-01-21 독립영양성 배양

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DE102013202106.2A DE102013202106A1 (de) 2013-02-08 2013-02-08 Autotrophe Kultivierung
DE102013202106.2 2013-02-08

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EP (1) EP2954052A1 (fr)
KR (1) KR20150115905A (fr)
CN (1) CN104955945A (fr)
BR (1) BR112015019156A2 (fr)
CA (1) CA2900293A1 (fr)
DE (1) DE102013202106A1 (fr)
MX (1) MX2015009925A (fr)
RU (1) RU2015137939A (fr)
WO (1) WO2014122005A1 (fr)

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US10787688B2 (en) 2012-05-11 2020-09-29 Evonik Operations Gmbh Multi-stage synthesis method with synthesis gas
EP4108776A1 (fr) * 2021-06-22 2022-12-28 CO2BioClean GmbH Production de biopolymères

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EP2944697A1 (fr) 2014-05-13 2015-11-18 Evonik Degussa GmbH Procédé de production de nylon
EP3390622B1 (fr) 2015-12-17 2020-05-13 Evonik Operations GmbH Cellule acétogène génétiquement modifiée
JP2019523271A (ja) 2016-07-27 2019-08-22 エボニック デグサ ゲーエムベーハーＥｖｏｎｉｋ Ｄｅｇｕｓｓａ ＧｍｂＨ Ｎ−アセチルホモセリン
WO2021130128A1 (fr) * 2019-12-23 2021-07-01 Co2Bioclean Gmbh Nouveaux bioplastiques
KR20220123019A (ko) 2019-12-31 2022-09-05 에어 프로틴 인코포레이티드 고단백질 식품 조성물
EP4093848A4 (fr) * 2020-01-24 2024-08-07 Air Protein, Inc. Hydrolysats de protéines dérivés de micro-organisme, ainsi que leurs méthodes de préparation et d'utilisation
CN113046260B (zh) * 2021-02-04 2023-04-25 兴安盟莱绅生物农业有限公司 一种促进大豆生长的微生物混合菌剂及其应用

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MX2015009925A (es) 2015-09-25
EP2954052A1 (fr) 2015-12-16
CN104955945A (zh) 2015-09-30
BR112015019156A2 (pt) 2017-07-18

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