[go: up one dir, main page]

WO2024203813A1 - Décomposition enzymatique de pef - Google Patents

Décomposition enzymatique de pef Download PDF

Info

Publication number
WO2024203813A1
WO2024203813A1 PCT/JP2024/011218 JP2024011218W WO2024203813A1 WO 2024203813 A1 WO2024203813 A1 WO 2024203813A1 JP 2024011218 W JP2024011218 W JP 2024011218W WO 2024203813 A1 WO2024203813 A1 WO 2024203813A1
Authority
WO
WIPO (PCT)
Prior art keywords
cutinase
amino acid
pef
acid sequence
plastic
Prior art date
Legal status (The legal status 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 status listed.)
Pending
Application number
PCT/JP2024/011218
Other languages
English (en)
Japanese (ja)
Inventor
遠山 絹華 太田
研吾 西村
勝巳 辻
淳 川井
昭介 吉田
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Nara Institute of Science and Technology NUC
Toyobo Co Ltd
Original Assignee
Nara Institute of Science and Technology NUC
Toyobo Co Ltd
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.)
Filing date
Publication date
Application filed by Nara Institute of Science and Technology NUC, Toyobo Co Ltd filed Critical Nara Institute of Science and Technology NUC
Publication of WO2024203813A1 publication Critical patent/WO2024203813A1/fr
Anticipated expiration legal-status Critical
Pending legal-status Critical Current

Links

Images

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
    • 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
    • C12P1/00—Preparation of compounds or compositions, not provided for in groups C12P3/00 - C12P39/00, by using microorganisms or enzymes
    • 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
    • C12P17/00—Preparation of heterocyclic carbon compounds with only O, N, S, Se or Te as ring hetero atoms
    • C12P17/02—Oxygen as only ring hetero atoms
    • C12P17/04—Oxygen as only ring hetero atoms containing a five-membered hetero ring, e.g. griseofulvin, vitamin C
    • 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
    • Y02W—CLIMATE CHANGE MITIGATION TECHNOLOGIES RELATED TO WASTEWATER TREATMENT OR WASTE MANAGEMENT
    • Y02W30/00—Technologies for solid waste management
    • Y02W30/50—Reuse, recycling or recovery technologies
    • Y02W30/62—Plastics recycling; Rubber recycling

Definitions

  • Plastics are cheap, durable and versatile materials used in a wide range of products. However, because of their durability, plastics also contribute to environmental problems, with significant amounts of them accumulating in landfills and natural habitats around the world.
  • Patent Document 1 proposes using cutinase to decompose the polyester that makes up plastics.
  • PET Polyethylene furanoate
  • FDCA furandicarboxylic acid
  • PEF also faces challenges related to the environmental issues of plastics. Therefore, one challenge is to provide a means to selectively decompose PEF.
  • cutinase is capable of decomposing polyethylene furanoate, and that its specificity for polyethylene furanoate changes depending on the reaction temperature. Based on this knowledge, further research has been carried out, and the invention encompasses the following:
  • Item 1 A method for decomposing plastics, comprising: The method comprises: subjecting a cutinase to the action of the plastic at a temperature of 60° C. or higher; The plastic includes polyethylene furanoate; The cutinase has an amino acid sequence having 90% or more identity to the amino acid sequence of SEQ ID NO:1. method.
  • Item 2. Item 10. The method of item 1, wherein the temperature is 65°C or higher.
  • Item 3. The method of claim 1 or 2, wherein the plastic further comprises polyethylene terephthalate.
  • the method according to any one of items 1 to 3, further comprising recovering one or more selected from the group consisting of 2,5-furandicarboxylic acid (FDCA), monohydroxyethyl 2,5-furandicarboxylate (MHEF), and bishydroxyethyl 2,5-furandicarboxylate (BHEF).
  • FDCA 2,5-furandicarboxylic acid
  • MHEF monohydroxyethyl 2,5-furandicarboxylate
  • BHEF bishydroxyethyl 2,5-furandicarboxylate
  • the method comprises the step of treating a plastic containing polyethylene furanoate with cutinase at a temperature of 60° C. or higher, The cutinase has an amino acid sequence having 90% or more identity to the amino acid sequence of SEQ ID NO:1.
  • a method for producing one or more decomposition products selected from the group consisting of 2,5-furandicarboxylic acid (FDCA), monohydroxyethyl 2,5-furandicarboxylate (MHEF), and bishydroxyethyl 2,5-furandicarboxylate (BHEF).
  • FDCA 2,5-furandicarboxylic acid
  • MHEF monohydroxyethyl 2,5-furandicarboxylate
  • BHEF bishydroxyethyl 2,5-furandicarboxylate
  • a means is provided for decomposing and recycling polyethylene furanoate with low energy compared to thermal recycling technology.
  • the base sequence of SEQ ID NO: 2 is a base sequence encoding the amino acid sequence of LCC, and is a base sequence in which codons have been optimized for expression in Escherichia coli.
  • a method for decomposing polyethylene furanoate (or a plastic containing it as a constituent resin) using cutinase is provided.
  • Cutinase is known to have the ability to decompose polyethylene terephthalate.
  • the cutinase used in the invention disclosed herein is not limited as long as it can decompose polyethylene furanoate.
  • the decomposition ability for polyethylene furanoate can be measured by the method described in the Examples below.
  • Decomposition products include 2,5-furandicarboxylic acid (FDCA), monohydroxyethyl 2,5-furandicarboxylate (MHEF), and bishydroxyethyl 2,5-furandicarboxylate (BHEF).
  • the cutinase has an amino acid sequence that has a certain level of identity to the amino acid sequence of SEQ ID NO: 1.
  • a certain level or higher is, for example, 60% or higher, 70% or higher, 80% or higher, 90% or higher, 91% or higher, 92% or higher, 93% or higher, 94% or higher, 95% or higher, 96% or higher, 97% or higher, 98% or higher, or 99% or higher.
  • the identity of amino acid sequences can be evaluated by any means known in the art. For example, it can be calculated using an analysis tool that is commercially available or available via telecommunication lines (Internet). As an example, the identity of amino acid sequences can be calculated using the National Center for Biotechnology Information (NCBI) homology algorithm BLAST (Basic local alignment search tool) http://www.ncbi.nlm.nih.gov/BLAST/ with default (initial settings) parameters.
  • NCBI National Center for Biotechnology Information
  • the type of the amino acid substitution is not particularly limited, but is preferably a conservative amino acid substitution.
  • conservative substitutions include, but are not limited to, substitutions between basic amino acids (H, K, R), substitutions between acidic amino acids (D, E), substitutions between neutral nonpolar amino acids (A, V, L, I, P, F, M, W), substitutions between neutral polar amino acids (G, N, Q, S, T, V, C), substitutions between aromatic amino acids (W, F, H, Y), substitutions between nitrogen-containing amino acids (K, R, N, Q, P), substitutions between sulfur-containing amino acids (C, M), substitutions between oxygen-containing amino acids (S, T), substitutions between ⁇ -branched amino acids (V, L, I), and substitutions between amino acids with linear alkyl or hydrogen side chains (A, G).
  • the cutinase may have any amino acid sequence at the C-terminus and/or N-terminus of an amino acid sequence having a certain level of identity to SEQ ID NO: 1, so long as the cutinase retains its activity of decomposing polyethylene furanoate.
  • the any amino acid sequence may be, for example, 30 amino acid residues or less, 25 amino acid residues or less, 20 amino acid residues or less, 15 amino acid residues or less, 10 amino acid residues or less, or 5 amino acid residues or less.
  • the cutinase may have a tag sequence (e.g., a His tag) at its C-terminus.
  • Cutinase can be obtained by any method.
  • cutinase can be prepared by genetic engineering methods. Specifically, cutinase can be prepared by transforming a suitable host cell (e.g., Escherichia coli or yeast) with DNA encoding cutinase and recovering the protein expressed in the transformant (or the protein secreted outside the transformant). The recovered protein is appropriately purified as necessary.
  • a suitable host cell e.g., Escherichia coli or yeast
  • An example of DNA encoding cutinase is DNA having a certain level of identity to the base sequence of SEQ ID NO: 2.
  • a certain level of identity is, for example, 60% or more, 70% or more, 80% or more, 90% or more, 91% or more, 92% or more, 93% or more, 94% or more, 95% or more, 96% or more, 97% or more, 98% or more, or 99% or more.
  • Cutinase can also be produced using general protein chemical synthesis methods (e.g., liquid phase and solid phase methods) based on the information of the amino acid sequence shown in SEQ ID NO:1. Cutinase can also be obtained according to the method described in Patent Document 1.
  • the polyethylene furanoate By allowing cutinase to act on polyethylene furanoate, the polyethylene furanoate can be decomposed. Therefore, by allowing cutinase to act on plastics that contain polyethylene furanoate as a constituent material, the plastics can be decomposed. Allowing cutinase to act on polyethylene furanoate or plastics can be achieved, for example, by bringing cutinase into contact with polyethylene furanoate or plastics.
  • the mode of acting cutinase on polyethylene furanoate (or plastic) is not particularly limited, and can be carried out, for example, by adding cutinase and polyethylene furanoate to a suitable solvent (e.g., buffer solution) and appropriately stirring, etc.
  • a suitable solvent e.g., buffer solution
  • the buffer solution is not particularly limited, and examples thereof include bicine, glycine, MES, Bis-Tris, Tris, ADA, PIPES, ACES, MOPSO, BES, MOPS, TES, HEPES, DIPSO, TAPSO, POPSO, HEPPSO, EPPS, Tricine, and Na 2 HPO 4 buffer solutions, and is preferably bicine or glycine buffer solution.
  • acting cutinase on polyethylene furanoate can also be carried out by adding cutinase to polyethylene furanoate (or plastic), or adding cutinase to a decomposition target buried in the ground.
  • the reaction conditions when cutinase acts on polyethylene furanoate (or plastic) are not particularly limited and can be set appropriately depending on the purpose.
  • the reaction temperature can be set, for example, in the range of 10°C to 90°C.
  • the reaction temperature is preferably 50°C or higher, 55°C or higher, 60°C or higher, 65°C or higher, 70°C or higher, 75°C or higher, or 80°C or higher, and preferably 90°C or lower, 85°C or lower, or 80°C or lower. These lower and upper limits of temperature can be combined arbitrarily.
  • the reaction temperature high (for example, 50°C or higher, 55°C or higher, 60°C or higher, 65°C or higher, 70°C or higher, or 75°C or higher)
  • the substrate specificity of cutinase for polyethylene furanoate for example, compared to the reactivity for polyethylene terephthalate
  • the pH during the reaction can be set appropriately, for example, in the range of 4 to 12. In one embodiment, the pH during the reaction can be set to 5 or more, 6 or more, 7 or more, or 8 or more, and can be set to 11 or less, or 10 or less. These lower and upper limits of the pH can be appropriately combined to form a range.
  • the reaction time can be set appropriately depending on the purpose.
  • the reaction time can be set in the range of 1 hour or more to 1 week or less.
  • the reaction time can be 2 hours or more, 3 hours or more, 4 hours or more, 5 hours or more, 6 hours or more, 7 hours or more, 8 hours or more, 9 hours or more, 10 hours or more, 11 hours or more, 12 hours or more, 24 hours or more, 36 hours or more, 48 hours or more, 3 days or more, 4 days or more, 5 days or more, or 6 days or more, and can be 7 days or less, 6 days or less, 5 days or less, 4 days or less, or 3 days or less.
  • the lower and upper limits of these reaction times can be appropriately combined to form a range.
  • the substrate specificity of cutinase for polyethylene furanoate can be increased by combining a long reaction time (e.g., 3 hours or more, 4 hours or more, 5 hours or more, 6 hours or more, 7 hours or more, 8 hours or more, 9 hours or more, 10 hours or more, 11 hours or more, 12 hours or more, or 24 hours or more) with a high reaction temperature.
  • a long reaction time e.g., 3 hours or more, 4 hours or more, 5 hours or more, 6 hours or more, 7 hours or more, 8 hours or more, 9 hours or more, 10 hours or more, 11 hours or more, 12 hours or more, or 24 hours or more
  • the concentration or amount of cutinase during the reaction can be set appropriately depending on the purpose.
  • the concentration of cutinase in the solvent can be set appropriately in the range of 10 nM to 5000 nM.
  • the concentration of cutinase during the reaction in the solvent is preferably 50 nM to 200 nM, 75 nM to 150 nM, or 80 nM to 130 nM from the viewpoint of exerting high substrate specificity for polyethylene furanoate.
  • the plastic to be decomposed by cutinase preferably contains other resins in addition to polyethylene furanoate.
  • the other resins are not particularly limited, but may be, for example, resins composed of one or more polymers selected from the group consisting of polyethylene terephthalate (PET), poly- ⁇ -caprolactone (PCL), poly-L-lactic acid (PLA), polybutylene succinate (PBS), polyethylene succinate (PES), polyethylene adipate (PEA), and polybutylene succinate-adipate polymer (PBSA).
  • the other resins preferably contain at least polyethylene terephthalate.
  • the plastic containing polyethylene furanoate is preferably a used plastic.
  • the polyethylene furanoate is decomposed into 2,5-furandicarboxylic acid (FDCA), monohydroxyethyl 2,5-furandicarboxylate (MHEF), and/or bishydroxyethyl 2,5-furandicarboxylate (BHEF).
  • FDCA 2,5-furandicarboxylic acid
  • MHEF monohydroxyethyl 2,5-furandicarboxylate
  • BHEF bishydroxyethyl 2,5-furandicarboxylate
  • the produced 2,5-furandicarboxylic acid (FDCA), monohydroxyethyl 2,5-furandicarboxylate (MHEF), and/or bishydroxyethyl 2,5-furandicarboxylate (BHEF) can be used for any purpose, for example, as a raw material when reproducing polyethylene furanoate.
  • the resuspension was sonicated on ice, centrifuged (15,000 ⁇ g, 20 min, 4° C.), and the supernatant was collected and applied to a His-Accept nickel column (Nacalai Tesque). After washing off unbound proteins with the above-mentioned dissolution buffer, the proteins bound to the column were eluted with an elution buffer (50 mM Tris-HCl (pH 7.5), 300 mM NaCl, 250 mM imidazole), and the buffer was exchanged with a PD-10 gel filtration column (GE Healthcare, Piscataway, NJ) into a 50 mM Na 2 HPO 4 -HCl (pH 7.0), 100 mM NaCl solution. The concentration of the purified enzyme was determined based on the molar extinction coefficient at 280 nm.
  • HPLC conditions were as follows: Equipment: LC-2010A HT (Shimadzu Corporation) Column: Cosmosil 5C18-AR-II guard column, Cosmosil 5C18-AR-II column (Nacalai Tesque) Mobile phase: Methanol/20 mM NaH2PO4 - H3PO4 (pH 2.5 ) Flow rate: 1.0 mL/min Detection wavelength: 240 nm Elution conditions: 0-15 min; 25% (v/v) methanol, 15-25 min; methanol concentration gradient changed from 25 to 100%

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Microbiology (AREA)
  • Biotechnology (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Biomedical Technology (AREA)
  • Molecular Biology (AREA)
  • Medicinal Chemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Mycology (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Separation, Recovery Or Treatment Of Waste Materials Containing Plastics (AREA)

Abstract

L'invention concerne un moyen de décomposition sélective de flanoate de polyéthylène.　L'invention concerne un procédé de décomposition d'un plastique, le procédé consistant à amener une cutinase à agir sur le plastique à une température supérieure ou égale à 60 °C, le plastique contenant du flanoate de polyéthylène, et la cutinase ayant une séquence d'acides aminés ayant 90 % ou plus d'identité avec la séquence d'acides aminés de SEQ ID NO : 1.
PCT/JP2024/011218 2023-03-31 2024-03-22 Décomposition enzymatique de pef Pending WO2024203813A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
JP2023057838 2023-03-31
JP2023-057838 2023-03-31

Publications (1)

Publication Number Publication Date
WO2024203813A1 true WO2024203813A1 (fr) 2024-10-03

Family

ID=92906272

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/JP2024/011218 Pending WO2024203813A1 (fr) 2023-03-31 2024-03-22 Décomposition enzymatique de pef

Country Status (2)

Country Link
TW (1) TW202449172A (fr)
WO (1) WO2024203813A1 (fr)

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2012099018A1 (fr) * 2011-01-19 2012-07-26 天野エンザイム株式会社 Nouvelle estérase dérivée d'un compost de feuilles
JP2019520833A (ja) * 2016-07-12 2019-07-25 キャルビオスＣａｒｂｉｏｓ 新規エステラーゼ及びその使用

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2012099018A1 (fr) * 2011-01-19 2012-07-26 天野エンザイム株式会社 Nouvelle estérase dérivée d'un compost de feuilles
JP2019520833A (ja) * 2016-07-12 2019-07-25 キャルビオスＣａｒｂｉｏｓ 新規エステラーゼ及びその使用

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
JOSHI ANUP S., ALIPOURASIABI NILOOFAR, VINNAKOTA KEERTHI, COLEMAN MARIA R., LAWRENCE JOSEPH G.: "Improved polymerization and depolymerization kinetics of poly(ethylene terephthalate) by co-polymerization with 2,5-furandicarboxylic acid", RSC ADVANCES, ROYAL SOCIETY OF CHEMISTRY, GB, vol. 11, no. 38, 5 July 2021 (2021-07-05), GB , pages 23506 - 23518, XP093216997, ISSN: 2046-2069, DOI: 10.1039/D1RA04359E *
WEINBERGER SIMONE, CANADELL JUDIT, QUARTINELLO FELICE, YENIAD BAHAR, ARIAS ANDREA, PELLIS ALESSANDRO, GUEBITZ GEORG: "Enzymatic Degradation of Poly(ethylene 2,5-furanoate) Powders and Amorphous Films", CATALYSTS, M D P I AG, CH, vol. 7, no. 11, CH , pages 318, XP093216995, ISSN: 2073-4344, DOI: 10.3390/catal7110318 *
YANG CUI, MA ZHONG‐SEN, ZHI HE‐WEN, LI HAO, HU YE‐MIN, ZHANG YA‐JIE: "Dissolution and initial esterification kinetics of 2,5‐furandicarboxylic acid in ethylene glycol without a catalyst", JOURNAL OF POLYMER SCIENCE, vol. 61, no. 3, 1 February 2023 (2023-02-01), pages 251 - 261, XP093217014, ISSN: 2642-4150, DOI: 10.1002/pol.20220420 *

Also Published As

Publication number Publication date
TW202449172A (zh) 2024-12-16

Similar Documents

Publication Publication Date Title
JP7520925B2 (ja) 新規エステラーゼ及びその使用
CN109642221B (zh) 新酯酶及其用途
Banki et al. Novel and economical purification of recombinant proteins: intein‐mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association
US10385183B2 (en) Process of recycling mixed PET plastic articles
CN120098957A (zh) 新酯酶及其用途
KR20210042122A (ko) 신규한 에스테라아제 및 이의 용도
Woroch et al. A semicrystalline furanic polyamide made from renewable feedstocks
Soong et al. Enzyme selection, optimization, and production toward biodegradation of post‐consumer poly (ethylene terephthalate) at scale
WO2024203813A1 (fr) Décomposition enzymatique de pef
US20240209331A1 (en) Ideonella sakaiensis pet-hydrolase variant with increased thermostability
Wu et al. Boosting extracellular FastPETase production in E. coli: A combined approach of cognate chaperones co-expression and vesicle nucleating peptide tag fusion
WO2025206322A1 (fr) Dégradation enzymatique de pef
WO2025206321A1 (fr) Dégradation enzymatique de pef
Tsuchiya et al. Chemoenzymatic Polymerization/Depolymerization of Semiaromatic Polyamides for Chemical Recycling
Junger et al. Biosynthesis of an Elastin‐Mimetic Polypeptide with Two Different Chemical Functional Groups within the Repetitive Elastin Fragment
WO2025047523A1 (fr) Estérase, produit de décomposition de polyester, procédé de traitement de polyester et procédé de production de polyester
KR102672773B1 (ko) 신규 비스-2-히드록시에틸테레프탈레이트 가수분해효소 및 이를 활용한 모노히드록시에틸테레프탈레이트의 생산방법
WO2024210848A1 (fr) Polypeptides microbiens et leurs utilisations
KR102877359B1 (ko) 열 안정성이 증가된 PETase 변이체 및 이의 용도
CN121175416A (en) Esterase variants and their use in polyester degradation
CN121086079A (zh) 一种融合蛋白及其在生产和粗纯化重组蛋白中的应用
KR20210042336A (ko) 신규한 에스테라아제 및 이의 용도

Legal Events

Date Code Title Description
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 24779932

Country of ref document: EP

Kind code of ref document: A1

WWE Wipo information: entry into national phase

Ref document number: 2025510698

Country of ref document: JP

NENP Non-entry into the national phase

Ref country code: DE