JP2018500003A - ポリエステル分解活性を有するポリペプチド及びその使用 - Google Patents
ポリエステル分解活性を有するポリペプチド及びその使用 Download PDFInfo
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- JP2018500003A JP2018500003A JP2017521492A JP2017521492A JP2018500003A JP 2018500003 A JP2018500003 A JP 2018500003A JP 2017521492 A JP2017521492 A JP 2017521492A JP 2017521492 A JP2017521492 A JP 2017521492A JP 2018500003 A JP2018500003 A JP 2018500003A
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- 238000010298 pulverizing process Methods 0.000 description 1
- 150000003212 purines Chemical class 0.000 description 1
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- 238000010188 recombinant method Methods 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 108020004418 ribosomal RNA Proteins 0.000 description 1
- 238000001175 rotational moulding Methods 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
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- 239000000377 silicon dioxide Substances 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 235000010378 sodium ascorbate Nutrition 0.000 description 1
- PPASLZSBLFJQEF-RKJRWTFHSA-M sodium ascorbate Substances [Na+].OC[C@@H](O)[C@H]1OC(=O)C(O)=C1[O-] PPASLZSBLFJQEF-RKJRWTFHSA-M 0.000 description 1
- 229960005055 sodium ascorbate Drugs 0.000 description 1
- WXMKPNITSTVMEF-UHFFFAOYSA-M sodium benzoate Chemical compound [Na+].[O-]C(=O)C1=CC=CC=C1 WXMKPNITSTVMEF-UHFFFAOYSA-M 0.000 description 1
- 235000010234 sodium benzoate Nutrition 0.000 description 1
- 239000004299 sodium benzoate Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 229910001415 sodium ion Inorganic materials 0.000 description 1
- LROWVYNUWKVTCU-STWYSWDKSA-M sodium sorbate Chemical compound [Na+].C\C=C\C=C\C([O-])=O LROWVYNUWKVTCU-STWYSWDKSA-M 0.000 description 1
- 235000019250 sodium sorbate Nutrition 0.000 description 1
- PPASLZSBLFJQEF-RXSVEWSESA-M sodium-L-ascorbate Chemical compound [Na+].OC[C@H](O)[C@H]1OC(=O)C(O)=C1[O-] PPASLZSBLFJQEF-RXSVEWSESA-M 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 238000000638 solvent extraction Methods 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 235000010356 sorbitol Nutrition 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
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- 238000003860 storage Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 238000000352 supercritical drying Methods 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 229920002994 synthetic fiber Polymers 0.000 description 1
- 239000012209 synthetic fiber Substances 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- KKEYFWRCBNTPAC-UHFFFAOYSA-L terephthalate(2-) Chemical compound [O-]C(=O)C1=CC=C(C([O-])=O)C=C1 KKEYFWRCBNTPAC-UHFFFAOYSA-L 0.000 description 1
- 238000003856 thermoforming Methods 0.000 description 1
- 229920001187 thermosetting polymer Polymers 0.000 description 1
- 239000010936 titanium Substances 0.000 description 1
- 229910052719 titanium Inorganic materials 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000013060 ultrafiltration and diafiltration Methods 0.000 description 1
- 230000036967 uncompetitive effect Effects 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 238000005292 vacuum distillation Methods 0.000 description 1
- 238000007738 vacuum evaporation Methods 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 125000000391 vinyl group Chemical group [H]C([*])=C([H])[H] 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
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Abstract
Description
本発明は、酵素活性を有する新規ポリペプチド及びその使用に関する。本発明はまた、このようなポリペプチド、コード核酸分子、リコンビナント細胞を生産する方法、及びこのようなポリペプチドを使用してポリエステル含有材料を分解する方法に関する。本発明のポリペプチドは、ポリ乳酸、及びプラスチック材料としてポリ乳酸を含有する材料を分解するために特に適切である。
ポリエステルは、食品包装から衣料品、自動車産業などを介して医療分野に至る多数の技術分野において、特にプラスチック材料の形態で使用されている。一例として、特定のポリエステル(例えば、ポリエチレンテレフタラート−PET、ポリ乳酸−PLAなど)は、衣類及び包装の製造において使用されているが、自動車又は他の部品の製造のために熱硬化性樹脂の形態でも使用されている。
本発明は一般に、配列番号:1に示されているアミノ酸配列の少なくとも生物学的に活性な部分を含む単離されたポリペプチドであって、ポリエステル、より好ましくはポリ乳酸を解重合することができる単離されたポリペプチドに関する。好ましくは、20℃〜90℃、少なくとも20℃〜60℃の温度範囲で活性であるこのポリペプチドは、ポリエステルプラスチック材料を分解するために使用され得る。このポリペプチド又はそのコード核酸配列はまた、ポリエステル含有材料の分解を引き起こすために役立ち得るリコンビナント微生物を作製するために使用され得る。このようなリコンビナント微生物は、天然又はリコンビナントポリマー合成活性をさらに示し得るので、該微生物は、ポリエステル分解から生じるモノマー及び/又はオリゴマーを再利用することができる。
本開示は、以下の定義を参照することによって最も良く理解されるであろう。
本発明は、分子構造中にエステル結合を有するプラスチックを分解する能力を有する新たなポリペプチドを対象とする。より具体的には、本発明は、ポリエステラーゼ活性を示す新たに同定及び単離されたポリペプチドを開示する。最初、該ポリペプチドは、Actinomadura keratinilyticaの天然細菌株T16−1又はDSMZ 45195から単離された。興味深いことに、本発明のポリペプチドは、天然及び人工ポリエステル中のエステル結合を加水分解することができる。
本発明のさらなる目的は、上記で定義されるポリペプチドをコードする核酸である。
本発明は、ポリエステルから作製された若しくはポリエステルを含有するプラスチック製品のようなポリエステル含有材料を好気性若しくは嫌気性条件下で分解し、及び/又は該ポリエステル含有材料をリサイクルするために本発明のポリペプチドを使用する方法を提供する。実際、その高いポリエステル解重合効率により、本発明のポリペプチドは、他の公知の化学的又は微生物的ポリエステル分解手段と比較してかなり有利である。本発明のポリペプチドは、特にPLA解重合に関して増加した解重合速度を有する。
本発明のさらなる目的は、本発明のポリペプチド並びに/又は前記ポリペプチドを発現及び排出するリコンビナント微生物が含まれるポリエステル含有材料を提供することである。特定の実施態様では、このようなポリエステル含有材料は、プラスチック化合物であり得る。
タイの森林土壌から単離されたkeratinilytica NBRC 104111株T16-1 (Sukkum et al. 2009)を、その上清の高いPLA分解活性について選択した。
10L発酵槽(Sartorius(登録商標)Biostat Cplus)において、バッチ実験を実施した。Yeast Malt Broth (YM, Sigma-Aldrich)前培養液500mLを使用して、基礎培地(ゼラチン2.4g/L;(NH4)2SO44g/L;MgSO4.7H2O 0.2g/L;酵母抽出物0.5g/L;K2HPO44g/L;KH2PO42g/L、NaOHでpH6.8に調整)4.5Lに植菌した。温度を46℃にレギュレーションし、10%(v/v)H3PO4溶液を追加してpHを6.8に維持した。撹拌速度を70rpmに固定して穏やかな混合を可能にし、酸素制限を防ぐために、通気速度(0.6〜1.6vvm)をレギュレーションして、空気飽和の20%よりも高い溶存酸素レベルを反応器に与えた。発酵槽をコンピュータに接続し、MFCS/DAソフトウェアにより、コントロールパラメータ(pH、温度、溶存酸素の分圧及びH3PO4の追加)のオンライン取得を行ったので、これらのパラメータをオンラインでモニタリング及びレギュレーションすることができた。
Amicon Cell 500mL (Merck Millipore)及び孔径10KDaのセルロース再生膜(GE Healthcare Life Science)を使用して、培養上清を40倍濃縮した。得られた溶液を、50mMグリシン−NaOH pH10緩衝液に対して透析した。
所望のバンドに含まれるポリペプチドのN末端の配列決定を、ゲルからの受動的抽出後に、Rouen (France)のPissaroプラットフォームで494マイクロシーケンサー装置(Perkin Elmer Applied Biosystems)を使用してエドマンマイクロシークエンシング技術によって行った。
特に指定がない限り、DNA操作に使用した一般的な手順は、以前に記載されている(Sambrook J, Russell DW. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY)。制限酵素及びT4 DNAリガーゼは、New England Biolabsから入手し、製造業者の説明書にしたがって使用した。CloneAmp HiFi PCR Premix (Takara-Clontech)を使用して、PCRを実施した。合成オリゴヌクレオチドは、Eurogentecによって合成された。GenElute PCR Clean-Up Kit (Sigma-Aldrich)を使用して、PCR産物を精製した。熱ショック法を使用して、プラスミドDNAをEscherichia coli DH5α株(Invitrogen)に導入した。QIAprep spin plasmid miniprep kit (Qiagen)を使用して、E. coliからプラスミドDNAを得た。RNeasy(登録商標)Plus Mini Kit (Qiagen)を使用して全RNAサンプルを得、続いて、Ribo-Zero(商標)rRNA Removal Kit (Epicentre)を使用してリボソームRNAを枯渇させた。
PLLA(NaturePlast、500μm)の存在下/非存在下におけるA. keratinilytica T16-1の発現プロファイルに対応する2つのRNAライブラリーを、Ilumina TruSeq Stranded mRNA kit及びultra-high-throughput sequencing system Ilumina HiSeq 2500を使用して構築した。TruSeq SBS kit (Ilumina)のchemistry v3を使用して、ペアエンドリード(2×100ob)を得た。
TBLASTN、BLASTX及びBLASTP(Altschul SF et al. 1997. Gapped BLAST and PSI-BLAST: a new generation of polypeptide database search programs. Nucleic Acids Res. 25:3389-3402)を使用する、National Center for Biotechnology Informationのウェブサイト(http://www.ncbi.nlm.nih.gov)でアクセス可能な非冗長配列データベースを使用して、データベースの検索を実施した。Vector NTI software (Life Technologies)を使用して、配列分析を実施し、ClustalW software (Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids. Res. 22:4673-4680)を用いて、マルチプルローカルアライメントを行った。
ポリペプチドの精製
pH10で陰イオン交換カラムを使用して、ポリペプチドの精製を達成した。PLAを含有するアガロースプレート上で、異なる画分の活性を試験した。PLAの加水分解を示すハロの形成は、フロースルー画分でのみ得られた。β−メルカプトエタノールによるSDS−PAGEにより、フロースルー画分がユニークなバンドを含有することが実証された(図1)。この精製プロセスにより、PLA加水分解活性を示す純粋なポリペプチドを取得することができた。該ポリペプチドの分子量は、27kDaと評価された。
ATQNNPPSWGLDRIDQTNLPLSRSYTYN(配列番号:3)
−残基1〜29は、ペプチドシグナルに対応し、
−残基30〜110は、仮想プロペプチドに対応し、
−残基111〜386は、成熟ポリペプチドに対応する)。
配列番号:5(下線付のプロペプチド配列;二重下線付のペプチドシグナル):
成熟ポリペプチド配列(配列番号:1):
該酵素の最適pH及び温度を決定し、該酵素の熱安定性を研究した。
該酵素の最適pHは、8.5である。磁気撹拌した試験管における解重合試験を、酵素600μgを含む緩衝液2mL及びGoodfellow PLAフィルム20mgを用いて、50℃、pH7〜9の範囲内で実施した。pH7において、該酵素は、ほとんど活性を示さない。
ポリエステラーゼ安定性アッセイを、4℃〜60℃の温度範囲内で行った。ポリエステラーゼは、4℃で数カ月間安定である。該酵素の安定性と活性との間の折衷点は、45℃の温度に相当する。45℃において、該酵素の半減期は、2.5週間である。加えて、凍結乾燥手順後に、ポリエステル分解活性の喪失がない。
これらの実験の目的は、潜在的な阻害因子及び反応中のpHの劇的な低下の両方を考慮して、乳酸の生産に関する問題を解決することであった。酵素及びPLAを10kDa透析チューブに導入及び封入した。このチューブは乳酸に対して透過性であり、これを一定量の緩衝液に入れることにより、一定のpHで作用し、乳酸を希釈してその潜在的阻害効果を限定することができた。
目的のポリペプチド(配列番号:1)の分解能力を、PLAの加水分解速度で研究した。乳酸へのPLA変換後に、HPLC分析を行った。
PLA粉末(PLLA NaturePlast、4%D−乳酸を含有するPLA Ingeo 7001D)の加水分解中に、酵素活性を評価した。市販のペレットの微粉化及び粉砕によって、異なる粒径(100〜250μm、250〜500μm、500μm〜1mm及び1〜2mm)を得た(表1)。
実施例3に記載されているのと同じプロトコール、酵素90μgを含むトリス−HCl 100mM pH8.5緩衝液3mLを用いて、異なる濃度(33〜300g/L)のPLLA粉末の加水分解中に、酵素活性を評価した。結果を表2に示す。
PLAフィルム(Goodfellow、厚さ50μm、2%D−乳酸)の加水分解中に、実施例3に示されているのと同じ実験プロトコールを使用した。ポリエステラーゼ90μgを含むトリス−HCl 100mM pH8.5緩衝液3mL及びフィルム(17g/L)50mgを用いて、動態分析を45℃、pH8.5で行った。
ポリエステラーゼによって触媒される市販品(PLAカップ、トレイ、フィルム及びカトラリー)の加水分解中に、実施例3に示されているのと同じ実験プロトコールを使用した。これらの物品の粉末(250〜500μm)について、加水分解試験を実施した。市販品の粉末100mg、酵素90μgを含むトリス−HCl 100mM pH8.5緩衝液3mLを使用した。
これらの実験の目的は、いかなる透析システムも用いずに配列番号:1の酵素及びPLAを反応器に導入する本発明のPLA分解法の産業上の利用可能性を検証することであった。
配列番号:1のアミノ酸配列を、その熱安定性を改善するために改変した。
3つの異なる宿主:Yarrowia lipolytica、Bacillus subtilis及びE. coliにおいて、配列番号:1のポリエステラーゼを発現させた。
Bordes et al., 2007 (F. Bordes, F. Fudalej, V. Dossat, J.M. Nicaud, et A. Marty (2007) A new recombinant protein expression system for high-throughput screening in the yeast Yarrowia lipolytica. J. of Mibrob. Meth., 70, 3, 493-502)によって以前に記載されているように、構成的プロモーターTEFのコントロール下で、酵母Yarrowia lipolytica(より正確には、JMY1212株)において、配列番号:1のポリエステラーゼを発現させた。成熟ポリエステラーゼを発現する遺伝子の配列が後に続くプロペプチドに対応する配列を、Yarrowia lipolyticaのコドン使用頻度に最適化した。この配列を、Y. lipolytica由来のリパーゼlip2をコードする遺伝子の分泌シグナル配列の下流に組み込んだ。
市販のTakara kitに記載されているように、配列番号:1のポリエステラーゼをクローニングし、Bacillus subtilisにおいて発現させた。成熟ポリエステラーゼを発現する遺伝子の配列が後に続くプロペプチドに対応する配列を、Bacillus subtilisのコドン使用頻度に最適化した。この配列を、B. subtilisの分泌シグナル配列の下流に組み込んだ。
配列番号:1のポリエステラーゼをクローニングし、E. coli(より正確には、BL21、Origami及びRosetta株)において発現させた。成熟ポリエステラーゼを発現する遺伝子の配列が後に続くプロペプチドに対応する配列を、E. coliのコドン使用頻度に最適化した。この配列を、ペリプラズム発現のためのPelBシグナル配列の下流に、又はマルトース結合タンパク質をコードする遺伝子の下流にヒスチジンタグの有無にかかわらず組み込んだ。
11A−プラスチック化合物の生産プロセス
予め65℃で4時間乾燥した粒状形態のPLAポリマー(Natureplastのポリ乳酸PLE 003)と、配列番号:1のポリペプチドの固体製剤とを含むプラスチック化合物を調製する。
−コントロールとして参照される、100重量%のPLAを含有する(すなわち、PLAデポリメラーゼを欠く)、実施例11Aに記載されているように生産したPLA化合物
を使用して、生分解性の異なる比較試験を実施した。
Claims (21)
- 配列番号:1に示されている全長アミノ酸配列と少なくとも94%、95%、99%又は100%の同一性を有するアミノ酸配列を含む単離されたポリペプチドであって、ポリエステル分解活性を有する、単離されたポリペプチド。
- T175C、R247C、N139D、S170R、N143R、N173E、S194P、H197D、L210P、G212N、I217K、R166K、T160A、L138A又はそれらの組み合わせから選択される、配列番号:1の残基に対応する残基における少なくとも1個のアミノ酸置換を含む、請求項1に記載の単離されたポリペプチド。
- 20℃〜60℃、好ましくは30℃〜55℃、より好ましくは40℃〜50℃の温度の範囲内で、特により好ましくは45℃で、及び/又は5〜11のpHの範囲内で、好ましくは7〜10のpHの範囲内で、より好ましくは8.5〜9.5のpHの範囲内で活性である、請求項1又は2に記載の単離されたポリペプチド。
- ポリ乳酸(PLA)、好ましくはポリ(L−乳酸)(PLLA)を分解することができる、請求項1〜3のいずれか一項に記載の単離されたポリペプチド。
- 配列番号:1又は配列番号:5に示されているアミノ酸配列を含む、単離されたポリペプチド。
- 請求項1〜5のいずれか一項に記載のポリペプチドをコードする、核酸。
- 請求項6に記載の核酸を含む、発現カセット。
- 請求項6に記載の核酸又は請求項7に記載の発現カセットを含む、ベクター。
- 請求項6に記載のヌクレオチド酸、請求項7に記載の発現カセット又は請求項8に記載のベクターを含有する、リコンビナント細胞。
- 請求項1〜5のいずれか一項に記載のポリペプチドを生産する方法であって、(i)請求項9に記載のリコンビナント細胞を培養すること、(ii)培養上清を回収すること、及び場合により(iii)該ポリペプチドを単離又は精製することを含む、方法。
- 請求項1〜5のいずれか一項に記載のポリペプチド又は請求項9に記載のリコンビナント細胞若しくはその抽出物を含む組成物であって、場合により、少なくとも1つのさらなる酵素及び/若しくは微生物若しくはその抽出物並びに/又は添加剤をさらに含む、組成物。
- 液体溶液、固体又は凍結乾燥組成物から選択され、好ましくは凍結乾燥粉末である、請求項11に記載の組成物。
- ポリエステル含有材料、好ましくはPLA含有材料、特により好ましくはPLLA含有材料の酵素分解のための、請求項1〜5のいずれか一項に記載のポリペプチド、請求項9に記載のリコンビナント細胞若しくはその抽出物又は請求項11若しくは12に記載の組成物の使用。
- ポリエステル含有材料を分解するための方法であって、ポリエステル含有材料と、請求項1〜5のいずれか一項に記載のポリペプチド、請求項9に記載のリコンビナント細胞若しくはその抽出物又は請求項11若しくは12に記載の組成物とを接触させる、方法。
- ポリエステル含有材料の少なくとも1つのポリエステルをモノマー及び/又はオリゴマーに解重合し、場合により、該解重合から生じるモノマー及び/又はオリゴマーを回収するさらなる工程を含む、請求項14に記載の方法。
- ポリエステル含有材料を機械的及び/若しくは物理的並びに/又は化学的及び/又は生物学的に改変するポリエステル含有材料前処理工程を含む、請求項14又は15に記載の方法。
- ポリエステル含有材料がPLA、より好ましくはPLLAを含み、少なくとも乳酸モノマー及び/又はオリゴマーを回収する、請求項14〜16のいずれか一項に記載の方法。
- ポリエステル含有材料からモノマー及び/又はオリゴマーを生産する方法であって、ポリエステル含有材料を、請求項1〜5のいずれか一項に記載のポリペプチド、請求項9に記載のリコンビナント細胞若しくはその抽出物又は請求項11若しくは12に記載の組成物に曝露すること、並びに場合によりモノマー及び/又はオリゴマーを回収することを含む、方法。
- 少なくとも1つのポリエステルと、請求項1〜5のいずれか一項に記載のポリペプチド及び/又は請求項9に記載のリコンビナント細胞とを含む、ポリエステル含有材料。
- 請求項19に記載のポリエステル含有材料を調製するための方法であって、ポリエステルと、請求項1〜5のいずれか一項に記載のポリペプチド及び/又は請求項9に記載のリコンビナント微生物とを混合する工程を含み、該ポリエステルが部分的又は全体的に溶融状態にある温度で、好ましくは押出プロセス中に、該混合工程を実施する、方法。
- ポリエステル含有材料を分解するための、配列番号:1に示されている全長アミノ酸配列と少なくとも75%、80%、85%、90%、92%、95%、99%又は100%の同一性を有するアミノ酸配列を含むポリペプチドであって、ポリエステル分解活性を有するポリペプチドの使用。
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Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
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JP2021508455A (ja) * | 2017-12-21 | 2021-03-11 | キャルビオスCarbios | 新規プロテアーゼ及びその使用 |
JP7465391B2 (ja) | 2017-12-21 | 2024-04-10 | キャルビオス | 新規プロテアーゼ及びその使用 |
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PT3209771T (pt) | 2021-01-12 |
CN113667659A (zh) | 2021-11-19 |
EP3209771A1 (en) | 2017-08-30 |
ES2842236T3 (es) | 2021-07-13 |
TN2017000085A1 (en) | 2018-07-04 |
CN106852154B (zh) | 2021-07-30 |
EP3209771B1 (en) | 2020-10-14 |
MA40138B1 (fr) | 2018-09-28 |
DK3209771T3 (da) | 2021-01-11 |
US10287561B2 (en) | 2019-05-14 |
CN106852154A (zh) | 2017-06-13 |
EP3778883A1 (en) | 2021-02-17 |
WO2016062695A1 (en) | 2016-04-28 |
US20170313998A1 (en) | 2017-11-02 |
JP2020185010A (ja) | 2020-11-19 |
JP6804440B2 (ja) | 2020-12-23 |
MA40138A1 (fr) | 2018-03-30 |
PL3209771T3 (pl) | 2021-05-31 |
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