JP6204018B2 - プロテアーゼ変異体の使用 - Google Patents
プロテアーゼ変異体の使用 Download PDFInfo
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- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
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- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
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Description
・タンパク分解活性(proteolytic activity):この用語は、本明細書において、タンパク分解によりタンパク質を分解する(break down)能力をいう。ここでタンパク分解(proteolysis)とは、タンパク質を形成するポリペプチド鎖内のアミノ酸を連結するペプチド結合を加水分解することにより、タンパク質を代謝することをいう。すなわち、タンパク分解活性を有するプロテアーゼによって、タンパク質はアミノ酸に分解される。用語「プロテアーゼ活性」(protease activity)及び「タンパク分解活性」は相互交換可能に用いられる。以下の「プロテアーゼ」の定義も参照。
(同一残基数 × 100)/(アラインメント長 − アラインメント中のギャップ総数)
(同一デオキシリボヌクレオチド数 × 100)/(アラインメント長 − アラインメント中のギャップ総数)
タンパク質基質中のアミド結合を開裂する酵素は、プロテアーゼに、或いは(ほぼ同義である)ペプチターゼ(peptitases)に分類される(Walsh, 1979, Enzymatic Reaction Mechanisms. W. H. Freeman and Company, San Francisco, Chapter 3参照)。
別途記載がない限り、本明細書で使用するアミノ酸の番号付けは、サブチラーゼBPN’(BASBPN)配列の番号に従う。BPN’配列の更なる説明は、配列番号2又は Siezen et al., Protein Engng. 4 (1991) 719-737 を参照のこと。
セリンプロテアーゼはペプチド結合の加水分解を触媒する酵素であり、その活性部位には重要なセリン残基が存在する(White, Handler and Smith, 1973 "Principles of Biochemistry," Fifth Edition, McGraw-Hill Book Company, NY, pp.271-272)。
セリンプロテアーゼのサブグループである仮称サブチラーゼは、Siezen et al., Protein Engng. 4 (1991) 719-737 及び Siezen et al., Protein Science 6 (1997) 501-523 により提案された。サブチラーゼは、従前はサブチリシン様プロテアーゼと呼ばれていたセリンプロテアーゼの170超のアミノ酸配列のホモロジー分析により定義された。サブチリシンは従前、グラム陽性細菌又は真菌により産生されるセリンプロテアーゼとして定義される場合が多かったが、Siezen et al. によれば、現在はサブチラーゼのサブグループとされている。様々なサブチラーゼが同定され、また、数々のサブチラーゼのアミノ酸配列が決定されてきた。サブチラーゼ及びそのアミノ酸配列のより詳しい解説については、Siezen et al. (1997) を参照のこと。
サビナーゼ(登録商標)は、NOVOZYMES A/Sが販売するB.レンタス(B. Lentus)由来のサブチリシン309であり、BAALKPとの差異は一箇所のみ(N87S)である。サビナーゼ(登録商標)のアミノ酸配列を配列番号1に示す。
「親サブチラーゼ」(parent subtilaze)という語は、Siezen et al. により定義されるサブチラーゼをいう(1991及び1997)。更なる詳細については、上記「サブチラーゼ」の欄を参照のこと。親サブチラーゼは、天然物から単離されたサブチラーゼに対して、サブチラーゼの特性を保持しつつ修飾を加えたものであってもよい。更には、例えばJ.E. Ness et al., Nature Biotechnology, 17, 893-896 (1999) 等に記載のDNAシャフリング(DNA shuffling)法により調製されたサブチラーゼであってもよい。
本明細書において「修飾」(modification(s))とは、サブチラーゼの化学修飾に加えて、サブチラーゼをコードするDNAの遺伝子操作をも含むものとして定義される。1又は2以上の修飾としては、1又は2以上のアミノ酸側鎖の1又は2以上の置換、1又は2以上の所望のアミノ酸における1又は2以上の置換、欠失及び/又は挿入が挙げられる。
「変異体」という語及び「サブチラーゼ変異体」という語は上述の通りである。
本明細書において、2つのアミノ酸配列間のホモロジーは、「同一性」というパラメーターにより記載される。本発明の目的においては、2つのアミノ酸配列間の同一性の程度は、上述の Needleman-Wunsch アルゴリズムを用いて決定される。上記ルーチンにより、アミノ酸アラインメントに加えて、2つの配列間の「%同一性」が出力される。
本発明者等は意外にも、特定の位置に置換を含む変異体が、特にタンパク質性の汚れ、例えば卵汚れに対し、改善された性能を示すことを見出した。
本発明の目的においては、配列番号2に記載のBPN’のアミノ酸配列を用いて、別のプロテアーゼ又はプロテアーゼ変異体の対応するアミノ酸残基を決定する。別のプロテアーゼ又はプロテアーゼ変異体のアミノ酸配列を、配列番号2に開示のプロテアーゼのアミノ酸配列とアラインし、このアラインメントに基づいて、配列番号2に開示のプロテアーゼ変異体のアミノ酸配列における任意のアミノ酸残基に対応するアミノ酸位置の番号を決定することができる。
置換 アミノ酸置換については、以下の命名法を使用する:原アミノ酸、位置、置換アミノ酸。従って、位置226におけるスレオニンのアラニンによる置換は、「Thr226Ala」又は「T226A」と表す。多重突然変異については、例えば加算記号(「+」)により区切って表記する。例えば「Gly205Arg+Ser411Phe」又は「G205R+S411F」は、位置205のグリシン(G)をアルギニン(R)に置換し、位置411のセリン(S)のフェニルアラニン(F)に置換する突然変異を表す。或いは、多重突然変異をスペースで区切り、例えばG205R S411Fのように表記し、又はカンマ(,)で区切り、例えばG205R,S411Fのように表記してもよい。
親プロテアーゼの変異体は、当業界で周知の任意の突然変異誘発法、例えば部位特異的突然変異誘発法、合成遺伝子構築法、半合成遺伝子構築法、ランダム突然変異誘発法、シャッフリング等を用いて調製可能である。
一側面によれば、本発明は、親サブチリシンに対する置換9R、15T、68A、245R及び218{D,G,V}を含む(前記位置は配列番号2の成熟ポリペプチド[BPN’]の位置に相当する)サブチリシン変異体の、硬表面清浄における使用に関する。
27、36、56、87、95、96、100、102、103、104、123、159、167、170、206、222、224、232、235、236、245、248、252及び274。
K27R、*36D、S56P、S87N、S103A、V104A、V104I、V104N、V104Y、S106A、N123S、G159D、Y167A、R170S、R170L、N204D、V205I、Q206E、L217D、M222S、M222A、T224S、A232V、K235L、Q236H、N248D、N252K及びT274A。
本発明は、本発明のプロテアーゼ変異体をコードするポリヌクレオチドと、これと作動式に連結された1又は2以上の調節配列とを含む核酸コンストラクトであって、適切な宿主細胞中において、調節配列に適合する条件下、前記調節配列により前記コーディング配列が発現されるような核酸コンストラクトにも関する。
本発明は、本発明の変異プロテアーゼ変異体をコードするポリヌクレオチドと、プロモーターと、転写及び翻訳停止シグナルとを含む組換え発現ベクターにも関する。上述の種々のヌクレオチド及び調節配列を組み合わせ、1又は2以上(数個)の制限部位を含む組換え発現ベクターを構築すれば、前記変異体をコードするポリヌクレオチドを斯かる部位に挿入又は置換することができ、好適である。或いは、前記ポリヌクレオチド又はポリヌクレオチドを含む核酸コンストラクトを、発現に適したベクターに挿入することにより、ポリヌクレオチドを発現させてもよい。発現ベクターを作製する際には、発現に適した調節配列とコーディング配列とが作動式に連結されるように、コーディング配列をベクター内に配置する。
本発明は、変異プロテアーゼ変異体をコードするポリヌクレオチドを含み、当該変異体の組換え産生に有利に使用される組換え宿主細胞にも関する。本発明のポリヌクレオチドを含むベクターを宿主細胞に導入し、ベクターが上述の染色体組み込み体として、或いは自己複製染色体外ベクターとして維持されるようにする。宿主細胞の選択は、ポリペプチドをコードする遺伝子及びその起源に大きく依存する。
本発明は、本発明に係る単離酵素を製造する方法を提供する。この手法によれば、酵素をコードするDNA配列で形質転換された適切な宿主細胞を、酵素の産生を可能とする条件下で培養し、得られた酵素を培養物から回収する。
本発明の酵素を洗剤組成物に添加してもよい。すなわち、本発明の酵素を洗剤組成物の構成要素としてもよい。清浄及び洗剤組成物については当業界では概して詳しく報告されているとおりであるが、適切な清浄及び洗剤組成物の更なる説明については、国際公開第96/34946号;国際公開第97/07202号;国際公開第95/30011号を参照のこと。
プロテアーゼ変異体活性の決定方法
標準的なメラミンタイルはCenter For Testmaterials BV, P.O. Box 120, 3133 KT Vlaardingen(オランダ)から入手される。特にタイプDM-21(卵黄)。
バシラス・レンタス(Bacillus lentus)株309はNCIBに寄託され、受託番号NCIB10309を受けているもので、米国特許第3,723,250号に記載されている。本公報は引用により本明細書に組み込まれる。親サブチラーゼ309又はサビナーゼ(登録商標)は、株309から取得される。発現宿主生物はバシラス・サブチリス(Bacillus subtilis)である。
別途記載しない限り、DNA操作及び形質転換は、分子生物学の標準的な手法を用いて行う(Sambrook et al. (1989) Molecular cloning:A laboratory manual, Cold Spring Harbor lab., Cold Spring Harbor, NY;Ausubel, F. M. et al. (eds.) "Current protocols in Molecular Biology". John Wiley and Sons, 1995; Harwood, C. R., and Cutting, S. M. (eds.) "Molecular Biological Methods for Bacillus". John Wiley and Sons, 1990)。
別途記載しない限り、DNA操作のための酵素(例えば制限エンドヌクレアーゼ、リガーゼ等)は全て、New England Biolabs, Inc. から入手する。DNA操作用の酵素は、サプライヤーの説明書に従って使用する。
サブチラーゼ酵素の産生のための醗酵は、50ml試験管内に15mlの二重TY培地(double TY media)を入れて、pH7.3、37℃で、回転振盪台を用いて225rpmで2〜3日かけて行う。
宿主細胞から分泌されるサブチラーゼ変異体は、周知の手法により培地から好適に回収できる。例としては、遠心分離又は濾過により細胞を培地から分離し、又は、例えば硫酸アンモニウム等の塩を用いて培地中のタンパク質成分を沈殿させた後、イオン交換クロマトグラフィーやアフィニティークロマトグラフィー等のクロマトグラフィー法にかける手法が挙げられる。
本発明の変異体の触媒活性は、例えば以下の「Kinetic Suc AAPF-pNA」アッセイを用いて決定することができる。
pNA基質:Suc-AAPF-pNA(Bachem L-1400)。
温度:室温。
アッセイ緩衝剤:50mM Tris/HCl、1mM CaCl2、pH9.0。
選択されたサブチラーゼ変異体の洗剤組成物中における洗浄性能を調べるには、洗浄実験を実施する。本発明の酵素変異体は自動機械負荷アッセイ(Automated Machine Stress Assay:AMSA)で試験する。AMSA試験により、少量の酵素洗剤溶液の洗浄性能を、多数調べることが可能になる。詳細は実施例3を参照のこと。
本発明のサブチラーゼ酵素の洗浄性能試験のための洗剤は、完成品である市販の洗剤を市場で購入し、熱処理(水溶液中85℃で5分間)によって酵素成分を不活性化することにより、得ることができる。また、酵素を含まない市販の洗剤基材を製造者から直接購入することも可能である。更には、本明細書の記載に従い、適切なモデル洗剤を調製し、洗浄性能試験に使用してもよい。
酵素変異体の構築及び発現:
本発明の変異体は、当業者に周知の手法で構築し、発現させることが可能である。下記は本発明に係る変異体の作製法の例である。
特定の挿入/欠失/置換を含む本発明のサブチリシン309(サビナーゼ(登録商標))の位置特異的変異体は、所望の突然変異を含むオリゴを用いたPCRで作製したDNA断片を従来法でクローニングすることにより作製される(Sambrook et al., Molecular Cloning:A Laboratory Manual, 2nd Ed., Cold Spring Harbor, 1989)。
変異原性プライマー(オリゴヌクレオチド)は、突然変異部位の側位に存在し、挿入/欠失/置換を定義するDNA塩基対により分離されるDNA配列に対応するように合成する。
酵素の精製及び濃度測定:
醗酵後、サブチリシン変異体の精製は、疎水性電荷誘導クロマトグラフィー(Hydrophobic Charge Induction Chromatography:HCIC)及びそれに続く真空濾過により行う。
本発明の変異体の硬表面に対する洗浄性能をAMSAで評価した。方法及び結果を以下に示す。
AMSA試験法の説明:
食器洗い用洗剤組成物、即ちMGDA添加ADWモデル洗剤及びSTPP添加ADWモデル洗剤中における、選択されたプロテアーゼ変異体の洗浄性能を評価するために洗浄実験を実施する。自動機械負荷分析(Automated Mechanical Stress Assay:AMSA)を用いて本発明のプロテアーゼを試験する。AMSAによれば、少量ずつ多数の酵素洗剤溶液の洗浄性能を調べることができる。AMSAプレートは、試験溶液用の多数のスロットと、食器洗いサンプル、即ち洗浄対象のメラミンタイルを、スロットの全開口部に対して硬く締め付けるリッドとを有する。洗浄期間の間、プレート、試験溶液、メラミンタイル及びリッドを烈しく振盪し、試験溶液を汚れたメラミンタイルに接触させると共に、定期的且つ周期的な振動による機械的応力を印加する。更なる説明については、国際公開第02/42740号、特に23〜24頁の「Special Method Examples」のパラグラフを参照のこと。
本発明の更なる変異体についても、硬表面に対する洗浄性能を、AMSAにより、上述と同様の条件下で評価した。
Claims (12)
- 卵の汚れを除去するための、硬表面清浄におけるサブチリシン変異体の使用であって、変異体が親サブチリシンに対する置換9R、15T、68A、245R及び218Dを含み、前記位置は配列番号2の成熟ポリペプチド[BPN’]の位置に相当する、使用。
- 変異体が更に、修飾G61{D,E}、N62{D,E}、N76{D,E};*97aG、A98{G,S}、S99G、S101G、H120{N,V,Q,D}、P131{T,S}、Q137H、A194P、A228V、A230V及びN261Dのうち少なくとも1つを含む、請求項1に記載の使用。
- 変異体が置換S9R、A15T、V68A、N218D及びQ245Rを含む、請求項1又は2に記載の使用。
- 変異体が更に置換G61Eを含む、請求項3に記載の使用。
- 変異体が更に置換A98Sを含む、請求項3又は4に記載の使用。
- 変異体が更に置換S99Gを含む、請求項3〜5の何れか一項に記載の使用。
- 変異体が置換S9R、A15T、G61E、V68A、A98S、S99G、N218D及びQ245Rを含む、請求項1〜6の何れか一項に記載の使用。
- 親サブチリシンがサブグループI−S2に属する、請求項1〜7の何れか一項に記載の使用。
- 親サブチリシンが、配列番号1に対して少なくとも80%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る、請求項1〜8の何れか一項に記載の使用。
- 変異体が、配列番号3に対して少なくとも80%の同一性を有するポリペプチド配列を有する、請求項1に記載の使用。
- 変異体が、配列番号4に対して少なくとも80%の同一性を有するポリペプチド配列を有する、請求項1に記載の使用。
- 変異体が親サブチリシンと比較して改善された1又は2以上の特性を有し、
改善された特性が、硬表面洗浄における改善された洗浄性能を含む、請求項1〜11の何れか一項に記載の使用。
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2010
- 2010-09-24 JP JP2012530277A patent/JP6204018B2/ja active Active
- 2010-09-24 BR BR112012006497A patent/BR112012006497A2/pt not_active Application Discontinuation
- 2010-09-24 CA CA2775048A patent/CA2775048A1/en not_active Abandoned
- 2010-09-24 EP EP10757601.9A patent/EP2480663B1/en not_active Not-in-force
- 2010-09-24 US US13/496,249 patent/US20120252106A1/en not_active Abandoned
- 2010-09-24 CN CN201080053391.3A patent/CN102648277B/zh active Active
- 2010-09-24 MX MX2012003387A patent/MX2012003387A/es active IP Right Grant
- 2010-09-24 AU AU2010299800A patent/AU2010299800B2/en not_active Ceased
- 2010-09-24 CN CN201510204996.2A patent/CN104946427A/zh active Pending
- 2010-09-24 WO PCT/EP2010/064174 patent/WO2011036264A1/en active Application Filing
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Also Published As
Publication number | Publication date |
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CN104946427A (zh) | 2015-09-30 |
RU2012116537A (ru) | 2013-10-27 |
AU2010299800A1 (en) | 2012-04-05 |
BR112012006497A2 (pt) | 2015-09-08 |
MX2012003387A (es) | 2012-04-10 |
RU2639534C2 (ru) | 2017-12-21 |
CA2775048A1 (en) | 2011-03-31 |
US20120252106A1 (en) | 2012-10-04 |
AU2010299800B2 (en) | 2014-08-07 |
EP2480663B1 (en) | 2017-11-15 |
CN102648277B (zh) | 2015-05-20 |
EP2480663A1 (en) | 2012-08-01 |
CN102648277A (zh) | 2012-08-22 |
JP2013506022A (ja) | 2013-02-21 |
WO2011036264A1 (en) | 2011-03-31 |
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