JP2005527193A - Bacillussp(DSM14392)由来の新規なアルカリ性プロテアーゼならびに該新規なアルカリ性プロテアーゼを含有する洗浄および浄化製品 - Google Patents
Bacillussp(DSM14392)由来の新規なアルカリ性プロテアーゼならびに該新規なアルカリ性プロテアーゼを含有する洗浄および浄化製品 Download PDFInfo
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- 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
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- CXVGEDCSTKKODG-UHFFFAOYSA-N sulisobenzone Chemical compound C1=C(S(O)(=O)=O)C(OC)=CC(O)=C1C(=O)C1=CC=CC=C1 CXVGEDCSTKKODG-UHFFFAOYSA-N 0.000 description 1
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- JSPLKZUTYZBBKA-UHFFFAOYSA-N trioxidane Chemical group OOO JSPLKZUTYZBBKA-UHFFFAOYSA-N 0.000 description 1
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- XOOUIPVCVHRTMJ-UHFFFAOYSA-L zinc stearate Chemical compound [Zn+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O XOOUIPVCVHRTMJ-UHFFFAOYSA-L 0.000 description 1
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)
- 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
- C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
Abstract
Description
・特定のアミノ酸残基をプロリンで置換する(WO92/19729、それぞれEP583339およびUS5858757、ならびにEP516200による);
・より高極性の基またはより高電荷の基を分子表面に導入する(EP525610、EP995801およびUS5453372による);
・金属イオンの結合を、特にカルシウム結合部位の突然変異誘発によって増強する(例えば、国際特許出願WO88/08028およびWO88/08033の教示による);
・修飾または突然変異誘発によって自己分解をブロックする(例えば、WO98/20116またはUS5543302による);
・複数の安定化戦略を組合せる(欧州特許出願EP398539A1に開示);
・US5340735、US5500364、US5985639およびUS6136553によれば、安定化に関連する位置を、3次元構造の分析によって見い出すことができる。
このための基礎が、特定の応用分野を標的としたさらなる開発が可能な新規なプロテアーゼによって広がる。
それぞれの場合に、Bacillus sp.(DSM 14392)由来の新規なアルカリ性プロテアーゼとの同一性の程度が増大しているものほど、好ましさが増大する。
「プロタンパク質」は、タンパク質の不活性前駆体である。シグナル配列を含む前者の前駆体は、「プレプロタンパク質」と称される。
このような酵素を、本願の実施例に記載のように、Bacillus sp.(DSM 14392)由来のアルカリ性プロテアーゼの形態で見い出すことができた。
同定される一致に基づいて、および他の示したスブチリシンとの関係に基づいて、このアルカリ性プロテアーゼは、スブチリシンとみなすべきである。
これらの中で、順に増大して好ましいのは、そのアミノ酸配列が、少なくともそれぞれの場合に、配列番号2に示されるアミノ酸配列に98.2%、98.3%、98.4%、98.5%、98.6%、98.7%、98.8%、98.9%、99%、99.1%、99.2%、99.3%、99.4%、99.5%、99.6%、99.7%、99.8%、99.9%および100%同一であるものである。
これは、これらの特性が、B.sp.(DSM 14392)由来のアルカリ性プロテアーゼの特性に、この順に増大して類似していると予測されるためである。
これらの中で、順に増大して好ましいのは、そのアミノ酸配列が、少なくともそれぞれの場合に、配列番号2に示されるアミノ酸配列に106〜375位において99%、99.1%、99.2%、99.3%、99.4%、99.5%、99.6%、99.7%、99.8%、99.9%および100%同一であるものである。
これは、このようなプロテアーゼが、本願により利用可能になったBacillus sp.(DSM 14392)由来の新規に見い出されたアルカリ性プロテアーゼを構成するためである。
図1の整列から推論することができるように、B.sp.(DSM 14392)由来のプロテアーゼは、洗浄または浄化製品における使用がこれまで記載されていないBacillus Ya-B由来のアルカリ性エラスターゼとは3つの位置において異なっている:即ち、1位(配列番号1におけるような本発明のプロテアーゼのアミノ酸番号付与に従う)において、それはMを有し;65位においてQの代わりにHを有し;182位においてTの代わりにSを有する。即ち、特に好ましいのは、B.sp.(DSM 14392)由来のプロテアーゼに対応する1またはそれ以上のアミノ酸位置を有する、上記した保護の範囲内にあるプロテアーゼである。
これらは、順に増大して好ましくはそれぞれの場合に、配列番号2に示した相同配列に少なくともそれぞれ98.9%、99%、99.1%、99.2%、99.3%、99.4%、99.5%、99.6%、99.7%、99.8%、99.9%および100%同一である、フラグメント化または欠失突然変異誘発によって導かれるタンパク質またはフラグメントである。
誘導体とは、上記したタンパク質からさらなる修飾によって導かれるタンパク質を意味する。このような修飾は、例えば、安定性、基質特異性もしくは基質への結合強さまたは酵素活性に影響を及ぼすことができる。また、このような修飾を用いて、タンパク質のアレルゲン性および/または免疫原性を低下させ、こうして例えば皮膚との適合性を増大させることができる。
・特定のアミノ酸残基をプロリンで置換する(EP583339に従う);
・より高極性またはより高電荷の基を分子の表面に導入する(EP995801に従う);
・金属イオンの結合、特にカルシウム結合部位を改変する(例えば、国際特許出願WO88/08028およびWO88/08033の教示に従う)。
・US5453372によれば、変性剤(例えば界面活性剤)の作用に対して表面における特定の突然変異によって、タンパク質を保護することができる。
さらなる同等の可能性は、US5340735、US5500364、US5985639およびUS6136553に示されている。
これは、これらが外側膜を持たず、従って分泌されたタンパク質を直接的に周囲培地に放出するためである。
バシラス属のグラム陽性細菌からのものが極めて特に好ましい。
これは、本発明の酵素の態様がそれから最初に得られたためである。その関連配列は配列表に示され、その酵素特性は実施例に記載されている。これからまたは関連の菌株から、特に分子生物学的標準法(例えば、自体既知のPCR法および/または点突然変異誘発法など)を適用することによって、上記の変異体を調製することができる。
核酸は、実質的に全ての分子生物学的研究およびタンパク質の開発およびその製造のための出発点である[特に、遺伝子の配列決定および対応するアミノ酸配列の誘導、あらゆる種類の突然変異誘発(上記を参照)およびタンパク質の発現を含む]。
これは、これらの核酸が、B.sp.(DSM 14392)由来のアルカリ性プロテアーゼの特性に、この順に増大して類似している特性を有するタンパク質をコードしていると予測されるためである。
上記した好ましい形態をコードしている核酸、特に突然変異誘発によって得られる核酸が、対応して好ましい。
・天然供給源、特に微生物から得られることを特徴とする核酸;
・これらの中で、微生物がグラム陽性細菌であることを特徴とする核酸;
・これらの中で、グラム陽性細菌がバシラス属の細菌であることを特徴とする核酸;および
・これらの中で、バシラス属の種がBacillus sp.、特にBacillus sp.(DSM 14392)であることを特徴とする核酸。
クローニングベクターは、所望の遺伝子の貯蔵、生物学的増幅または選択に加えて、その分子生物学的な特性化に適している。同時に、これらは、特許請求されている核酸の輸送可能および貯蔵可能な形態であり、また、細胞に関係しない分子生物学的技術(例えば、PCRまたはインビトロ突然変異誘発法など)の出発点である。
この種の発現ベクターは、生物学的な製造系において対応する核酸を働かせ、これによって、対応するタンパク質を製造するための基礎となるものである。本発明のこの対象の好ましい態様は、発現に必要な遺伝子エレメント、例えば該遺伝子の上流に元から位置する天然プロモーターまたは別の生物からのプロモーターを担持する発現ベクターである。該エレメントを、例えば、「発現カセット」の形態で配置することができる。別の可能性は、調節エレメントのいずれかまたは全部を、それぞれの場合に宿主細胞から得ることである。これら発現ベクターを、特に好ましくは、さらなる特性、例えば選択した発現系(特に宿主細胞)に対する最適コピー数などに関連して適合させる(後記を参照)。
即ち、上記した本発明のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体を、上記した本発明の核酸を用いて、および/または上記した本発明のベクターを用いて、および/または上記した本発明の細胞のいずれかを用いて製造するためのあらゆる方法が特許請求されている。
これらには、例えば化学的合成法が含まれ、これは、特に比較的短いフラグメントのために経済的に有用である。
で示されるポリヒドロキシ脂肪酸アミドである。
このポリヒドロキシ脂肪酸アミドは、アンモニア、アルキルアミンまたはアルカノールアミンを用いた還元糖の還元的アミノ化、およびその後の、脂肪酸、脂肪酸アルキルエステルまたは脂肪酸塩化物を用いたアシル化によって通常得られる既知の物質である。
で示される化合物を包含する。
即ち、上記した本発明のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体に加えて、さらなる酵素によっても特徴付けられる洗浄または浄化製品が本発明の好ましい態様である。これらには、特に、他のプロテアーゼ、アミラーゼ、セルラーゼ、ヘミセルラーゼ、例えばβ-グルカナーゼ、オキシドレダクターゼ、例えばラッカーゼ、クチナーゼ、および/またはリパーゼだけでなく、エステラーゼおよびこの使用分野に対して先行技術に記載されている他の全ての酵素が含まれる。
上記した濃度範囲は、この使用に好ましく当てはまる。
即ち、上記した本発明のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体を含有する化粧品、あるいは、上記した本発明のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体を組み込んだ化粧方法、あるいは、上記した本発明のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の、化粧目的のための、特に対応する方法の枠内での、または対応する製品における使用が特許請求されている。
土壌試料(0.1g)を、滅菌0.9%濃度NaCl溶液(1ml)に懸濁させ、ミルク粉末を含有する寒天プレート[1.5%寒天、0.5%NaCl、0.1%K2HPO4、0.1%酵母エキス、2%ペプトン(ICN、Eschwede、Cat.No.104808)、1%ミルク粉末(スキムミルク;Difco、Heidelberg、Cat.No.232100)、pH10]上にプレーティングした。30℃で72時間インキュベートした後、透明ゾーンを有するコロニーが、ミルク寒天において明らかであった。単一コロニーをこれから取り、エルレンマイヤーフラスコ中、Horikoshi培地[0.1%K2HPO4、0.5%酵母エキス、1%ペプトン、0.02%MgSO4、0.3%Na2CO3、pH9]において、37℃で200rpmにて振盪しながら培養した。
Bacillus sp.(DSM 14392)由来の染色体DNAを、標準法によって調製し、制限酵素Sau3Aで処理し、得られたフラグメントをベクターpAWA22中にクローン化した。これは、バシラス種において使用するためのpBC16から導いた発現ベクターである[Bernhardら(1978)、J.Bacteriol.、Vol.133(2)、p.897-903]。このベクターを、プロテアーゼ陰性の宿主菌株 Bacillus subtilis DB 104 [KawamuraおよびDoi (1984)、J.Bacteriol.、Vol.160 (1)、p.442-444]に導入した。
Horikoshi培地(上記を参照)(100ml)を、500mlのエルレンマイヤーフラスコに入れ、実施例2におけるように形質転換したバシラス菌株の1つのコロニーを接種し、増殖の定常期に到達するまで37℃で72時間培養した。
この培養物の上清から以下の精製工程によって単一のタンパク質分解酵素を単離することができた:20mM HEPES/NaOH緩衝液(pH7.6)に対する上清の透析;Q-SepharoseR(Pharmacia-Amersham Biotech、スウェーデン国)における負アニオン交換クロマトグラフィー;HEPES/NaOHの勾配緩衝液(0〜1M NaCl、pH7.6)で溶離するS-SepharoseR(Pharmacia-Amersham)における通過物のカチオン交換クロマトグラフィー。プロテアーゼは、0.2M NaClで溶出し、次いでこれを、溶離液としてHEPES/NaOH(pH7.6)を用いるResource SR(Pharmacia-Amersham)におけるカチオン交換クロマトグラフィーによって濃縮した。
SDSゲル電気泳動およびクーマッシー染色によれば純粋であるタンパク質を、このようにして得た。
実施例2および3におけるようにして得たB.sp.(DSM 14392)由来のアルカリ性プロテアーゼは、PHASTR系(Pharmacia-Amersham Biotech、スウェーデン国から供給)における変性SDSポリアクリルアミドゲル電気泳動において、26kDの分子量を示す。
同様にPHASTR系(Pharmacia-Amersham Biotechから供給)における等電点電気泳動によれば、B.sp.(DSM 14392)由来のアルカリ性プロテアーゼの等電点は11である。
比活性
実施例2および3におけるようにして精製したB.sp.(DSM 14392)由来のアルカリ性プロテアーゼの比活性を、基質 Suc-Ala-Ala-Pro-Phe-p-ニトロアニリド(AAPF;Bachem Biochemica GmbH、Heidelbergから)を用いて測定した。それは、pH8.6および25℃で5分間インキュベートしたときに、9U/mgの活性を示した。この場合、1Uは、1μモルの切断された基質/分に等しい。
Eidgenoessische Material-Pruefungs- und -Versuchsanstalt(St.Gallen、スイス国;EMPA)あるいはWaeschereiforschungsanstalt(Krefeld、独国)から入手し、標準化された方法で汚した織物を、この実施例に使用した。以下の汚れおよび織物を使用した:A(血液/ミルク/すす;綿)、B(血液/ミルク/インク;綿)、C(血液/ミルク/インク;ポリエステル-綿ブレンド)、D(血液;綿)。
この試験材料を用い、洗濯計(launderometer)を用いて、種々の洗浄製品配合物の洗浄性能を試験した。この目的のために、液比をそれぞれ1:12に設定し、洗浄を40℃の温度で30分間行った。用量は、1Lの洗浄液あたり、5.88gの特定の製品であった。水硬度は、16°ドイツ硬度であった。
これらのデータは、B.sp.(DSM 14392)由来の本発明のプロテアーゼが、試験した全ての汚れに対して、確立されたプロテアーゼであるB.lentusアルカリ性プロテアーゼF49およびSavinaseRよりも明らかに良好な性能を呈するか、または少なくともそれらに近づくことを示す。
硬く滑らかな表面を有する容器を、標準化した方法で、混合デンプン(E)およびミルク(F)と接触させ、市販の家庭用食器洗浄機により洗浄した。試料Eは、MieleR G 676型の食器洗浄機の通常プログラムを用いて45℃で洗浄し、試料Fは、BoschR SGS 4002型の食器洗浄機の通常プログラムを用いて55℃で洗浄した。20gの食器洗浄剤を、それぞれ1回の食器洗浄試行あたりに使用した。水硬度は、16°ドイツ硬度であった。
これらの結果は、本発明のBacillus sp.(DSM 14392)プロテアーゼの性能が、機械食器洗浄剤において、試験した他のプロテアーゼの性能と少なくとも同等であり、これが、比較的低い活性を使用したときであってもそうであることを示す。
実施例7におけるように、容器を、標準化した方法により、半熟卵(G)、卵/ミルク(H)およびミルク(I)で汚し、それぞれ同じ浄化製品配合物を用いて、同じ方法で洗浄した。試料GおよびHは、BoschR SGS 4002型の食器洗浄機の通常プログラムを用いて55℃で洗浄し、試料Iは、MieleR G676型の食器洗浄機の通常プログラムを用いて45℃で洗浄した。実施例7との唯一の相違は、それぞれの場合に、20000PEの各プロテアーゼを使用したことである。これは、それぞれの場合に、浄化製品濃厚物において約0.2mgのプロテアーゼに相当した。
機械食器洗浄製品のために確立されたプロテアーゼであるB.lentusアルカリ性プロテアーゼF49およびProperaseRと比較して、関連製品の全体の浄化性能に対する本発明のプロテアーゼの、より高いかまたは少なくとも同等の寄与が、使用したプロテアーゼ活性が比較的高いときにも明らかである。
図1は、Bacillus sp.(DSM 14392)由来の本発明のプロテアーゼと、表2にまとめた最も類似する最も重要な既知のスブチリシン(それぞれ、成熟形態、即ちプロセシングされた形態にある)とのアミノ酸配列の整列図である。
以下の数字は、以下のプロテアーゼを意味する(カッコ内は、それぞれデータベース受入のIDである;実施例2の表2をも参照):
Claims (51)
- 配列番号2に示されるアミノ酸配列に少なくとも98.1%同一であるアミノ酸配列を有するスブチリシン型のアルカリ性プロテアーゼ。
- 配列番号2に示されるアミノ酸配列に少なくとも99%同一であるアミノ酸配列を有するスブチリシン型のアルカリ性プロテアーゼ。
- 配列番号2に示されるアミノ酸配列に、106〜375位において、少なくとも98.9%同一であるアミノ酸配列を有するスブチリシン型のアルカリ性プロテアーゼ。
- 配列番号2に示されるアミノ酸配列に、106〜375位において、少なくとも99.3%同一であるアミノ酸配列を有するスブチリシン型のアルカリ性プロテアーゼ。
- 配列番号1に示されるヌクレオチド配列に、特に配列番号2中の106〜375位に対応する部分領域にわたり、少なくとも98.1%同一であるヌクレオチド配列から導かれるスブチリシン型のアルカリ性プロテアーゼ。
- 配列番号1に示されるヌクレオチド配列に、特に配列番号2中の106〜375位に対応する部分領域にわたり、少なくとも99%同一であるヌクレオチド配列から導かれるスブチリシン型のアルカリ性プロテアーゼ。
- 配列番号2に示されるアミノ酸配列の全体と、好ましくは106〜375位において、同一であるアミノ酸配列、および/または、配列番号1に示されるヌクレオチド配列から導かれるアミノ酸配列の全体と、好ましくは配列番号2中の106〜375位において、同一であるアミノ酸配列を有するスブチリシン型のアルカリ性プロテアーゼ。
- 請求項1〜7のいずれかに記載のスブチリシン型のアルカリ性プロテアーゼからフラグメント化または欠失突然変異誘発によって導かれ、出発分子において既に結合した少なくとも120個、好ましくは少なくとも150個、特に好ましくは少なくとも200個のアミノ酸を有するか、あるいは、配列番号1のアミノ酸番号付与に従って1位、65位および/または182位を含む出発分子において既に結合した少なくとも40個、好ましくは少なくとも100個、特に好ましくは少なくとも150個のアミノ酸を有するタンパク質またはフラグメント。
- 請求項1〜8のいずれかに記載のスブチリシン型のアルカリ性プロテアーゼあるいは誘導タンパク質またはフラグメントから、挿入突然変異誘発によって、置換突然変異誘発によって、および/または少なくとも1つの他のタンパク質またはタンパク質フラグメントとの融合によって導かれたタンパク質。
- それ自体がタンパク質を加水分解しうることを特徴とする、請求項1〜9のいずれかに記載のタンパク質、タンパク質フラグメントまたは融合タンパク質。
- さらに誘導体化されていることを特徴とする、請求項1〜10のいずれかに記載のタンパク質、タンパク質フラグメントまたは融合タンパク質。
- さらに安定化されていることを特徴とする、請求項1〜11のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体。
- 請求項1〜12のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体のいずれかと共通する少なくとも1つの抗原決定基を有することを特徴とする、タンパク質、タンパク質フラグメント、融合タンパク質または誘導体。
- 天然供給源、特に微生物から得られることを特徴とする、請求項1〜13のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体。
- 微生物がグラム陽性細菌であることを特徴とする、請求項14に記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体。
- グラム陽性細菌がバシラス属のいずれかであることを特徴とする、請求項15に記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体。
- バシラスの種がBacillus sp.、特にBacillus sp.(DSM 14392)であることを特徴とする、請求項16に記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体。
- スブチリシン型のアルカリ性プロテアーゼをコードしている核酸であって、そのヌクレオチド配列が、配列番号1に示されるヌクレオチド配列に、特に316〜1125位の部分領域にわたり、少なくとも98.1%同一である核酸。
- スブチリシン型のアルカリ性プロテアーゼをコードしている核酸であって、そのヌクレオチド配列が、配列番号1に示されるヌクレオチド配列に、特に316〜1125位の部分領域にわたり、少なくとも99%同一である核酸。
- スブチリシン型のアルカリ性プロテアーゼをコードしている核酸であって、そのヌクレオチド配列が、配列番号1に示されるヌクレオチド配列に、特に316〜1125位の部分領域にわたり、同一である核酸。
- 請求項1〜14のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体のいずれかをコードしている核酸。
- 天然供給源、特に微生物から得られることを特徴とする、請求項18〜21のいずれかに記載の核酸。
- 微生物がグラム陽性細菌であることを特徴とする、請求項22に記載の核酸。
- グラム陽性細菌がバシラス属のいずれかであることを特徴とする、請求項23に記載の核酸。
- バシラスの種がBacillus sp.、特にBacillus sp.(DSM 14392)であることを特徴とする、請求項24に記載の核酸。
- 請求項18〜25のいずれかに記載の核酸領域、特に、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体のいずれかをコードしている核酸を含んでなるベクター。
- 請求項26に記載のクローニングベクター。
- 請求項26に記載の発現ベクター。
- 請求項18〜25のいずれかに記載の核酸領域、特に、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体のいずれかをコードしている核酸を、好ましくは請求項26〜28のいずれかに記載のベクター上に含んでなる細胞。
- 請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体のいずれかを、特に請求項18〜25のいずれかに記載の核酸領域を用いることにより、さらに具体的には請求項28に記載の発現ベクターを用いることにより、発現するかまたは発現するように誘導しうる宿主細胞。
- 細菌、特に産生したタンパク質を周囲培地に分泌する細菌であることを特徴とする、請求項30に記載の宿主細胞。
- グラム陽性細菌、特にバシラス属の細菌、さらに具体的にはBacillus lentus種、Bacillus licheniformis種、Bacillus amyloliquefaciens種、Bacillus subtilis種またはBacillus alcalophilus種の細菌であることを特徴とする、請求項31に記載の細菌。
- 真核細胞、特に産生したタンパク質を翻訳後修飾する真核細胞であることを特徴とする、請求項29または30に記載の細胞。
- 請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体のいずれかを、請求項18〜25のいずれかに記載の核酸を用いて、および/または請求項26〜28のいずれかに記載のベクターを用いて、および/または請求項29〜33のいずれかに記載の細胞を用いて製造する方法。
- 請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体を含有することを特徴とする製品。
- 請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体を含有することを特徴とする洗浄または浄化製品。
- タンパク質、タンパク質フラグメント、融合タンパク質または誘導体を、製品1gあたり、2μg〜160mg、好ましくは5μg〜140mg、特に好ましくは20μg〜120mg、なお特に好ましくは50μg〜80mgの量で含有することを特徴とする請求項36に記載の製品。
- さらなる酵素、特に他のプロテアーゼ、アミラーゼ、セルラーゼ、ヘミセルラーゼ、オキシドレダクターゼおよび/またはリパーゼをさらに含有することを特徴とする請求項36または37に記載の製品。
- 請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体を、単独でまたは他の活性成分に加えて含有することを特徴とする、織物原料の処理のためまたは織物ケアのための製品、特に天然成分を含有する繊維または織物のため、さらに具体的には羊毛または絹を含有する繊維または織物のための製品。
- 織物または硬表面を機械浄化するための方法であって、その行程の少なくとも1つにおいて、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体が、好ましくは1回の適用あたり、40μg〜32g、好ましくは50μg〜24g、特に好ましくは100μg〜16g、なお特に好ましくは200μg〜8gの量で活性になることを特徴とする方法。
- 織物原料の処理のためまたは織物ケアのための方法であって、その行程の少なくとも1つにおいて、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体が、特に天然成分を含有する織物原料、繊維または織物のために、さらに具体的には羊毛または絹を含有する織物原料、繊維または織物のために活性になることを特徴とする方法。
- 特に1回の適用あたり40μg〜32g、好ましくは50μg〜24g、特に好ましくは100μg〜16g、なお特に好ましくは200μg〜8gの量で織物または硬表面を浄化するための、請求項1〜17のいずれかに記載のタンパク質分解活性なタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の使用。
- 洗浄または浄化製品の成分を活性化または不活性化するための、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の使用。
- 低分子量化合物またはタンパク質を合成するためまたは生化学的に分析するための、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の使用。
- 天然物質または生物学的有用物質を調製、精製または合成するための、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の使用。
- 天然原料の処理のため、特に表面の処理のため、さらに具体的には皮革の処理のための方法における、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の使用。
- 織物製造における原料または中間体の取得または処理のため、特に生地から保護層を除去するための、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の使用。
- 織物原料の処理のためまたは織物ケアのため、特に羊毛または絹あるいは羊毛または絹を含有する織物ブレンドの処理のための、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の使用。
- 写真フィルムの処理のため、特にゼラチン含有層または同様の保護層を除去するための、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の使用。
- 食品または動物飼料を調製するための、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の使用。
- 請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体を含有する化粧品、あるいは、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体を組み込んだ化粧方法、あるいは、請求項1〜17のいずれかに記載のタンパク質、タンパク質フラグメント、融合タンパク質または誘導体の、化粧目的のための、特に対応する方法の枠内での、または対応する製品における使用。
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DE10163884A DE10163884A1 (de) | 2001-12-22 | 2001-12-22 | Neue Alkalische Protease aus Bacillus sp. (DSM 14392) und Wasch- und Reinigungsmittel enthaltend diese neue Alkalische Protease |
PCT/EP2002/014132 WO2003055974A2 (de) | 2001-12-22 | 2002-12-12 | Neue alkalische protease aus bacillus sp. (dsm 14392) und wasch- und reinigungsmittel enthaltend diese neue alkalische protease |
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ES (1) | ES2381539T3 (ja) |
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- 2002-12-12 WO PCT/EP2002/014132 patent/WO2003055974A2/de active Application Filing
- 2002-12-12 CN CN02825897.5A patent/CN1608129B/zh not_active Expired - Fee Related
- 2002-12-12 ES ES02796618T patent/ES2381539T3/es not_active Expired - Lifetime
- 2002-12-12 AU AU2002361402A patent/AU2002361402A1/en not_active Abandoned
- 2002-12-12 HU HU0500286A patent/HU228735B1/hu not_active IP Right Cessation
- 2002-12-12 JP JP2003556495A patent/JP4495967B2/ja not_active Expired - Fee Related
- 2002-12-12 DK DK02796618.3T patent/DK1456368T3/da active
- 2002-12-12 EP EP02796618A patent/EP1456368B1/de not_active Expired - Lifetime
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2004
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JP2012516930A (ja) * | 2009-02-05 | 2012-07-26 | アメリカン ステリライザー カンパニー | 低臭の硬表面殺芽胞剤および化学除染剤 |
JP2015228859A (ja) * | 2014-06-06 | 2015-12-21 | 森永乳業株式会社 | 食肉改質用処理液、及び該食肉改質用処理液を用いた加工肉又は食肉加工品の製造方法、並びに加工肉又は食肉加工品 |
Also Published As
Publication number | Publication date |
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EP1456368B1 (de) | 2012-02-01 |
HUP0500286A3 (en) | 2010-03-29 |
DE10163884A1 (de) | 2003-07-10 |
HU228735B1 (en) | 2013-05-28 |
ATE543903T1 (de) | 2012-02-15 |
JP4495967B2 (ja) | 2010-07-07 |
AU2002361402A1 (en) | 2003-07-15 |
CN1608129A (zh) | 2005-04-20 |
CN1608129B (zh) | 2010-06-16 |
AU2002361402A8 (en) | 2003-07-15 |
WO2003055974A2 (de) | 2003-07-10 |
US20050043198A1 (en) | 2005-02-24 |
HUP0500286A2 (hu) | 2005-06-28 |
US7569226B2 (en) | 2009-08-04 |
EP1456368A2 (de) | 2004-09-15 |
HK1071766A1 (en) | 2005-07-29 |
DK1456368T3 (da) | 2012-05-21 |
WO2003055974A3 (de) | 2004-03-11 |
ES2381539T3 (es) | 2012-05-29 |
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