JP5912251B2 - 炭化水素産生遺伝子およびその使用方法 - Google Patents
炭化水素産生遺伝子およびその使用方法 Download PDFInfo
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Description
本特許出願は、引用により組み込んだ2007年5月22日出願の米国仮特許出願第60/931,370号、2007年5月25日出願の米国仮特許出願第60/931,939号、2007年7月25日出願の米国仮特許出願第60/951,944号、および2007年9月24日出願の米国仮特許出願第60/974,810号からの優先権を主張する。
本明細書と同時に提出され、2008年5月20日に作成された「702724_ST25.TXT」という名称の1,359,078バイトのASCII(テキスト)ファイルで特定されたコンピュータで読み取り可能なヌクレオチド/アミノ酸配列のリストは、全体が本明細書に引用により組み込まれる。
本発明は、OleA、OleB、OleCまたはOleDアミノ酸モチーフ配列を含むポリペプチドをコードする単離核酸を提供する。
本発明は、少なくとも部分的に、炭化水素の生合成に関与するタンパク質をコードするいくつかの遺伝子の発見に基づいている。本明細書で同定した1種または複数のタンパク質をコードする1種または複数の核酸配列で形質転換された生物は、オレフィンなどの炭化水素および脂肪族ケトンなどの炭化水素中間体の生成に使用することができる。「オレフィン」および「アルケン」という用語は本明細書では同義に使用される。本明細書で記載したように、これらの核酸配列は、炭化水素の生合成に関与する遺伝子として定義された。したがって、1種または複数のこれらの遺伝子で形質転換された細胞は、オレフィンおよびそれらの前駆体(例えば、脂肪族ケトン)を含む炭化水素の製造のための供給源として使用できる。この発見は、限界のある再生不可能な炭化水素資源(例えば、石油をベースにした燃料)の代わりに燃料として使用できる炭化水素供給源を提供する。さらに、特定の適用のために考案された広範な特定なオレフィンおよび脂肪族ケトン生成物を産生することが可能である。宿主生物および/または反応基質を制御することによって(例えば、鎖長、分枝、飽和および/または2重結合の位置を制御することによって)、特定の分枝および不飽和位置を有する炭化水素生成物を含む広範な炭化水素生成物を産生する生物を創出することができる。
1)R+ATP→R−OPO3−アデノシン+ピロリン酸
2)R−OPO3−アデノシン+CoASH→R−SCoA+AMP
δ13C(0/00)=[(13C/12C)試料−(13C/12C)標準物質]/(13C/12C)標準物質×1000
本実施例は、本特許の範囲内で実施例を実行する際に用いられる材料および方法を記載する。特定の方法を記載するが、当業者は他の同様の方法も用い得ることを理解するであろう。一般的に、他に明記しない限りは標準的な実験室業務(laboratory practice)を用いた。例えば、標準的な実験室業務を以下のために用いた: クローニング; 核酸の操作およびシークエンシング; タンパク質の精製および解析; ならびに他の分子生物学的および生化学的手法。かかる手法は、標準的な実験マニュアル、例えば前掲の Sambrook et al.; および前掲の Ausubel et al. において詳細に説明される。
微生物の菌株: 本発明において用いた微生物の菌株は、以下の通りであった:
S. maltophilia (ATCC 菌株番号: 17674、17679、17445、17666);
S. maltophilia ATCC 17679 ΔoleA
S. maltophilia ATCC 17679 ΔoleC
S. maltophilia ATCC 17679 ΔoleD
E. coli T7 Express lysY/Iq (New England Biolabs、Ipswich、MA 01938-2723)
E. coli C41(DE3) (Lucigen Corporation、Middleton、WI 53562)
E. coli C41(DE3) ΔfadE (Lucigen Corporation、Middleton の E. coli C41(DE3)株、fadE 遺伝子 EC 1.3.99.3、アシル-CoA デヒドロゲナーゼの欠失を有する WI 53562、Klein. K. et al.、Eur. J. Biochem. II I 19: 442-450 (1971))。
E. coli C41(DE3) ΔfadE; pET-21b(+)_OleA、pCOLADuet-1_OleC、pCDFDuet-1_OleD
E. coli C41(DE3); pET-21b(+)_OleA
E. coli C41(DE3); pET-21b(+)_OleB
E. coli C41(DE3); pET-21b(+)_OleD
E. coli C41(DE3); pETDuet-1_OleAB; pCOLADuet-1_OleCD
E. coli MG1655 ΔfadE (fadE 遺伝子の欠失を有する E. coli MG1655)
E. coli MG1655 ΔfadE、fadD(+) (fadE 遺伝子の欠失、および fadD の上流の T5 プロモーター配列を有する E. coli MG1655 株)
Saccharomyces cerevisiae Hansen、teleomorph BY4741 (ATCC 201388)
S. cerevisiae BY4741; pESC-HIS_OleA
Bacillus megaterium WH320 (Mo Bi Tec、Germany からの菌株)
B. megaterium WH320; pWH1520_OleCDAB
B. megaterium WH320; pWH1520
Bacillus subtilis IHA01 lacA::spec leuB8 metB5 r(-)m(+) Sp (Bacillus Genetic Stock Center、Columbus からの菌株、OH 菌株番号 BGSC 1A785)
B. subtilis IHA01、pHT01_OleA
Arthrobacter aurescens TC1 (ATCC BAA-1386 からの菌株)
抽出方法 1: 5 mL ペレット抽出
有機化合物(オレフィン、脂肪族ケトンおよび炭化水素)を、メタノール:ヘキサン抽出プロトコールを用いて細菌の細胞ペレットから抽出した。簡潔には、5 mL の培養物/発酵ブロス(broth)をガラス試験管において 3500 rpm で 15 分間遠心し(Allegra X-15R Centrifuge with rotor SX-4750A、Beckman Coulter、Fullerton、CA)、上清をデカントし、得られたペレットを 100 μL の滅菌蒸留水中に再懸濁し、ボルテックスミキサー上で均一になるまで混合した。次に、1 mL のメタノールを添加し、ボルテックスミキサーを用いてサンプルを混合した。次いで、サンプルを超音波ウォーターバス(Bransonic(登録商標)、Tabletop Ultrasonic Cleaners、model 5510、Danbury、CT)中で 15 分から 1.5 時間の間超音波処理した。超音波処理の後、4 mL のヘキサンを添加し、サンプルをボルテックスミキサー上で混合した。次いでサンプルを、3500 rpm で 15 分間遠心した(Allegra X-15R Centrifuge with rotor SX-4750A、Beckman Coulter、Fullerton、CA)。上層(ヘキサン層)を取り除き、清潔なガラスチューブに添加した。次いで、サンプルを、遠心機(Vacufuge 5301、Eppendorf、Westbury、NY)中において減圧下でおよそ 30 分間、本質的に溶剤が存在しなくなるまで乾燥させた。次いでサンプルを 100 μL の酢酸エチルまたはクロロホルム中に再懸濁した。次に、1 μL のサンプルを以下に記載される検出方法にしたがって GC/MS 上で解析した。
インビトロアッセイのために、有機化合物(オレフィン、脂肪族ケトンおよび炭化水素)を、酢酸エチル/1% 酢酸抽出プロトコールを用いて、インビトロのサンプルから抽出した。インビトロアッセイのサンプルを、1% 酢酸を含有する酢酸エチルを 500 μL 添加することによって抽出した。サンプルをボルテックスミキサー上で混合し、その後、水層と有機層を分離するため 3500 rpm で 5 分間遠心した (ローター FA-45-24-11 を備える遠心機 5424、Eppendorf、Westbury、NY)。上層(酢酸エチル層)を、清潔なチューブに移した。次いでサンプルを、遠心機(Vacufuge 5301、Eppendorf、Westbury、NY)中において減圧下でおよそ 30 分間、本質的に溶剤が存在しなくなるまで乾燥させた。サンプルを 50 μL の酢酸エチル中に再懸濁し、GC/MS および/または GC/FID によって解析した。1 から 10 μL の間を、以下に記載される検出方法にしたがって GC/MS または GC/FID 上で炭化水素含有量について解析した。
0.5 から 1 mL の間の発酵培養物を、1.7 mL のエッペンドルフチューブに加えた。次いで、この培養物を、適切な炭化水素のスパイク(spike)(例えば 10 mg/L のシス-9-トリコセンまたはオレフィンのための 10 mg/L のヘキサコサン、脂肪族ケトンのための 10 mg/L の14-ヘプタコサノン等)を含有する 0.25 から 0.5 mL の間の酢酸エチルを用いて抽出した。培養物と酢酸エチルの混合物を、ボルテックスミキサー上で高速で 10 分間、混合した。次いで、サンプルをエッペンドルフ遠心機において 13,000 rpm で 5 分間遠心した (ローター FA-45-24-11 を備える遠心機 5424、Eppendorf、Westbury、NY)。有機層(上層)を、以下に記載される GC/MS または GC/FID 検出法を用いる解析のために取り除いた。
検出方法 1: 20 分 GC/MS
GC/MS 検出について、以下のプロトコールを用いて炭化水素および脂肪族ケトンを観察し、検証した:
実行時間: 20 分
カラム: HP-5-MS (5% ジフェニルシロキサン、95% ジメチルシロキサン) 部品番号 19091S-433E、長さ: (メートル) 30、内径: (mm) 0.25 ナローボア(narrowbore)、フィルム: (μM) 0.25
MSD スキャン範囲: 50 - 800 M/Z
注入: 1μL Agilent 6850 注入口
注入口: 300℃ スプリットレス
キャリアガス: ヘリウム
オーブン温度: 5 分保持 100℃; 25℃/分で 320℃まで; 5 分保持 320℃
検出: Agilent 5975B VL MSD
検出温度: 300℃
GC/MS 検出について、以下のプロトコールを用いて炭化水素および脂肪族ケトンを検出し、検証した:
実行時間: 4.9 分
カラム: HP-5-MS (5% ジフェニルシロキサン、95% ジメチルシロキサン) 部品番号 19091S-433E、長さ: (メートル) 30、内径: (mm) 0.25 ナローボア(narrowbore)、フィルム: (μM) 0.25
MSD スキャン範囲: 50 - 140 M/Z
注入: 1μL Agilent 6850 注入口
注入口: 300℃ スプリットレス
キャリアガス: ヘリウム
オーブン温度: 225℃で保持なし; 25℃/分で 320℃まで; 1.1 分保持 320℃
検出: Agilent 5975B VL MSD
検出温度: 300℃
GC/FID 検出について、以下のプロトコールを用いて炭化水素および脂肪族ケトンを検出し、検証した:
実行時間: 興味の対象である炭化水素の長さに応じて 2.75 から 4 分。より長い炭化水素にはより長い時間を用いる。
カラム: Thermo Electron Corporation: (部品番号 UFMC 002 000 000 00): Ph5、フィルム厚 0.4 mm、
長さ: (メートル) 5、
内径: 0.1 mm、
注入するサンプル容積: 実験に応じて 1 から 10 μl
注入口: スプリットレス
キャリアガス: ヘリウム
オーブン温度: 1 分保持 100℃; 200℃/分で 350℃まで; 0.50 分保持 350℃
検出: Thermo FID detector
GC/MS 検出について、以下のプロトコールを用いて炭化水素および脂肪族ケトンを観察し、検証した:
実行時間: 5.83 分
カラム: DB-1HT (100% ジメチルポリシロキサン) 部品番号 122-1111 (Agilent Technologies、Inc)、長さ: (メートル) 15、内径: (mm) 0.25 ナローボア(narrowbore)、フィルム: (μM) 0.1
MSD スキャン範囲: 50 - 550 m/z
注入: 1μL Agilent 6890 N 注入口
注入口: 300℃ スプリットレス
キャリアガス: ヘリウム (流速: 1.3 mL/分)
オーブン温度: 160℃で 0.3 分保持; 30℃/分で 320℃まで; 0.2 分保持 320℃
検出: Agilent 5975B XL EI/CI MSD
検出温度: 250℃
以下の4つの遺伝子を様々な順序で含有する複数のプラスミドを構築した: oleA、oleB、oleC および oleD。これらのオペロンからの遺伝子を発現する菌株を用いて試験したすべての発酵が、オレフィンを産生した。合成オペロン中の遺伝子の順序は、生物の炭化水素を生産する能力に影響を与えなかった。これらのプラスミドの多くは、以下に記載される実施例において互換的に用いることができる。各々の実施例において用いた実際のプラスミドを、関連の(pertinent)実施例において記載する。
Uc FatB1、Cc FatB1、Ch FatB2 および‘tesA を含む様々なチオエステラーゼについてのコード領域を含有する複数のプラスミドを構築した。E. coli‘tesA の遺伝子配列を、E. coli MG1655 のゲノム DNA からの PCR 増幅によって得た。Umbellularia californica の FatB1 (Uc FatB1)、Cinnamomum camphora の FatB1 (Cc FatB1) および Cuphea hookeriana の FatB2 (Ch FatB2) についての遺伝子配列を、契約に基づく(Codon Devices、Cambridge、MA 02139)合成の遺伝子の設計および生産によって得た。簡潔には、プライマー TesA_F (配列番号50) および TesA_R (配列番号51)を用いて‘tesA (配列番号25) を増幅した。合成の遺伝子を、PCR 増幅ならびに標準的な消化およびライゲーションのプロトコールによって発現プラスミドへ再クローニングした。Cc FatB1 (配列番号26) を、プライマー CcFatB_F (配列番号52) および CcFatB_R (配列番号53) を用いて増幅した。Ch FatB2 (配列番号27) を、プライマー ChFatB2_F (配列番号54) および ChFatB2_R (配列番号55) を用いて増幅した。Uc FatB1 (配列番号28) を、プライマー UcFatB1_F (配列番号56) および UcFatB1_R (配列番号57) を用いて増幅した。‘tesA (配列番号25) および Cc FatB1 (配列番号26) の増幅産物を、制限酵素 NdeI および AvrII を用いて pETDuet-1 へクローニングした。Ch FatB2 (配列番号27) および Uc FatB1 (配列番号28) の増幅産物を、制限酵素 XbaI および HindIII を用いて、malE 遺伝子とインフレームの状態で pMAL-c2X (NEB、Ipswich、MA) へクローニングした。
2つの別個のベクター、pETDuet-1 および pACYCpTrc を含む多数の異なるコンストラクトから、および E. coli 宿主菌株へ直接組み込まれた構成的プロモーターから、fadD 遺伝子を発現させた。これらのコンストラクトを、以下に記載する。
Cre lox 抗菌性耐性マーカーの除去がその後に続く相同組換え(アレル交換)を用いて、fadD 遺伝子の上流の 5’フランキング領域(配列番号495)を T5 プロモーター配列(配列番号496)を含有する合成の DNA 配列と置換することによって、FadD を構成的に発現させた(詳細なプロトコールについては、例えば Valle, Fernando and Noemi Flores, Overexpression of Chromosomal Genes in Escherichia coli. Vol. 267, Recombinant Gene Expression: Reviews and Protocols. Totowa: Humana Press, 2004 and Palmeros et al., Gene, 247: 255-64 (2000) を参照されたい)。簡潔には、プライマー LB284 (配列番号83) および LB285 (配列番号84) を、loxPcat カセットを pLoxCat2 (配列番号89; Genebank 受入# AJ401047) から PCR 増幅するために用いた。次いで、増幅産物を、プラスミド pKD46 を含有する MG1655 ΔfadE (Genebank 受入 # AY048746) へ形質転換した。loxPcat カセットの組み込みについての選抜後、菌株から pKD46 をキュアリングし、その後、プラスミド pJW168 (Palmeros et al.、Gene、247: 255-64 (2000)) を用いてクロラムフェニコール耐性を除去した。T5 プロモーターによる fadD プロモーターの置換を確認した後、菌株から pJW168 をキュアリングした。得られた菌株は、E. coli MG1655 Δ,fadE、fadD(+) である。
本実施例は、細菌における OleA、OleC および OleD の発現がオレフィンの生産をもたらすことを実証する。
本実施例は、細菌における oleA の発現が脂肪族ケトンの生産をもたらしたことを実証する。
本実施例は、oleA (配列番号2) を発現する E. coli の細胞からのライセートをアシル-CoA 基質と混合するインビトロアッセイを用いて、脂肪族ケトンの生産を観察できることを実証する。
本実施例は、pH 7.0 の 0.1 M リン酸バッファー中において精製された酵素(例えば OleA タンパク質)を精製された基質(例えばアシル補酵素A、アシル-ACP 等)と混合するインビトロアッセイを用いて、脂肪族ケトンを観察できることを実証する。
本実施例は、本明細書に記載される S. maltophilia の核酸配列およびアミノ酸配列を用いる、さらなる oleA、oleC および oleD の核酸配列およびアミノ酸配列の同定を記載する。
本実施例は、公的に利用可能なデータベースにおいてさらなる OleA、OleB、OleC および OleD タンパク質配列を同定するために、アミノ酸モチーフを用い得ることを実証する。
本実施例は、脂肪酸生合成経路が変更された細胞における OleA の発現が、脂肪族ケトンの生産の増強をもたらすことを実証する。
(1) 野生型 E. coli C41(DE3);
(2) アシル-CoA デヒドロゲナーゼ fadE の完全な欠失を有する E. coli C41(DE3) ΔfadE;
(3) IPTG で誘導をかけると fadD を発現するプラスミドを有する E. coli C41(DE3);
(4) IPTG で誘導をかけると fadD を発現するプラスミドを有する E. coli C41(DE3) ΔfadE;
(5) IPTG で誘導をかけると tesA チオエステラーゼ A 遺伝子の切断されたバージョンである‘tesA を発現するプラスミドを有する E. coli C41(DE3);
(6) IPTG で誘導をかけると tesA チオエステラーゼ A 遺伝子の切断されたバージョンである‘tesA を発現するプラスミドを有する E. coli C41(DE3) ΔfadE;
(7) 個別のプラスミド上に含有された、IPTG で誘導をかけると発現する‘tesA および fadD の両方を有する E. coli C41(DE3); および
(8) 個別のプラスミド上に含有された、IPTG で誘導をかけると発現する‘tesA および fadD の両方を有する E. coli C41(DE3) ΔfadE。
本実施例は、脂肪酸生合成経路が変更された細胞における oleA、oleC および oleD の発現が、オレフィンの生産の増強をもたらすことを実証する。
本実施例は、OleA および OleD を含有するインビトロアッセイにおいて、アルデヒド、脂肪族ケトンおよびオレフィンが観察されることを実証する。
本実施例は、精製された OleB タンパク質がインビトロアッセイ中に添加されると、アシル補酵素A 基質、OleA および OleD を含むインビトロアッセイにおいて観察されるアルデヒドおよびオレフィンの量が有意に増強されることを実証する。
本実施例は、オレフィンシンターゼ遺伝子 (oleA、oleB、oleC および oleD) と併せてアシル-CoA シンターゼ遺伝子を発現する細菌によって、脂肪酸をオレフィンへ変換し得ることを実証する。
宿主 1: オレフィンシンターゼ オペロン pCL1920pTrcOleABpTrcOleCD (配列番号78) およびアシル-CoA シンターゼ FadD 過剰発現プラスミド pACYCpTrcFadD で形質転換された E. coli MG1655 ΔfadE。
宿主 2: オレフィンシンターゼ オペロン pCL1920pTrcOleABpTrcOleCD (配列番号78) およびアシル-CoA シンターゼ FadD 過剰発現プラスミド pETDuetFadD で形質転換された E. coli C41 (DE3) ΔfadE。
本実施例は、アシル縮合化(acyl-condensing)酵素 OleA と組み合わせてアシル-CoA シンターゼ遺伝子を発現する細菌によって、脂肪酸を脂肪族ケトンへ変換し得ることを実証する。
本実施例は、細菌において生産され得るオレフィンの型を制御する方法を示す。
本実施例は、Saccharomyces cerevisiae における oleA の機能的発現がインビトロでの脂肪族ケトンの生産をもたらすことを実証する。
本実施例は、精製された OleA、OleD を含有する細胞ライセートおよび重水素化された NADPH を含有するインビトロアッセイにおいて、重水素化されたアルデヒドおよびオレフィンが観察されることを実証する。
本実施例は、インビトロで脂肪族オレフィンを合成できることを実証する。
pETDuet_OleAB および pCOLADuet_OleCD で形質転換された E. coli C41(DE3) を、4つの Ole タンパク質 (OleA、OleB、OleC および OleD) を含有する細菌ライセートを作成するために用いた。
ミリストイル-ACP を、いくつかの改変を伴って Rock et al., Methods Enzymol., 72: 397-403 (1981) に記載される通りに合成した。簡潔には、1-4 mL の最終容量中に 5 mM ATP、2 mM DTT、2% Triton X-100、10 mM LiCl、160 μM ミリスチン酸ナトリウム塩、65 μM ACP-SH、10 mM MgCl2、pH 8.0 の 0.1 M トリス-HCl および 1.5 - 3 μg/mL アシル-ACP シンターゼを含有する反応混合物を、37℃で 3 時間インキュベートし、その後 30℃で終夜インキュベートした。用いたアシル-ACP シンターゼは、Invitrogen から購入した。反応混合物を3容量の水で希釈し、酢酸を用いて pH を 6.0 まで滴定した。溶液を HiTrap DEAE FF 5mL カラム (GE Healthcare) にアプライした。Triton X-100 の大部分を除去するため、カラムを、3カラム容量の pH 6.0 の 10 mM ビス-トリス-HCl で洗浄した。3カラム容量の 80% 2-プロパノールを用いてカラムを溶出することによって、残余の Triton X-100 および遊離の脂肪酸を除去した。3カラム容量の pH 6.0 の 10 mM ビス-トリス-HCl を用いて、2-プロパノールを除去した。10 mL の、pH 6.0 の 10 mM ビス-トリス-HCl 中における 0.6 M LiCl を用いて、ミリストイル-ACP および未反応の ACP-SH をカラムから溶出させた。ミリストイル-ACP を含有する溶出物を、pH 7.0 の 50 mM リン酸ナトリウムバッファーへとバッファー交換し、MWCO 3 kDa concentrators (Millipore) を用いて 1 mL まで濃縮した。ミリストイル-ACP の濃度を、Bradford アッセイ (BioRad) および NuPAGE 12% ビス-トリス SDS-PAGE ゲル上でのデンシトメトリー解析 (Invitrogen) を用いて、2段階で決定した: 最初に、C14-ACP/ACP-SH 画分の全タンパク質濃度を Bradford アッセイ (BioRad proten assay) によって決定した; 第二に、C14-ACP 濃度を、その後にデンシトメトリー解析が続く SDS-PAGE に基づいて、全タンパク質濃度のパーセントとして算出した。C14-ACP は、pH 7.0 の 50mM Na-リン酸バッファー中において -20℃で保管され、3 ヶ月間まで安定であった。
上記の通り、OleA、OleB、OleC および OleD タンパク質を含有する細胞ライセートを作成するために、pETDuetOleAOleB および pCOLADuetOleCOleD で形質転換された E. coli C41(DE3) を用いた。インビトロアッセイ反応は、1 mL の総容量中に 0.1 mM ミリストイル補酵素A もしくは 0.1 mM ミリストイル-ACP、10 mM MgCl2、pETDuetOleAOleB および pCOLADuetOleCOleD で形質転換された E. coli C41(DE3) からの 360 μL の細胞ライセート、1 mM NADPH (Sigma、MO)、1 mM ATP (Sigma、MO)、1 mM HSCoA (Sigma、MO) および 100 mM リン酸バッファー (pH 7.0) を含有した。用いたミリストイル補酵素A は、Sigma (M4414、St Louis MO) から入手し、pH 7.0 の 0.1 M リン酸バッファー中における 10 mM ストック溶液として調製した。サンプルを、37℃で 1 時間インキュベートした。反応を、1% 酢酸/0.1% ギ酸を含有する 5 mL の酢酸エチルを用いてクエンチした。混合物をボルテックスによって混合し、その後遠心した。4 mL の上層(酢酸エチル層)を清潔なガラス管へ移し、遠心機(Vacufuge 5301、Eppendorf、Westbury、NY)中において減圧下で乾燥させた。サンプルを、40 μL の酢酸エチルおよび 10 μL の、対照スパイクとして機能する (酢酸エチル中で調製された) 0.1 mg/mL のヘキサコサン溶液中に再懸濁し、GC/MS によって解析した。1 μL を、特定の炭化水素について解析した。
本実施例は、OleA、OleB、OleC および OleD タンパク質配列を、自然に炭化水素を生産する生物を同定するために用い得ることを実証する。
本実施例は、生物に基づく(biologically based)オレフィンは石油に基づくオレフィンとは区別できることを実証する。特に、本実施例は、生物、例えば oleA、oleB、oleC および oleD 遺伝子を発現する E. coli によって生産されるオレフィンを、石油に基づくオレフィンから区別し得ることを実証する。
δ13C (‰) = [(13C/12C)サンプル- (13C/12C)標準]/ (13C/12C)標準 × 1000。
Claims (17)
- 配列番号2の配列と少なくとも90%の同一性を有するアミノ酸配列を含むOleAポリペプチドをコードする単離核酸配列で形質転換された細胞であって、該細胞が、該細胞内の該OleAの発現により脂肪族ケトンを生産するものである、形質転換細胞。
- 配列番号6の配列と少なくとも90%の同一性を有するアミノ酸配列を含むOleCポリペプチドをコードする核酸配列、及び、配列番号8の配列と少なくとも90%の同一性を有するアミノ酸配列を含むOleDポリペプチドをコードする核酸配列でさらに形質転換され、細胞が、細胞内のOleA、OleCおよびOleDの発現によりオレフィンを生産するものである、請求項1に記載の形質転換細胞。
- 配列番号10の配列と少なくとも90%の同一性を有するアミノ酸配列を含むOleBポリペプチドをコードする核酸配列でさらに形質転換され、細胞が、細胞内のOleA、OleC、OleDおよびOleBの発現によりオレフィンを生産するものである、請求項2に記載の形質転換細胞。
- OleAポリペプチドが、1500アミノ酸残基以下であり、配列番号64〜69、98〜102、116〜120、150〜229および478〜483からなる群から選択されるアミノ酸配列を含む、請求項1〜3いずれか1項に記載の形質転換細胞。
- OleAポリペプチドが、配列番号2の配列と少なくとも95%の同一性を有するアミノ酸配列を含む、請求項4に記載の形質転換細胞。
- OleCポリペプチドが、1500アミノ酸残基以下であり、配列番号72〜74、103〜108、121〜126および327〜402からなる群から選択されるアミノ酸配列を含む、請求項2〜5いずれか1項に記載の形質転換細胞。
- OleDポリペプチドが、1500アミノ酸残基以下であり、配列番号70〜71、109〜115、127〜133、142〜149および403〜487からなる群から選択されるアミノ酸配列を含む、請求項3〜6いずれか1項に記載の形質転換細胞。
- 細胞が、酵母細胞、真菌細胞、細菌細胞、藻類細胞または植物細胞である、請求項1〜7のいずれか1項に記載の形質転換細胞。
- 細胞が、エシェリキア属(Escherichia)、バシラス属(Bacillus)、ラクトバシラス属(Lactobacillus)、ロドコッカス属(Rhodococcus)、シュードモナス属(Pseudomonas)、アスペルギルス属(Aspergillus)、トリコデルマ属(Trichoderma)、ニューロスポラ属(Neurospora)、フザリウム属(Fusarium)、ヒューミコラ属(Humicola)、リゾムコール属(Rhizomucor)、クリベロマイセス属(Kluyveromyces)、ピチア属(Pichia)、ムコール属(Mucor)、マイセリオフトラ属(Myceliophtora)、ペニシリウム属(Penicillium)、ファネロケーテ属(Phanerochaete)、プレウロタス属(Pleurotus)、トラメテス属(Trametes)、クリソスポリウム属(Chrysosporium)、サッカロマイセス属(Saccharomyces)、シゾサッカロマイセス属(Schizosaccharomyces)、ステノトロホモナス属(Stenotrophamonas)、キネオコッカス属(Kineococcus)、ヤロウイア属(Yarrowia)、またはストレプトマイセス属(Streptomyce)からなる群から選択される、請求項1〜8のいずれか1項に記載の形質転換細胞。
- 細胞が、アシル−CoAデヒドロゲナーゼをコードする遺伝子における変異を含む、請求項1〜9のいずれか1項に記載の形質転換細胞。
- 細胞が、アシル−CoAシンターゼをさらに含む、請求項1〜10のいずれか1項に記載の形質転換細胞。
- 細胞が、チオエステラーゼをさらに含む、請求項1〜11のいずれか1項に記載の形質転換細胞。
- 炭化水素の生産方法であって、オレフィンを生産する請求項3〜7のいずれか1項に記載の細胞を基質とともに、オレフィンを生産するのに十分な条件下で培養することを含む、方法。
- 脂肪族ケトンの生産方法であって、脂肪族ケトンを生産する請求項1に記載の細胞を基質とともに、脂肪族ケトンを生産するのに十分な条件下で培養することを含む、方法。
- OleCおよび/またはOleDをコードする遺伝子が欠失または減衰されている、請求項1、4及び5のいずれか1項に記載の形質転換細胞。
- 請求項15に記載の形質転換細胞を培養することを含む、脂肪族ケトンの生産方法。
- オレフィンの産生に有用な酵素を同定する方法であって、
(a)
(i)OleAおよびOleD、
(ii)OleAおよびOleC、ならびに
(iii)OleCおよびOleD
からなる群から選択されたポリペプチドを含む細胞を、オレフィンを産生する能力を有すると推測される酵素をコードする核酸で形質転換すること;および、
(b)細胞がオレフィンを産生するかどうかを決定すること、ここで、細胞によるオレフィン産生の存在が、該核酸がオレフィンの産生に有用なポリペプチドをコードすることを示し、
さらに、OleAは配列番号2の配列と少なくとも90%の配列同一性を有し、OleCは配列番号6の配列と少なくとも90%の配列同一性を有し、OleDは配列番号8の配列と少なくとも90%の配列同一性を有するものである、
方法。
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CN112574913B (zh) * | 2020-12-15 | 2023-06-16 | 上海海洋大学 | 深海玫瑰变色菌及其在诱导厚壳贻贝附着中的应用 |
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US7314974B2 (en) * | 2002-02-21 | 2008-01-01 | Monsanto Technology, Llc | Expression of microbial proteins in plants for production of plants with improved properties |
US7566813B2 (en) | 2002-03-21 | 2009-07-28 | Monsanto Technology, L.L.C. | Nucleic acid constructs and methods for producing altered seed oil compositions |
CA2496630A1 (en) | 2002-08-30 | 2004-03-11 | North Carolina State University | Abiz phage resistance gene |
US7652167B2 (en) | 2004-07-19 | 2010-01-26 | Board Of Trustees Of Michigan State University | Process for production of organic acid esters |
DE102006022718B4 (de) | 2006-05-16 | 2008-10-02 | Clariant International Limited | Zusammensetzung von Brennstoffölen |
US8110670B2 (en) | 2006-05-19 | 2012-02-07 | Ls9, Inc. | Enhanced production of fatty acid derivatives |
WO2007136762A2 (en) | 2006-05-19 | 2007-11-29 | Ls9, Inc. | Production of fatty acids and derivatives thereof |
US20100242345A1 (en) | 2006-05-19 | 2010-09-30 | LS9, Inc | Production of fatty acids & derivatives thereof |
KR20100015763A (ko) | 2007-03-28 | 2010-02-12 | 엘에스9, 인코포레이티드 | 지방산 유도체의 생산 증가 |
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KR101646966B1 (ko) | 2016-08-09 |
US20190376094A1 (en) | 2019-12-12 |
EP2160460A2 (en) | 2010-03-10 |
CA2679085C (en) | 2018-04-10 |
AU2008256921A1 (en) | 2008-12-04 |
KR20100022984A (ko) | 2010-03-03 |
US20160076058A1 (en) | 2016-03-17 |
US20100235934A1 (en) | 2010-09-16 |
JP2015091244A (ja) | 2015-05-14 |
BRPI0813359A2 (pt) | 2014-10-14 |
US9200299B2 (en) | 2015-12-01 |
CA2679085A1 (en) | 2008-12-04 |
AU2008256921B2 (en) | 2015-01-22 |
ES2646815T3 (es) | 2017-12-18 |
CN101809146A (zh) | 2010-08-18 |
CN101809146B (zh) | 2013-12-11 |
JP2010527612A (ja) | 2010-08-19 |
EP2160460B1 (en) | 2017-08-02 |
KR20160099717A (ko) | 2016-08-22 |
WO2008147781A2 (en) | 2008-12-04 |
MX2009009383A (es) | 2009-09-15 |
JP6173294B2 (ja) | 2017-08-02 |
KR101862691B1 (ko) | 2018-05-31 |
WO2008147781A3 (en) | 2009-04-30 |
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