JP2022103196A - リパーゼ変異体およびこれをコードするポリヌクレオチド - Google Patents
リパーゼ変異体およびこれをコードするポリヌクレオチド Download PDFInfo
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Abstract
Description
本出願は、コンピュータ読み取り可能な形態の配列表を含んでおり、これは、本明細書おいて参照により援用される。
c)これらの混合物、
(式中、各R1は、独立して、3~24個の炭素を含む分枝状アルキル基または1~24個の炭素を含む直鎖状アルキル基である)
を有する有機触媒、これらの混合物からなる群から選択される有機触媒の存在下で向上した性能を有するステップと;前記変異体を回収するステップを含む。
リパーゼ:「リパーゼ」または「脂肪分解酵素」または「脂質エステラーゼ」という用語は、酵素命名法によって定義されている、クラスEC3.1.1に属する酵素である。これは、リパーゼ活性(トリアシルグリセロールリパーゼ、EC3.1.1.3)、クチナーゼ活性(EC3.1.1.74)、ステロールエステラーゼ活性(EC3.1.1.13)および/またはワックス-エステルヒドロラーゼ活性(EC3.1.1.50)を有し得る。本発明の目的のために、リパーゼ活性は、実施例に記載する手順に従い決定される。一態様では、本発明の変異体は、配列番号2の成熟ポリペプチドのリパーゼ活性の少なくとも20%、例えば、少なくとも25%、少なくとも30%、少なくとも35%、少なくとも40%、少なくとも45%、少なくとも50%、少なくとも55%、少なくとも60%、少なくとも65%、少なくとも70%、少なくとも75%、少なくとも80%、少なくとも85%、少なくとも90%、少なくとも95%、または少なくとも100%を有する。
c)これらの混合物、
(式中、各R1は、独立して、3~24個の炭素を含む分枝状アルキル基または1~24個の炭素を含む直鎖状アルキル基であり、特に、Rは、2-ブチルオクチルである)
を有する有機触媒、これらの混合物からなる群から選択される有機触媒に関し、好ましくは、向上した安定性は、Rが2-ブチルオクチルである式2の存在下で達成される。
(同等の残基×100)/(アラインメントの長さ-アラインメント中のギャップの総数)
(同一のデオキシリボヌクレオチド×100)/(アラインメントの長さ-アラインメント中のギャップの総数)
本発明の目的のために、配列番号2において開示されている成熟ポリペプチドは、他のリパーゼ中の対応するアミノ酸残基の判定に用いられる。別のリパーゼのアミノ酸配列を配列番号2に開示した成熟ポリペプチドとアラインメントし、アラインメントに基づいて、配列番号2に開示した成熟ポリペプチドにおける任意のアミノ酸残基に対応するアミノ酸位置番号を、EMBOSSパッケージのNeedleプログラム(EMBOSS:The European Molecular Biology Open Software Suite,Rice et al.,2000,Trends Genet.16:276-277)で実行されているようなNeedleman-Wunschアルゴリズム(NeedlemanおよびWunsch,1970,J.Mol.Biol.48:443-453)、好ましくはバージョン5.0.0以降を用いて決定する。用いるパラメータは、ギャップ開始ペナルティ10、ギャップ伸長ペナルティ0.5、およびEBLOSUM62(BLOSUM62のEMBOSSバージョン)置換マトリックスである。
本発明は、配列番号2の成熟ポリペプチドの位置T37A、D、E、F、G、H、I、L、N、P、Q、R、S、V、W、Y、N39A、C、D、E、F、G、I、K、L、M、P、Q、R、T、V、W、Y、およびG91D、H、I、P、Qに対応する1つまたは複数(例えばいくつか)の位置で置換を含む、単離されたリパーゼ変異体に関し、ここで、変異体はリパーゼ活性を有する。
(1)事前に形成した過酸:好適な事前に形成した過酸としては、これらに限定されないが、事前に形成した過酸もしくはその塩からなる群から選択される化合物、典型的には、ペルオキシカルボン酸もしくはその塩、またはペルオキシスルホン酸もしくはその塩のいずれかが挙げられる。
式中、R14は、アルキル、アラルキル、シクロアルキル、アリールもしくは複素環式基から選択され;R14基は、直鎖または分岐状の、置換もしくは非置換であってよく;Yは、電荷中性を達成する任意の好適な対イオンであり、好ましくは、Yは、水素、ナトリウムもしくはカリウムから選択される。好ましくは、R14は、直鎖または分岐状の、置換もしくは非置換C6~9アルキルである。好ましくは、過酸もしくはその塩は、ペルオキシヘキサン酸、ペルオキシヘプタン酸、ペルオキシオクタン酸、ペルオキシノナン酸、ペルオキシデカン酸、それらの任意の塩、またはそれらの任意の組合せから選択される。特に好ましい過酸は、フタルイミド-ペルオキシ-アルカン酸、とりわけ、ε-フタルイミド-ペルオキシ-ヘキサン酸(PAP)である。好ましくは、過酸もしくはその塩は、30℃~60℃の範囲の融点を有する。
式中、R15は、アルキル、アラルキル、シクロアルキル、アリールもしくは複素環式基から選択され;R15基は、直鎖または分岐状の、置換もしくは非置換であってよく;Zは、電荷中性を達成する任意の好適な対イオンであり、好ましくは、Zは、水素、ナトリウムもしくはカリウムから選択される。好ましくは、R15は、直鎖または分岐状の、置換もしくは非置換C6~9アルキルである。好ましくはこのような漂白成分は、0.01~50%、最も好ましくは0.1%~20%の量で組成物中に存在してよい。
R1-C(O)-OO-(O)C-R2
(式中、R1は、少なくとも5個の炭素原子を含み、任意選択で1個または複数個の置換基(例えば、-N+(CH3)3、-COOHもしくは-CN)および/またはアルキルラジカルの隣接する炭素原子間に挿入された1つまたは複数の割り込み部分(例えば、-CONHもしくはCH=CH-)を含む、C6~C18アルキル、好ましくはC6~C12アルキル基を示し;R2は、過酸化物部分と適合性の脂肪族基を示し、ここで、R1およびR2は合わせて計8~30個の炭素原子を含む)のジアシル過酸化物から選択されるものが挙げられる。一態様では、R1およびR2は、直鎖状非置換C6~C12アルキル鎖である。最も好ましくは、R1およびR2は同一である。R1およびR2の両方がC6~C12アルキル基であるジアシル過酸化物は、C6~C12アルキル基であり、これが特に好ましい。好ましくは、R基の少なくとも一方、最も好ましくはその一方のみ(R1またはR2)は、α位置、または好ましくはαおよびβ位置のいずれにも、あるいは最も好ましくはαまたはβまたはγ位置のいずれにも分岐もしくはペンダント環を含まない。1つのさらに好ましい実施形態において、好ましくは、R1アシル基の加水分解は高速で、過酸を生成するが、R2アシル基の加水分解は低速であるように、DAPが非対称であってもよい。
R3-C(O)-OO-C(O)-(CH2)n-C(O)-OO-C(O)-R2
(式中、R3は、C1~C9アルキル、好ましくはC3~C7アルキル基を示し;nは、2~12、好ましくは4~10の整数(両端の値を含む)を示す)
のテトラアシル過酸化物から選択される。
式中、nおよびmは、独立して、0~4であり、好ましくは、nおよびmは両方が0であり;各R1は、独立して、水素、アルキル、シクロアルキル、アリール、融合アリール、複素環、融合複素環、ニトロ、ハロ、シアノ、スルホナト、アルコキシ、ケト、カルボキシルおよびカルボアルコキシラジカルからなる群から選択される置換もしくは非置換ラジカルから選択され;ならびに任意の2つの隣接R1置換基が結合して、融合アリール、融合炭素環もしくは融合複素環を形成してもよく;各R2は、独立して、水素、ヒドロキシ、アルキル、シクロアルキル、アルカリル、アリール、アラルキル、アルキレン、複素環、アルコキシ、アリールカルボニル基、カルボキシアルキル基およびアミド基からなる群から選択される置換もしくは非置換ラジカルから独立して選択され;任意のR2がいずれか他のR2と結合して、共通環の一部を形成してもよく;任意のジェミナルR2が結合してカルボニルを形成してもよく;また、任意の2つのR2が結合して、置換もしくは非置換の融合した不飽和部分を形成してもよく;R3は、C1~C20置換もしくは非置換アルキルであり;R4は、水素または部分Qt-Aであり、ここで、Qは、分岐または非分岐アルキレンであり、t=0または1であり、Aは、OSO3 -、SO3 -、CO2 -、OCO2 -、OPO3 2-、OPO3H-およびOPO2 -からなる群から選択されるアニオン基であり;R5は、水素または部分-CR11R12-Y-Gb-Yc-[(CR9R10)y-O]k-R8であり;ここで、各Yは、独立して、O、S、N-H、またはN-R8からなる群から選択され;各R6は、独立して、アルキル、アリールおよびヘテロアリールからなる群から選択され、前記部分は、置換もしくは非置換であり、置換もしくは非置換のいずれにかかわらず、前記部分は、21個未満の炭素を有し;各Gは、独立して、CO,SO2、SO、POおよびPO2からなる群から選択され;R9およびR10は、独立して、HおよびC1~C4アルキルからなる群から選択され;R11およびR12は、独立して、Hおよびアルキルからなる群から選択されるか、または合わせて考える場合、結合してカルボニルを形成してもよく;b=0または1;c=0または1であってよいが、b=0であるとき、c=0でなければならない;yは1~6の任意の整数であり;kは0~20の整数であり;R6はH、またはアルキル、アリールもしくはヘテロアリール部分であり;前記部分は、置換もしくは非置換であり;Xは、それが存在すれば、好適な電荷平衡対イオンであり、R4が水素である場合には、Xが存在するのが好ましく、好適なXとしては、これらに限定されないが、塩化物、臭化物、硫酸塩、メトサルフェート、スルホン酸塩、p-トルエンスルホン酸塩、ボロンテトラフルオリドおよびリン酸塩が挙げられる。
式中、R13は、3~24個の炭素原子(分岐炭素原子を含む)を含む分岐アルキル基および1~24個の炭素原子を含む直鎖アルキル基であり;好ましくは、R13は、8~18個の炭素原子を含む分岐アルキル基または8~18個の炭素原子を含む直鎖アルキル基であり;好ましくは、R13は、2-プロピルへプチル、2-ブチルオクチル、2-ペンチルノニル、2-ヘキシルデシル、n-ドデシル、n-テトラデシル、n-ヘキサデシル、n-オクタデシル、イソ-ノニル、イソ-デシル、イソ-トリデシルおよびイソ-ペンタデシル;好ましくは、R13は、2-ブチルオクチル、2-ペンチルノニル、2-ヘキシルデシル、イソ-トリデシルおよびイソ-ペンタデシルからなる群から選択される。
c)これらの混合物
(式中、各R1は、独立して、3~24個の炭素を含む分枝状アルキル基または1~24個の炭素を含む直鎖状アルキル基である)
を有する有機触媒からなる群から選択される有機触媒の存在下で、向上した性能を有する。
親リパーゼは、(a)配列番号2の成熟ポリペプチドに対し少なくとも60%の配列同一性を有するポリペプチド;(b)低ストリンジェンシー条件下で(i)配列番号1の成熟ポリペプチドコード配列もしくは(ii)(i)の完全長補体とハイブリダイズするポリヌクレオチドによりコードされるポリペプチド;または(c)配列番号1の成熟ポリペプチドコード配列に対し少なくとも60%の配列同一性を有するポリヌクレオチドによりコードされるポリペプチドであってよい。
本発明はまた、リパーゼ変異体を得るための方法に関し、この方法は、親リパーゼに、配列番号2の成熟ポリペプチドの位置T37、N39、またはG91に対応する1つまたは複数の位置で置換を導入するステップであって、変異体が、リパーゼ活性を有し、親リパーゼと比較して、下記の式:
c)これらの混合物、
(式中、各R1は、独立して、3~24個の炭素を含む分枝状アルキル基または1~24個の炭素を含む直鎖状アルキル基である)
を有する有機触媒からなる群から選択される有機触媒の存在下で、向上した性能を有するステップと;前記変異体を回収するステップを含む。
本発明はまた、本発明の変異体をコードする単離されたポリヌクレオチドにも関する。
本発明はまた、制御配列と適合性のある条件下で好適な宿主細胞においてコード配列の発現をもたらす1つまたは複数の制御配列と作動可能に結合した本発明の変異体をコードするポリヌクレオチドを含む核酸構築物に関する。
本発明はまた、本発明の変異体をコードするポリヌクレオチド、プロモータ、ならびに、転写および翻訳終止シグナルを含む組換え発現ベクターに関する。種々のヌクレオチドおよび制御配列が一緒になって、このような部位で変異体をコードするポリヌクレオチドの挿入または置換を可能とするために1つまたは複数の好都合な制限部位を含み得る組換え発現ベクターが生成される。または、ポリヌクレオチドは、ポリヌクレオチドまたはポリヌクレオチドを含む核酸構築物を発現に適切なベクターに挿入することにより発現され得る。発現ベクターの形成において、コード配列は、コード配列が、発現に適切な制御配列と作動可能にリンクするようベクター中に位置されている。
本発明はまた、本発明の変異体の生成をもたらす1つまたは複数の制御配列に作動可能にリンクした本発明の変異体をコードするポリヌクレオチドを含む組換え宿主細胞に関する。ポリヌクレオチドを含む構築物もしくはベクターは、構築物もしくはベクターが染色体性組み込み体として、もしくは、既述の自己複製余剰-染色体性ベクターとして維持されるよう宿主細胞に導入される。「宿主細胞」という用語は、複製の最中に生じる突然変異により親細胞と同等ではない親細胞のいずれかの子孫を包含する。宿主細胞の選択は、変異体をコードする遺伝子およびそのソースに大きく依存することとなる。
本発明はまた:(a)変異体の発現に好適な条件下で本発明の宿主細胞を培養するステップ;および、(b)変異体を回収するステップを含む変異体の生成方法に関する。
本発明は、リパーゼ変異体を含む欧州特許第11170520号明細書に記載の微粒子組成物にも関し、この変異体は、配列番号2の成熟ポリペプチドの位置T37A、D、E、F、G、H、I、L、N、P、Q、R、S、V、W、Y、N39A、C、D、E、F、G、I、K、L、M、P、Q、R、T、V、W、Y、およびG91D、H、I、P、Qに対応する1つまたは複数の位置で置換を含み、変異体は、リパーゼ活性を有する。
本発明は、欧州特許第11170520号明細書に記載のリパーゼ粒子を製造するための、配列番号2の成熟ポリペプチドの位置T37A、D、E、F、G、H、I、L、N、P、Q、R、S、V、W、Y、N39A、C、D、E、F、G、I、K、L、M、P、Q、R、T、V、W、Y、およびG91D、H、I、P、Qに対応する1つまたは複数の位置で置換を含むリパーゼ変異体の使用にも関し、ここで、変異体は、リパーゼ活性を有する。
本発明はまた、回収可能な量で変異体を発現および生成するように、本発明のポリヌクレオチドを含む植物、例えば、トランスジェニック植物、植物部分、または植物細胞に関する。変異体は、植物または植物部分から回収することができる。あるいは、変異体を含む植物または植物部分は、食品または飼料の品質を改善する、例えば、栄養価、嗜好性および流体学的性質を高めるように、または非栄養因子を破壊するために用いられる。
洗濯における洗浄性能を評価するために、自動機械的応力分析(AMSA)を用いて、洗浄実験を実施する。AMSAで、多量の少容量リパーゼ-洗剤溶液の洗浄性能を試験することができる。AMSAプレートは、試験溶液のための多くのスロットと、汚れた繊維製品をすべてのスロット開口部にしっかりと締め付けるリッドを有する。洗浄時間中、プレート、試験溶液、繊維製品およびリッドを激しく振ることにより、試験溶液を繊維製品に接触させて、規則的、周期的振動方式で機械的応力を加える。さらに詳しい説明については、国際公開第02/42740号パンフレット、特に第23~24頁のパラグラフ“Special method embodiments”を参照のこと。
相対性能スコア(RPwash)は、従来のリパーゼに対する本発明のリパーゼ変異体の性能(P)を与える:RP=P(本発明のリパーゼ変異体)/P(従来のリパーゼ)。従来のリパーゼより良好に実施すれば、リパーゼ製剤は、向上した洗浄性能を示すと考えられる。
Claims (25)
- R1が、独立して、2-プロピルへプチル、2-ブチルオクチル、2-ペンチルノニル、2-ヘキシルデシル、n-ドデシル、n-テトラデシル、n-ヘキサデシル、n-オクタデシル、イソ-ノニル、イソ-デシル、イソ-トリデシルおよびイソ-ペンタデシルからなる群から選択される、請求項1に記載の方法。
- 前記親リパーゼが、配列番号2の成熟ポリペプチドに対し少なくとも60%同一性を有するアミノ酸配列を含み;配列番号2の前記成熟ポリペプチドのアミノ酸配列、またはリパーゼ活性を有するその断片から構成される、請求項1または2に記載の方法。
- 前記変異体が、以下:
a)配列番号2の成熟ポリペプチドに対し少なくとも60%の配列同一性を有するアミノ酸配列を含むポリペプチド;
b)少なくとも低ストリンジェンシー条件下で(i)配列番号1の成熟ポリペプチドコード配列;もしくは(ii)(i)の完全長相補鎖とハイブリダイズするポリヌクレオチドによりコードされるポリペプチド、または
c)配列番号1の成熟ポリペプチドコード配列に対し少なくとも60%の同一性を有するヌクレオチド配列を含むポリヌクレオチドによりコードされるポリペプチド
である、請求項1~3のいずれか1項に記載の方法。 - 前記置換が、T37A、D、E、F、G、H、I、L、N、P、Q、R、S、V、W、Y、N39A、C、D、E、F、G、I、K、L、M、P、Q、R、T、V、W、Y、およびG91D、H、I、P、Qから選択される、請求項1~4のいずれか1項に記載の方法。
- 前記変異体が、配列番号2の前記成熟ポリペプチドの位置D96、T143、A150、E210、G225、T231、N233およびP250に対応する1つまたは複数の位置での置換をさらに含む、請求項1~5のいずれか1項に記載の方法。
- 前記置換が、D96G、T143A、A150G、E210Q、G225R、T231R、N233RおよびP250Rから選択される、請求項6に記載の方法。
- 前記変異体が、以下:
a)G91A+D96G+T231R+N233R;
b)G91Q+T143A+E210Q+T231R+N233R+P250R;
c)G91Q+A150G+E210Q+T231R+N233R+P250R;
d)T37R+N39R+G91A+D96G+T231R+N233R;
e)G91A+D96G+G225R+T231R+N233R;
f)G91Q+E210Q+T231R+N233R+P250R;
g)G91N+E210Q+T231R+N233R+P250R;
h)G91I+E210Q+T231R+N233R+P250R;
i)G91L+E210Q+T231R+N233R;または
j)G91A+D96G+A150G+T231R+N233R
である、請求項1に記載の方法。 - 配列番号2の前記成熟ポリペプチドの位置T37A、D、E、F、G、H、I、L、N、P、Q、R、S、V、W、Y、N39A、C、D、E、F、G、I、K、L、M、P、Q、R、T、V、W、Y、およびG91D、H、I、P、Qに対応する1つまたは複数の位置での置換を含み、リパーゼ活性を有する、リパーゼ変異体。
- 以下:
a)配列番号2の成熟ポリペプチドに対し少なくとも60%の配列同一性を有するポリペプチド;
b)低ストリンジェンシー条件下で(i)配列番号1の成熟ポリペプチドコード配列;もしくは(ii)(i)の完全長補体とハイブリダイズするポリヌクレオチドによりコードされるポリペプチド、または
c)配列番号1の成熟ポリペプチドコード配列に対し少なくとも60%の同一性を有するポリヌクレオチドによりコードされるポリペプチド;及び
d)リパーゼ活性を有する配列番号2の成熟ポリペプチドの断片
からなる群から選択される親リパーゼの変異体である、請求項9に記載の変異体。 - 前記親リパーゼのアミノ酸配列に対して、少なくとも60%、少なくとも65%、少なくとも70%、少なくとも75%、少なくとも80%、少なくとも85%、少なくとも90%、少なくとも95%、少なくとも96%、少なくとも97%、少なくとも98%、または少なくとも99%であるが、100%未満の配列同一性を有する、請求項10に記載の変異体。
- 前記置換の数が、1~20、例えば、1~10及び1~5、例えば1、2、3、4、5、6、7、8、9、10、11、12、13、14、15、16、17、18、19または20置換である、請求項9~11のいずれか1項に記載の方法。
- 位置D96、T143、A150、E210、G225、T231、N233およびP250に対応する1つまたは複数の位置での置換をさらに含む、請求項9~12のいずれか1項に記載の変異体。
- 前記置換が、D96G、T143A、A150G、E210Q、G225R、T231R、N233RおよびP250Rから選択される、請求項13に記載の方法。
- 前記変異体が、以下:
a)G91Q+T143A+E210Q+T231R+N233R+P250R;
b)G91Q+A150G+E210Q+T231R+N233R+P250R;
c)T37R+N39R+G91A+D96G+T231R+N233R;
d)G91Q+E210Q+T231R+N233R+P250R;または
e)G91I+E210Q+T231R+N233R+P250R
である、請求項1~14のいずれか1項に記載の変異体。 - 前記変異体が、以下:
a)G91A+D96G+T231R+N233R;
b)G91A+D96G+G225R+T231R+N233R;
c)G91N+E210Q+T231R+N233R+P250R;
d)G91L+E210Q+T231R+N233R;または
e)G91A+D96G+A150G+T231R+N233R
である、変異体。 - R1が、独立して、2-プロピルへプチル、2-ブチルオクチル、2-ペンチルノニル、2-ヘキシルデシル、n-ドデシル、n-テトラデシル、n-ヘキサデシル、n-オクタデシル、イソ-ノニル、イソ-デシル、イソ-トリデシルおよびイソ-ペンタデシルからなる群から選択される、請求項17に記載の変異体。
- 請求項9~18のいずれか1項に記載の変異体をコードする単離ポリヌクレオチド。
- 請求項19に記載のポリヌクレオチドを含む核酸構築物。
- 請求項19に記載のポリヌクレオチドを含む発現ベクター。
- 請求項19に記載のポリヌクレオチドを含む宿主細胞。
- 請求項9~18のいずれか1項に記載の変異体を生成する方法であって、以下:
a)前記変異体の発現に好適な条件下で請求項22の宿主細胞を培養するステップと;
b)前記変異体を回収するステップと
を含む方法。 - 請求項19に記載のポリヌクレオチドで形質転換したトランスジェニック植物、植物部分または植物細胞。
- 請求項9~18のいずれか1項に記載の変異体を生成する方法であって、以下:
a)前記変異体の生成を実施可能にする条件下で、前記変異体をコードするポリヌクレオチドを含むトランスジェニック植物または植物細胞を培養するステップと;
b)前記変異体を回収するステップと
を含む方法。
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