JP2019504616A - パエニバチルス(Paenibacillus)属種及びバチルス(Bacillus)属種のマンナナーゼ - Google Patents
パエニバチルス(Paenibacillus)属種及びバチルス(Bacillus)属種のマンナナーゼ Download PDFInfo
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- JP2019504616A JP2019504616A JP2018522947A JP2018522947A JP2019504616A JP 2019504616 A JP2019504616 A JP 2019504616A JP 2018522947 A JP2018522947 A JP 2018522947A JP 2018522947 A JP2018522947 A JP 2018522947A JP 2019504616 A JP2019504616 A JP 2019504616A
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- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
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- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
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- 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
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- 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
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- C12Y—ENZYMES
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Abstract
Description
本出願は、2015年11月5日出願の米国仮特許出願第62/251516号明細書、及び2016年1月13日出願の米国仮特許出願第62/278383号明細書の優先権の利益に関し、且つこれを主張する。これらの出願は双方とも、それらの全体が参照によって本明細書に組み込まれる。
ASCIIテキストファイル(名前:NB40831WOPCT_ST25;サイズ:59.3KB;作成日:2016年11月2日)として本出願と共に電子的に提出された配列表の内容は、本出願の一部を形成し、そしてその全体が参照によって本明細書に組み込まれる。
アッセイ
以下に記載する実施例に用いる以下のアッセイは、標準的なアッセイである。時折、特定のプロトコルが、これらの標準的なアッセイからの逸脱を必要とする。そのような場合、以下の標準的なアッセイプロトコルからの逸脱を、実施例において同定する。
酵素の性能指数(PI)は、変異体の性能(測定値)を親酵素(理論値又は測定値)と、同じタンパク質濃度にて比較している。親酵素の洗浄性能についての理論値を、親酵素の標準曲線のLangmuirフィットから抽出したパラメータを用いて算出することができる。1を超えるPI(PI>1)は、特定の親、例えばPspMan4(配列番号2)又はBspMan5(配列番号16)と比較して、変異体による性能の向上を示す一方、1のPI(PI=1)は、特定の親と同じ性能で実行する変異体を同定し、1未満のPI(PI<1)は、特定の親よりも悪い性能で実行する変異体を同定する。
タンパク質濃度判定を、積分ピーク面積を測定する高速液体クロマトグラフィ(HPLC)法を用いて実行して、96ウェルマイクロタイタープレート(MTP)中で増殖させた培養液由来の上澄み中でのタンパク質の発現レベルを判定した。サンプルを、濾過した培養液の上澄みから得て、25mMトリス−HClバッファ、pH7.5中の4倍希釈液として調製した。逆相HPLCを、Poroshell 300SB−C8カラム(2.1×75mm)を備えたAgilent 1200 Series HPLC系で、0.1%TFAをそれぞれ補った水及びアセトニトリルの溶媒で構成した勾配溶離を用いて実行した。サンプルを、50℃にて2mL/分の流量で溶出した。タンパク質を、220nmでの吸光度を測定することによって検出して、ピークを、ChemStationソフトウェア(Agilent Technologies)を用いて積分した。サンプルのタンパク質濃度を、精製した親タンパク質(例えば、PspMan4(配列番号2)又はBspMan5(配列番号16))の標準曲線に基づいて判定した。
後に続く実施例において記載するマンナナーゼ変異体のマンナナーゼ活性を、溶液中ローカストビーンガム(LBG)ガラクトマンナン(Sigma G0753)(おおよそ0.3%(w/v)のLBG基質)の加水分解を測定することによって試験した。用いた試薬溶液は、50mMトリス−HClバッファ、pH7.5(基質希釈バッファ)、及び50mM MOPSバッファ、pH7.2、0.005%TWEEN(登録商標)−80含有(酵素希釈バッファ)であった。作用基質溶液を調製するために、LBG粉末(製品No.G0753,Sigma−Aldrich,St.Louis,MO)を、50mMトリスHClバッファ、pH7.5の加熱溶液中に撹拌下で溶解させた。室温に冷却して直ぐに、溶液を遠心分離して、澄明な上澄みを基質溶液として用いた。
後に続く実施例において記載するマンナナーゼ変異体の安定性を、50mM MOPSバッファ、pH7.2、0.005%TWEEN(登録商標)−80中の57℃でのストレス条件下で、高温での5分間のインキュベーション後にサンプルの残留活性を測定することによって試験した。初期の(ストレスのない)活性を測定するために、先の節「マンナナーゼ活性アッセイ」に記載したアッセイを用いて、酵素サンプルを、50mM MOPSバッファ、pH7.2、0.005%TWEEN(登録商標)−80中に希釈して、直ちに、LBGに対する活性についてアッセイした。ストレスを受けた活性を測定するために、先の節「マンナナーゼ活性アッセイ」に記載したように、50mM MOPSバッファ、pH7.2、0.005%TWEEN(登録商標)−80中に希釈した酵素サンプルを、シールしたPCRプレート内で、サーモサイクラー(Tetrad2 Peltier Thermal Cycler,Bio−Rad Laboratories,Hercules,CA)において57℃にて5分間インキュベートしてから、活性についてアッセイした。
先に記載したように、ストレスを受けた活性の値及びストレスのない活性の値を、LBG基質の加水分解によって一旦測定して、ストレスを受けた活性の、ストレスのない活性に対する比率をとって、100を乗じることによって、%残留活性を算出した。変異体の残留活性を親の残留活性で割ることによって、安定性PI値を得た。
変異体を、LBGミクロスワッチ(CFT C−S−73,Center for Testmaterials,Vlaardingen,The Netherlands)に対する洗浄性能について、親の性能と比較して試験した。
」に記載した、親の標準曲線について測定した値のLangmuirフィットから抽出したパラメータを用いて、関連タンパク質濃度での親の洗浄性能についての理論値を算出した。
PspMan4の部位評価ライブラリの作成
PspMan4タンパク質配列中に単一アミノ酸置換を導入するための標準的な分子生物学プロトコルを用いて、PspMan4についての部位評価ライブラリ(SEL)を作成した。PspMan4遺伝子(配列番号1)を含有する鋳型プラスミドを構築した。SELを、PspMan4(配列番号2)の成熟した領域における予め選択した位置にて生産した。SELにおける各アミノ酸部位についてのフォワードNNSオリゴマー及びリバースNNSオリゴマー、並びに外側のプライマー(発現カセットの始点又は終点にハイブリダイズする)を、Eurofins Genomics,Huntsville,AL,USAに注文した。
PspMan4突然変異の評価
コンビナブル突然変異を、コンビナトリアル変異体を作製するのに用いることができる、分子中の置換として説明することができる。コンビナブル突然変異は、分子の少なくとも1つの所望される特性を向上させる一方で、発現、活性、又は安定性をいずれも大きく低下させないものである。生産的位置を、特性の向上を示すコンビナトリアル変異体を作製するのに最も有用な、分子内の位置として説明し、当該位置はそれ自体、少なくとも1つのコンビナブル突然変異を許容する。
PspMan4変異体の結晶構造
2つのPspMan4変異体、PspMan118及びPspMan148の三次元構造を、X線結晶学的方法を用いて判定した。
BspMan5及びその変異体のクローニング及び異種発現
BspMan5(配列番号16)は、US6566114−002(残基32〜340)(配列番号17)の変異体であり、BspMan5のアミノ酸配列は、突然変異:P85L、及びN末端に挿入されたアミノ酸AGKを有し、アミノ酸位置は、配列番号2のアミノ酸配列との対応によって番号を付けている。
BspMan5〜15を、清澄化した枯草菌(B.subtilis)培養ブロスから精製した。イオン交換、疎水性相互作用、又はサイジング分画樹脂が挙げられるカラムクロマトグラフィの組合せを用いた。LBGに対する活性を、PAHBAH(p−ヒドロキシ安息香酸ヒドラジド)アッセイ(Lever,Anal Biochem,47:248,1972)を介して試験することによって、マンナナーゼを含有する画分を同定した。注目する画分をプールして、10K Amicon Ultra装置を用いて濃縮して、サンプルを40%グリセロールに調整して、長期間の保存用に−20℃にて保存した。
BspMan5及びその変異体の熱安定性
熱安定性を、T50値を判定することによって評価した。これは、アッセイの条件下で酵素が活性を50%保持する温度として定義される。各酵素を、サーモサイクラー内で、0.005%Tween−80を含有する50mMクエン酸ナトリウムバッファpH6.0中で、以下の温度にて2時間インキュベートした:40、41.7、44.7、49.4、55、59.7、63、65、67、及び70℃。LBGを基質として用いて(50mMクエン酸ナトリウムバッファpH6.0中、0.45%LBG溶液)、50℃にて10分のインキュベーション後に、酵素活性を測定した。放出された還元糖を、PAHBAH(p−ヒドロキシ安息香酸ヒドラジド)アッセイ(Lever,Anal.Biochem,47:273,1972)で定量化した。氷上で維持した各酵素サンプルのアリコートを試験して、100%の活性値を判定した。T50温度値を、2時間のインキュベーション後に測定して、残留活性を判定した。データをプロットして、各酵素サンプルについてT50値を判定して、表5に示す。
BspMan5及びその変異体の洗浄性能
人為的な汚れからのLBGの放出を測定するミクロスワッチアッセイで、BspMan5〜15マンナナーゼの洗浄性能を評価した。放出された還元糖を、PAHBAH(p−ヒドロキシ安息香酸ヒドラジド)アッセイ(Lever,Anal.Biochem,47:273,1972)を用いて定量化した。2つのCS−73ミクロスワッチ(直径5.5cm)(CFT,Vlaardingen,Holland)を、平底ノンバインディング96ウェルアッセイプレートの各ウェルに入れた。酵素サンプルを、脱イオン水中に希釈した。表6に、用いた洗剤及び購入場所を一覧にする。表7に、以下が挙げられる、用いた洗剤条件を一覧にする:洗浄アッセイ用の用量、pH、バッファ系(用いる場合)、硬度(3:1 Ca:Mg;ppm)、温度(℃)、及び洗い時間(分)。2.5ppmの最終用量に希釈した酵素、及び洗剤溶液を各ウェルに加えて、総容量を100μlにした。プレートをシールして、洗剤のそれぞれの洗浄条件下でインキュベートした。洗浄評価時間を終えた後、10μlの各反応混合液を、ウェルあたり100μlのPAHBAH溶液を含有するPCRプレートに移した。プレートをシールして、PCR機器内で95℃にて5分間インキュベートした。後に、プレートを25℃に冷却して、80μlの上澄みを、フレッシュな平底MTPに移して、405nmでの吸光度を分光光度計で測定した。405nmでの吸光度の増加を、マンナンベースのCS−73ミクロスワッチに対する洗浄性能の尺度として用いた。結果を、PI値として表8に示す。これは、変異体の吸光度の、BspMan5親酵素について観察された値に対する比率をとることによって算出した。
Claims (32)
- (i)10、19、38、59、60、62、63、66、67、68、70、71、74、75、78、79、80、97、129、131、135、136、143、167、168、184、213、214、225、228、235、242、244、258、259、261、及び283;
(ii)19、38、63、67、71、97、129、143、168、184、225、228、235、244、258、及び261;
(iii)19、38、67、97、129、143、168、184、225、228、235、244、258、及び261;
(iv)19、38、67、129、168、184、225、244、258、及び261;
(v)19、38、67、97、129、168、184、244、258、及び261;
(vi)85、19−85、38−85、67−85、85−129、85−168、85−184、85−225、85−244、85−258、及び85−261;又は
(vii)19−85、38−85、67−85、85−129、85−168、85−184、85−225、85−244、85−258、及び85−261;
から選択される1つ又は複数の位置にて、配列番号2に対する1つ又は複数の変異を含むアミノ酸配列を含むマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片であって:
前記変異の1つ又は複数が、天然に存在しないことを条件とし;
前記変異体、又はその組換えポリペプチド若しくは活性断片のアミノ酸位置は、配列番号2のアミノ酸配列との対応によって番号を付けられている、マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。 - 前記変異体、又はその組換えポリペプチド若しくは活性断片は:
(i)X10Q/T、X19E/V、X38E/I/L/M/Q/R/V、X59D/G/K/N/Q/T、X60F/M/V、X62E/I/Q/V、X63L、X66C/T/V、X67A/D/E/G/P/Q/S/V、X68L/M/R/S/W、X70R/V、X71D/H、X74E/C/Q/V、X75I、X78A/D/L/M、X79E/F/W、X80Q/T、X97E/L/P/Q、X129M、X131P、X135A/C/Q、X136E、X143Q/R、X167L/S/W/Y、X168A/E/G/L/M/S/T、X184D/F/H/L/M/P、X213E、X214C/Q、X225A/C/P/W、X228A/G/H/I/K/S/V/Y、X235G/I/L/Q/S/V、X242S/E、X244A/C/G/L/M/P/S、X258A/D/E/G/M/N/P/T、X259A/E/R/S/W、X261I/M/P/Q/R/S/T/V/W/Y、及びX283G/H/T;
(ii)X19E/V、X38E/I/L/M/Q/R/V、X63L、X67A/D/E/G/P/Q/S/V、X71D/H、X97E/L/P/Q、X129M、X143Q/R、X168A/E/G/L/M/S/T、X184D/F/H/L/M/P、X225A/C/P/W、X228A/G/H/I/K/S/V/Y、X235G/I/L/Q/S/V、X244A/C/G/L/M/P/S、X258A/D/E/G/M/N/P/T、及びX261I/M/P/Q/R/S/T/V/W/Y;
(iii)X19E/V、X38E/I/L/M/Q/R/V、X67A/D/E/G/P/Q/S/V、X97E/L/P/Q、X129M、X143Q/R、X168A/E/G/L/M/S/T、X184D/F/H/L/M/P、X225A/C/P/W、X228A/G/H/I/K/S/V/Y、X235G/I/L/Q/S/V、X244A/C/G/L/M/P/S、X258A/D/E/G/M/N/P/T、及びX261I/M/P/Q/R/S/T/V/W/Y;
(iv)X19E/V、X38E/I/L/M/Q/R/V、X67A/D/E/G/P/Q/S/V、X129M、X168A/E/G/L/M/S/T、X184D/F/H/L/M/P、X225A/C/P/W、X244A/C/G/L/M/P/S、X258A/D/E/G/M/N/P/T、及びX261I/M/P/Q/R/S/T/V/W/Y;
(v)X19E/V、X38E/I/L/M/Q/R/V、X67A/D/E/G/P/Q/S/V、X97E/L/P/Q、X129M、X168A/E/G/L/M/S/T、X184D/F/H/L/M/P、X244A/C/G/L/M/P/S、X258A/D/E/G/M/N/P/T、及びX261I/M/P/Q/R/S/T/V/W/Y;
(vi)X85L、X19E/V−X85L、X38E/I/L/M/Q/R/V−X85L、X67A/D/E/G/P/Q/S/V−X85L、X85L−X129M、X85L−X168A/E/G/L/M/S/T、X85L−X184D/F/H/L/M/P、X85L−X225A/C/P/W、X85L−X244A/C/G/L/M/P/S、X85L−X258A/D/E/G/M/N/P/T、及びX85L−X261I/M/P/Q/R/S/T/V/W/Y;
(vii)X85L、X19E−X85L、X38E−X85L、X67D−X85L、X85L−X129M、X85L−X168S、X85L−X184L、X85L−X225P、X85L−X244L、X85L−X258D、及びX85L−X261R;又は
(viii)X19E−X85L、X38E−X85L、X67D−X85L、X85L−X129M、X85L−X168S、X85L−X184L、X85L−X225P、X85L−X244L、X85L−X258D、及びX85L−X261R;
から選択される、配列番号2に対する1つ又は複数の変異を含み:
Xは、あらゆるアミノ酸である、請求項1に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。 - 前記変異体、又はその組換えポリペプチド若しくは活性断片は:
(i)N/T10Q/T、P19E/V、T38E/I/L/M/Q/R/V、G/S59D/G/K/N/Q/T、L/Q60F/M/V、E/T62E/I/Q/V、K63L、I/L66C/T/V、D/H/N67A/D/E/G/P/Q/S/V、A/T68L/M/R/S/W、K/R70R/V、E/N71D/H、E/N/S74E/C/Q/V、L/V75I、D/Q78A/D/L/M、N79E/F/W、H/K80Q/T、A/N/S97E/L/P/Q、F/Y129M、S/T131P、D/S135A/C/Q、A136E、D/K/Q143Q/R、F/Y167L/S/W/Y、P168A/E/G/L/M/S/T、L/Q184D/F/H/L/M/P、D/N213E、K/Q214C/Q、G/H225A/C/P/W、T228A/G/H/I/K/S/V/Y、A/D/Y235G/I/L/Q/S/V、E/Q242S/E、K/R/Y244A/C/G/L/M/P/S、P/S/T258A/D/E/G/M/N/P/T、E/G/S259A/E/R/S/W、D/E/N261I/M/P/Q/R/S/T/V/W/Y、及びD/G283G/H/T;
(ii)N10Q/T、P19E/V、T38E/I/L/M/Q/R/V、S59D/G/K/N/Q/T、L60F/M/V、T62E/I/Q/V、K63L、L66C/T/V、N67A/D/E/G/P/Q/S/V、A68L/M/R/S/W、K70R/V、N71D/H、N74E/C/Q/V、V75I、Q78A/D/L/M、N79E/F/W、K80Q/T、N97E/L/P/Q、Y129M、T131P、S135A/C/Q、A136E、K143Q/R、F167L/S/W/Y、P168A/E/G/L/M/S/T、Q184D/F/H/L/M/P、N213E、K214C/Q、G225A/C/P/W、T228A/G/H/I/K/S/V/Y、Y235G/I/L/Q/S/V、Q242S/E、K244A/C/G/L/M/P/S、S258A/D/E/G/M/N/P/T、G259A/E/R/S/W、N261I/M/P/Q/R/S/T/V/W/Y、及びD283G/H/T;
(iii)P19E/V、T38E/I/L/M/Q/R/V、K63L、N67A/D/E/G/P/Q/S/V、N71D/H、N97E/L/P/Q、Y129M、K143Q/R、P168A/E/G/L/M/S/T、Q184D/F/H/L/M/P、G225A/C/P/W、T228A/G/H/I/K/S/V/Y、Y235G/I/L/Q/S/V、K244A/C/G/L/M/P/S、S258A/D/E/G/M/N/P/T、及びN261I/M/P/Q/R/S/T/V/W/Y;
(iv)P19E/V、T38E/I/L/M/Q/R/V、D/H/N67A/D/E/G/P/Q/S/V、A/N/S97E/L/P/Q、F/Y129M、D/K/Q143Q/R、P168A/E/G/L/M/S/T、L/Q184D/F/H/L/M/P、G/H225A/C/P/W、T228A/G/H/I/K/S/V/Y、A/D/Y235G/I/L/Q/S/V、K/R/T244A/C/G/L/M/P/S、P/S/T258A/D/E/G/M/N/P/T、及びD/E/N261I/M/P/Q/R/S/T/V/W/Y;
(v)P19E/V、T38E/I/L/M/Q/R/V、N67A/D/E/G/P/Q/S/V、N97E/L/P/Q、Y129M、K143Q/R、P168A/E/G/L/M/S/T、Q184D/F/H/L/M/P、G225A/C/P/W、T228A/G/H/I/K/S/V/Y、Y235G/I/L/Q/S/V、K244A/C/G/L/M/P/S、S258A/D/E/G/M/N/P/T、及びN261I/M/P/Q/R/S/T/V/W/Y;
(vi)P19E/V、T38E/I/L/M/Q/R/V、D/H/N67A/D/E/G/P/Q/S/V、F/Y129M、P168A/E/G/L/M/S/T、L/Q184D/F/H/L/M/P、G/H225A/C/P/W、K/R/T244A/C/G/L/M/P/S、P/S/T258A/D/E/G/M/N/P/T、及びD/E/N261I/M/P/Q/R/S/T/V/W/Y;
(vii)P19E/V、T38E/I/L/M/Q/R/V、N67A/D/E/G/P/Q/S/V、Y129M、P168A/E/G/L/M/S/T、Q184D/F/H/L/M/P、G225A/C/P/W、K244A/C/G/L/M/P/S、S258A/D/E/G/M/N/P/T、及びN261I/M/P/Q/R/S/T/V/W/Y;
(viii)P19E/V、T38E/I/L/M/Q/R/V、N67A/D/E/G/P/Q/S/V、N97E/L/P/Q、Y129M、P168A/E/G/L/M/S/T、Q184D/F/H/L/M/P、K244A/C/G/L/M/P/S、S258A/D/E/G/M/N/P/T、及びN261I/M/P/Q/R/S/T/V/W/Y;
(ix)P/V85L、P19E/V−P/V85L、T38E/I/L/M/Q/R/V−P/V85L、D/H/N67A/D/E/G/P/Q/S/V−P/V85L、P/V85L−F/Y129M、P/V85L−P168A/E/G/L/M/S/T、P/V85L−L/Q184D/F/H/L/M/P、P/V85L−G/H225A/C/P/W、P/V85L−K/R/T244A/C/G/L/M/P/S、P/V85L−P/S/T258A/D/E/G/M/N/P/T、及びP/V85L−D/E/N261I/M/P/Q/R/S/T/V/W/Y;
(x)P85L、P19E/V−P85L、T38E/I/L/M/Q/R/V−P85L、H67A/D/E/G/P/Q/S/V−P85L、P85L−F129M、P85L−P168A/E/G/L/M/S/T、P85L−Q184D/F/H/L/M/P、P85L−H225A/C/P/W、P85L−R244A/C/G/L/M/P/S、P85L−P258A/D/E/G/M/N/P/T、及びP85L−E261I/M/P/Q/R/S/T/V/W/Y;
(xi)P85L、P19E−P85L、T38E−P85L、N/H67D−P85L、P85L−F/Y129M、P85L−P168S、P85L−Q184L、P85L−G/H225P、P85L−K/R244L、P85L−S/P258D、及びP85L−N/E261R;
(xii)P85L、P19E−P85L、T38E−P85L、H67D−P85L、P85L−F129M、P85L−P168S、P85L−Q184L、P85L−H225P、P85L−R244L、P85L−P258D、及びP85L−E261R;又は
(xiii)P19E−P85L、T38E−P85L、H67D−P85L、P85L−F129M、P85L−P168S、P85L−Q184L、P85L−H225P、P85L−R244L、P85L−P258D、及びP85L−E261R
から選択される、配列番号2に対する1つ又は複数の変異を含む、請求項1又は2に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。 - 配列番号2又は配列番号16のアミノ酸配列に対するアミノ酸配列同一性が少なくとも59%又は少なくとも80%であるアミノ酸配列を含む、請求項1〜3のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 配列番号2のアミノ酸配列に対するアミノ酸配列同一性が少なくとも80%であるアミノ酸配列を含むが、ACU30843、ETT37549、WP_036608478、WP_036670707、WP_017688745、WP_053782127、WP_024633848、AAX87003、WP_046227931、WP_017813111、AEX60762、そしてWP_046214462でなく、且つ場合によってはPamMan2、PamMan3、PtuMan2、PpaMan2、そしてPspMan9でないことを条件とする、請求項1〜4のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 配列番号2のアミノ酸配列に対するアミノ酸配列同一性が少なくとも80%であるアミノ酸配列を含むが、ACU30843、ETT37549、WP_036608478、WP_036670707、WP_017688745、WP_053782127、PamMan2、PamMan3、PtuMan2、WP_024633848、PpaMan2、AAX87003、WP_046227931、WP_017813111、PapMan9、AEX60762、WP_046214462、そしてEP2260105−0418でないことを条件とする、マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 前記変異体、又はその組換えポリペプチド若しくは活性断片はさらに:
(i)位置31〜40にてWXaKNDLXXAI(配列番号11)のモチーフ(式中、Xaは、F又はYであり、Xは、あらゆるアミノ酸である);(ii)位置263〜274にてLDXXXGPXGXLT(配列番号12)のモチーフ(式中、Xは、あらゆるアミノ酸である);(iii)位置263〜274にてLDX1V/AT/AGPX2GX3LT(配列番号13)のモチーフ(式中、X1は、M又はLであり、X2は、N、A、又はSであり、X3は、S、T、又はNである);及び(iv)位置263〜274にてLDM/LATGPN/AGS/TLT(配列番号14)のモチーフから選択される1つ又は複数のモチーフを含む、請求項1〜6のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。 - 前記変異体、又はその組換えポリペプチド若しくは活性断片はさらに:
(i)位置31〜40にてWXaKNDLXXAI(配列番号11)のモチーフ(式中、Xaは、F又はYであり、Xは、あらゆるアミノ酸である);(ii)位置263〜274にてLDXXXGPXGXLT(配列番号12)のモチーフ(式中、Xは、あらゆるアミノ酸である);(iii)位置263〜274にてLDX1V/AT/AGPX2GX3LT(配列番号13)のモチーフ(式中、X1は、M又はLであり、X2は、N、A、又はSであり、X3は、S、T、又はNである);及び(iv)位置263〜274にてLDM/LATGPN/AGS/TLT(配列番号14)のモチーフから選択される1つ又は複数のモチーフを含み、
前記変異体、又はその組換えポリペプチド若しくは活性断片のアミノ酸位置は、配列番号2のアミノ酸配列との対応によって番号を付けられているが、前記変異体、又はその組換えポリペプチド若しくは活性断片は、ACU308431、ETT37549、WP_036608478、WP_036670707、WP_017688745、WP_053782127、AAX87003、WP_046227931、WP_024633848、WP_017813111、PspMan9、AEX60762、WP_046214462、YP_003868989、YP_003944884、WP_017427981、AAX87002、WP_009593769、YP_006190599、そしてWP_019912481でなく、且つ場合によってはPamMan2、PamMan3、PtuMan2、そしてPpaMan2でないことを条件とする、請求項1〜7のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。 - 前記変異体、又はその組換えポリペプチド若しくは活性断片はさらに、位置31〜40にてWXaKNDLXXAI(配列番号11)のモチーフを含み、式中、Xaは、Fであり、Xは、あらゆるアミノ酸であり、前記変異体、又はその組換えポリペプチド若しくは活性断片のアミノ酸位置は、配列番号2のアミノ酸配列との対応によって番号を付けられているが、前記変異体、又はその組換えポリペプチド若しくは活性断片は、ACU308431、ETT37549、WP_036608478、WP_036670707、WP_017688745、WP_053782127、WP_024633848、AAX87003、そしてAEX60762でなく、且つ場合によってはPamMan2、PamMan3、PtuMan2、PpaMan2、そしてPspMan9でないことを条件とする、請求項8に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 前記変異体、又はその組換えポリペプチド若しくは活性断片はさらに、位置263〜274にてLDX1V/AT/AGPX2GX3LT(配列番号13)又はLDM/LATGPN/AGS/TLT(配列番号14)のモチーフを含み、式中、X1は、Mであり;X2は、N、A、又はSであり;X3は、S、T、又はNであり、前記変異体、又はその組換えポリペプチド若しくは活性断片のアミノ酸位置は、配列番号2のアミノ酸配列との対応によって番号を付けられているが、前記変異体、又はその組換えポリペプチド若しくは活性断片は、ACU30843、ETT37549、WP_036608478、WP_036670707、WP_017688745、そしてWP_046214462でなく、且つ場合によってはPamMan2でないことを条件とする、請求項8に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 前記変異体、又はその組換えポリペプチド若しくは活性断片はさらに、(i)位置31〜40にてWXaKNDLXXAI(配列番号11)のモチーフ(式中、Xaは、Fであり、Xは、あらゆるアミノ酸である)、及び(ii)位置263〜274にてLDX1V/AT/AGPX2GX3LT(配列番号13)又はLDM/LATGPN/AGS/TLT(配列番号14)のモチーフ(式中、X1は、Mであり;X2は、N、A、又はSであり;X3は、S、T、又はNである)を含み、前記変異体、又はその組換えポリペプチド若しくは活性断片のアミノ酸位置は、配列番号2のアミノ酸配列との対応によって番号を付けられているが、前記変異体、又はその組換えポリペプチド若しくは活性断片は、ACU30843、ETT37549、WP_036608478、WP_036670707、そしてWP_017688745でなく、且つ場合によってはPamMan2でないことを条件とする、請求項8に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 前記マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片は、基準ポリペプチドに由来し、前記基準ポリペプチドは、配列番号2、配列番号8、配列番号9、配列番号10、配列番号15、配列番号16、及び配列番号17から選択される、請求項1〜11のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 前記マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片は、前記基準ポリペプチドのアミノ酸配列とのアミノ酸配列同一性が、少なくとも59%、60%、65%、70%、75%、80%、81%、82%、83%、84%、85%、86%、87%、88%、89%、90%、91%、92%、93%、94%、95%、96%、97%、98%、又は99%である、請求項12に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 前記マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片は、基準ポリペプチドに由来し、前記基準ポリペプチドは、GH5マンナナーゼであり、前記マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片は、場合によっては、GH5マンナナーゼ又はエンド−β−マンナナーゼである、請求項1〜13のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 前記マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片は、マンナナーゼ活性を有する、請求項1〜14のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- マンナナーゼ活性は、界面活性剤及び/又はプロテアーゼの存在下で示される、請求項15に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 前記マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片は、基準ポリペプチドに対して1つ又は複数の特性が向上している、請求項1〜16のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 向上する前記特性は、熱的安定性、洗剤安定性、マンナン基質に対する特異的活性、及び洗浄性能から選択される、請求項17に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 前記マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片はさらに、炭水化物−結合モジュールを含まない、請求項1〜18のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片。
- 請求項1〜19のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片を含む洗浄組成物。
- 少なくとも1つの界面活性剤;カルシウム及び亜鉛から選択される少なくとも1つのイオン;少なくとも1つの補助剤成分;少なくとも1つの安定化剤;約0.001重量%〜約1.0重量%の、請求項1〜19のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片;少なくとも1つの漂白剤;並びに/あるいはアシルトランスフェラーゼ、アミラーゼ、アルファ−アミラーゼ、ベータ−アミラーゼ、アルファ−ガラクトシダーゼ、アラビナーゼ、アラビノシダーゼ、アリールエステラーゼ、ベータ−ガラクトシダーゼ、ベータ−グルカナーゼ、カラギナーゼ、カタラーゼ、セロビオヒドラーゼ、セルラーゼ、コンドロイチナーゼ、クチナーゼ、エンド−ベータ−1,4−グルカナーゼ、エンド−ベータ−マンナナーゼ、エキソ−ベータ−マンナナーゼ、エステラーゼ、エキソ−マンナナーゼ、ガラクタナーゼ、グルコアミラーゼ、ヘミセルラーゼ、ヒアルロニダーゼ、ケラチナーゼ、ラッカーゼ、ラクターゼ、リグニナーゼ、リパーゼ、脂肪分解酵素、リポキシゲナーゼ、マンナナーゼ、オキシダーゼ、ペクチン酸リアーゼ、ペクチンアセチルエステラーゼ、ペクチナーゼ、ペントサナーゼ、ペルヒドロラーゼ、ペルオキシダーゼ、フェノールオキシダーゼ、ホスファターゼ、ホスホリパーゼ、フィターゼ、ポリガラクツロナーゼ、プロテアーゼ、プルラナーゼ、リダクターゼ、ラムノガラクツロナーゼ、ベータ−グルカナーゼ、タンナーゼ、トランスグルタミナーゼ、キシランアセチルエステラーゼ、キシラナーゼ、キシログルカナーゼ、キシロシダーゼ、メタロプロテアーゼ、及びそれら組合せから選択される少なくとも1つの酵素又は酵素誘導体:をさらに含む、請求項20のいずれか一項に記載の洗浄組成物。
- 前記洗浄組成物は、洗濯洗剤、布地柔軟仕上げ洗剤、食器洗い洗剤、及び硬質表面洗浄洗剤から選択される洗剤組成物である、請求項20又は21に記載の洗浄組成物。
- 前記洗浄組成物は、液体、粉末、顆粒状の固体、タブレット、シート、及び単位用量から選択される形態である、請求項20〜22のいずれか一項に記載の洗浄組成物。
- 前記組成物は、ホスフェートを含有し、若しくはホスフェートを含有せず、且つ/又はホウ素を含有し、若しくはホウ素を含有しない、請求項20〜23のいずれか一項に記載の洗浄組成物。
- マンナンを含む汚れ又は染みを含む表面又はアイテムを、(i)請求項1〜19のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片、あるいは(ii)請求項20〜24のいずれか一項に記載の洗浄組成物と接触させることを含み、前記汚れ又は前記染みに含有される前記マンナンは加水分解される、洗浄方法
- 前記アイテムは、皿類又は布地である、請求項25に記載の方法。
- 請求項1〜19のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片をコードする核酸配列を含むポリヌクレオチド。
- 請求項27に記載のポリヌクレオチドを含む発現ベクター。
- 請求項28に記載の発現ベクターを含む宿主細胞。
- 請求項1〜19のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片を生産する方法であって:
(a)請求項28に記載の発現ベクターで請求項29に記載の宿主細胞を安定して形質転換することと;
(b)形質転換された前記宿主細胞を、前記宿主細胞が前記マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片を産生するのに適した条件下で培養することと;
(c)前記マンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片を回収することと
を含む方法。 - 請求項1〜19のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片を含む食品組成物若しくは飼料組成物及び/又は食品添加物。
- 請求項1〜19のいずれか一項に記載のマンナナーゼ変異体、又はその組換えポリペプチド若しくは活性断片の、食品組成物若しくは飼料組成物、並びに/又は食品添加物若しくは飼料添加物、並びに/又は食品若しくは飼料及び/若しくはペットフードの調製における使用。
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WO2017079756A1 (en) | 2017-05-11 |
CN108603183A (zh) | 2018-09-28 |
BR112018009050A2 (pt) | 2018-11-06 |
JP7364330B2 (ja) | 2023-10-18 |
EP3371307A1 (en) | 2018-09-12 |
BR112018009050A8 (pt) | 2019-02-26 |
CN108603183B (zh) | 2023-11-03 |
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