JP2011087582A - 新規変異体egiii様セルラーゼ組成物 - Google Patents
新規変異体egiii様セルラーゼ組成物 Download PDFInfo
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- JP2011087582A JP2011087582A JP2010250662A JP2010250662A JP2011087582A JP 2011087582 A JP2011087582 A JP 2011087582A JP 2010250662 A JP2010250662 A JP 2010250662A JP 2010250662 A JP2010250662 A JP 2010250662A JP 2011087582 A JP2011087582 A JP 2011087582A
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- Prior art keywords
- cellulase
- egiii
- dna
- spp
- cellulases
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Abstract
【解決手段】動作感受性残基が改良された安定性を持つ新規変異体EGIIIまたはEGIII様セルラーゼ。好適には修飾されるべきアミノ酸はトリコデルマレーセイからのEGIII中の残基T2、S3、A8、F10、S18、A24、S25、F30、G31、V36、L38、A42、A46、D47、Q49、Q61、Q64、I65、A66、Q69、A83、S86、S90、V109、T110、Y111、K123、D126、S133、Q134、G135、V139、T145、Q162、N164、T166、Y168、N174、R180、K183、N186、A188、G189、V192、L193、S205、G206、N209、A211、T214および/またはI217の位置に該当する。
【選択図】なし
Description
熱ストレス条件下で改良された性能を持つ新規変異体EGIIIまたはEGIII様セルラーゼ組成物を提供するのが本発明のさらなる目的である。
動物試料添加物として、デンプン処理およびベーキング応用において、バイオマスを減少させるための改良された特性を持つ新規変異体EGIIIまたはEGIII様セルラーゼ組成物を提供するのが本発明のさらなる目的である。
出願者はトリコデルマ レーセイからのEGIIIと相同性を持つセルラーゼファミリーの新規酵素を単離した。これらのセルラーゼの分析により、著しい相同性にもかかわらず、セルラーゼ間で異なった性能を生じる結果となった。特に、フミコーラ インソレンス、フミコーラ グリセア、メムノレラ エキナータ、フサリウム ジャバニクムおよびエメリセラ デセルトルからのEGIII様セルラーゼは熱ストレス条件下で優れた性能を持っていることが発見された。これらのより高い性能を持つEGIII様セルラーゼ中の残基をEGIII中の残基を比較することにより、より安定なセルラーゼおよびEGIII間の残基の相違を同定することが可能であり、より安定なEGIII様セルラーゼの改良された熱安定性に重要である残基が同定される。従って、EGIIIと異なったEGIII様セルラーゼ中の残基を最適化することにより、EGIII様セルラーゼの熱安定性をさらに改良することが可能であろう。同様に、これらの比較的より安定なEGIII様セルラーゼ中の残基とEGIIIまたはより不安定な類似体の残基を比較することにより、より安定なセルラーゼおよびEGIIIまたはより不安定なEGIII様セルラーゼ間における残基の相違を同定することが可能であり、従って、より安定なEGIII様セルラーゼの熱安定性を改良するために重要である残基が同定される。従って、EGIIIまたは他のより不安定なEGIII様セルラーゼ中のこれらの残基を変更することにより、EGIIIの熱安定性をさらに改良することが可能であろう。それ故、本発明は安定性データならびにEGIII様セルラーゼの配列比較により可能になるすべてのそのような修飾を包含している。配列アラインメントは異なったEGIII様セルラーゼを使用して得られるであろうが、配列の数および相同性の程度に依存して一つのアラインメントと別のアラインメントはわずかに異なっているであろう。適切な修飾を決定するために適した実験は、本開示に関係する当業者には日常的なものである。
”セルラーゼ”は本分野の酵素ではよく分類された種類であり、セルロースポリマーをより短いセロオリゴ糖オリゴマー、セロビオースおよび/またはグルコースへ加水分解できる酵素が含まれる。セルラーゼ酵素の共通の例にはエキソ−セロビオヒドロラーゼおよびエンドグルカナーゼが含まれ、セルロース分解性生物(特に真菌および細菌を含んで)の多くの種から得ることが可能である。
(a)Asn−Asn−(Leu/Phe/Lys/IIe)−Trp−Gly
(b)Glu−(Leu/Phe/IIe)−Met−IIe−Trp
(c)Gly−Thr−Glu−Pro−Phe−Thr;
(d)(Ser/Tyr/Cys/Trp/Thr/Asn/Lys/Arg)−(Val/Pro)−(Lys/Ala)−(Ser/Ala)−(Tyr/Phe);および
(e)Lys−Asn−Phe−Phe−Asn−Tyr
の一つまたはそれ以上から成る群より選択されるアミノ酸列を含んでいるアミノ酸配列から成る、セルロース分解活性を持っている酵素が含まれる。一つの態様において、本発明の酵素はさらにEGIIIに対する有意な構造および/または配列相同性を持っている。それ故、本発明の具体化での一つの態様において、酵素はEGIIIに対して少なくとも30%、好適には少なくとも40%および最も好適には少なくとも60%のアミノ酸同一性を持っている。しかしながら、相同性単独では、本明細書に記載された方法により同定された特定の酵素がEGIII様酵素を意味するかどうかの適切な尺度ではないことを認識しなければならない。従って、相同的酵素が実際にここに記載および例示した方法により検出されるが、相同性の程度を本発明の範囲を制限するものとしてみてはならない。
(a)Asn−Asn−(Leu/Phe/Lys/IIe)−Trp−Gly
(b)Glu−(Leu/Phe/IIe)−Met−IIe−Trp
(c)Gly−Thr−Glu−Pro−Phe−Thr;
(d)(Ser/Tyr/Cys/Trp/Thr/Asn/Lys/Arg)−(Val/Pro)−(Lys/Ala)−(Ser/Ala)−(Tyr/Phe);および
(e)Lys−Asn−Phe−Phe−Asn−Tyr
の一つまたはそれ以上から成る群より選択されるアミノ酸列をコードしているDNAプライマーが構築され、確立された方法に従ってセルラーゼ活性を持っている酵素をコード化しているDNA、および遺伝子、を得るために使用された。加えて、本発明のEGIIIは、EGIII様セルラーゼと本明細書同定されたセルラーゼ主鎖の一つを使用して、分子生物学での通常の方法(例えば、PCRクローニング)により得られるであろう。
セルラーゼを除いた加水分解酵素
適した加水分解酵素には、エステル結合に作用するカルボン酸エステル加水分解酵素、チオエステル加水分解酵素、リン酸モノエステル加水分解酵素、およびリン酸ジエステル加水分解酵素;グリコシル化合物に作用するグリコシド加水分解酵素;N−グリコシル化合物を加水分解する酵素;エーテル結合に作用するチオエーテル加水分解酵素;およびペプチド結合に作用するa−アミノ−アシル−ペプチド加水分解酵素、ペプチジル−アミノ酸加水分解酵素、アシル−アミノ酸加水分解酵素、ジペプチド加水分解酵素およびペプチジル−ペプチド加水分解酵素が含まれる。これらの中で好適であるのはカルボン酸エステル加水分解酵素、グリコシド加水分解酵素およびペプチジル−ペプチド加水分解酵素である。適した加水分解酵素には以下のものが含まれる:(1)ペプシン、ペプシンB、レニン、トリプシン、キモトリプシンA、キモトリプシンB、エラスターゼ、エンテロキナーゼ、カテプシンC、パパイン、キモパパイン、フィシン、トロンビン、フィブリノシン、サブチリシン、アスペルギロペプチダーゼA、コラゲナーゼ、クロストリジオペプチダーゼB、カリクレイン、ガストリシン、カテプシンD、ブロメリン、ケラチナーゼ、キモトリプシンC、ペプシンC、アスペルギロペプチダーゼB、ウロキナーゼ、カルボキシペプチダーゼAおよびBおよびアミノペプチダーゼのようなペプチジル−ペプチド加水分解酵素に属しているプロテアーゼ;(2)グリコシド加水分解酵素(必須の構成要素であるセルラーゼはこの群から除かれている)α−アミラーゼ、β−アミラーゼ、グルコアミラーゼ、インベルターゼ、リゾチーム、ペクチナーゼ、キチナーゼおよびデキストラーゼ。これらは酸から中性系で機能するが、細菌から得られたものはアルカリ性系で高い活性を示す;(3)カルボキシルエステラーゼ、リパーゼ、ペクチンエステラーゼおよびクロロフィラーゼを含むカルボン酸エステル加水分解酵素。これらの中で特に有効なのはリパーゼである。
ビルダー
A.二価金属イオン封鎖剤
組成物は以下の化合物のアルカリ金属塩およびアルカノールアミン塩から成る群より選択される一つまたはそれ以上のビルダー成分を約0から約50重量パーセント含んでいるであろう:リン酸塩、ホスホン酸塩、ホスホノカルボン酸塩、アミノ酸の塩、アミノポリ酢酸塩高分子量電解質、非解離性ポリマー、二カルボン酸の塩およびアルミノケイ酸塩。適した二価金属イオン封鎖剤は英国特許出願第2 094 826 Aに開示されている(その開示は本明細書において援用される)。
B.アルカリまたは無機電解質
組成物は、下記の化合物の一つまたはそれ以上のアルカリ金属塩の組成に基づいて、約1から約50重量パーセント、好適には約5から約30重量パーセント、アルカリまたは無機電解質として含んでいるであろう:ケイ酸塩、炭酸塩および硫酸塩ならびにトリエタノールアミン、ジエタノールアミン、モノエタノールアミンおよびトリイソプロパノールアミンのような有機アルカリ。
抗再沈殿剤
組成物は一つまたはそれ以上の下記の化合物を約0.1から約5重量パーセント、抗再沈殿剤として含んでいるであろう:ポリエチレングリコ−ル、ポリビニルアルコール、ポリビニルピロリドンおよびカルボキシメチルセルロース。
漂白剤
一過硫酸カリウム、過炭酸ナトリウム、過ホウ酸ナトリウム、硫酸ナトリウム/過酸化水素付加体および塩化ナトリウム/過酸化水素付加体または/およびスルホン酸化フタロシアニンの亜鉛またはアルミニウム塩のような光感受性漂白色素のような漂白剤と組み合わされた本発明のセルラーゼの使用は洗浄効果をさらに改良する。同様に、EP683 304に開示されているような漂白剤および漂白触媒を使用してもよい。
青味剤および蛍光色素
種々の青味剤および蛍光色素が必要に応じ、組成物へ組み込まれるであろう。適した青味剤および蛍光色素は英国特許出願第2 094 826 Aに開示されている(その開示は本明細書において援用される)。
ケーキング阻害剤
以下のケーキング阻害剤が粉末状洗浄剤に組み込まれるであろう:p−トルエンスルホン酸塩、キシレンスルホン酸塩、酢酸塩、スルホコハク酸塩、タルク、細かく微粉状にしたシリカ、無定形シリカ、粘土、ケイ酸カルシウム(Johns Manville Co.のMicro−Cellのような)、炭酸カルシウムおよび酸化マグネシウム。
セルラーゼ活性を阻害する因子のためのマスキング剤
本発明のセルラーゼ組成物はいくつかの場合、銅、亜鉛、クロム、水銀、鉛、マンガン、または銀イオンまたはそれらの化合物の存在で不活性化される。種々の金属キレート剤および金属沈殿剤がこれらの阻害剤に対して有効である。それらには、例えば、追加の添加物に関して前に掲げたような二価金属イオン封鎖剤ならびにケイ酸マグネシウムおよび硫酸マグネシウムが含まれる。
セルラーゼ活性化剤
活性化剤は特定のセルラーゼに依存して変化するであろう。タンパク質、コバルトおよびその塩、マグネシウムおよびその塩、カルシウムおよびその塩、カリウムおよびその塩、ナトリウムおよびその塩、またはマンノースおよびキシロースのようなモノサッカリドの存在下、多くのセルラーゼは活性化され、それらの洗浄力は顕著に改良される。
抗酸化剤
抗酸化剤には、例えば、tert−ブチル−ヒドロキシトルエン、4,4’−ブチリデンビス(6−tert−ブチル−3−メチルフェノール)、2,2’−ブチリデンビス(6−tert−ブチル−4−メチルフェノール)、一スチレン化クレゾール、一スチレン化フェノール、二スチレン化フェノールおよび1,1−ビス(4−ヒドロキシ−フェニル)シクロヘキサンが含まれる。
可溶化剤
可溶化剤には、例えば、エタノールのような低級アルコール、ベンゼンスルホン酸塩、p−トルエンスルホン酸塩のような低級アルキルベンゼンスルホン酸塩、プロピレングリコールのようなグリコール、アセチルベンゼンスルホン酸塩、アセトアミド、ピリジンカルボン酸アミド、安息香酸塩および尿素が含まれる。
EGIII様セルラーゼをコード化しているゲノムDNAの調製
EGIII様セルラーゼが特定の生物体のDNAによりコード化されているかどうかを決定するPCR反応を行う目的のため、いくつかの異なった微生物でゲノムDNAが調製された。
1)98℃で1分 1サイクル;
2)94℃で1分
40℃で90秒
72℃で1分
3)工程2を30サイクル繰り返す
4)72℃で7分 1サイクル
5)保存およびさらなる分析のため15℃へ温度を下げる。
BOX1:(N/Q)NLWGをコードしているプライマー
正プライマー FRG001:AAY AAY YTN TGG GG
正プライマー FRG002:CAR AAY YTN TGG GG
BOX1’:NNN(F/L/Y/I/L/N/K)WGをコードしているプライマー
正プライマー FRG010:AAY AAY AAY HWI TGG GG
BOX2:ELMIWをコードしているプライマー
正プライマー FRG003:GAR YTN ATG ATH TGG
逆プライマー FRG004:CCA DAT CAT NAR YTC
BOX2’:YELMIWをコードしているプライマー
正プライマー FRG011:TAY GAR YTI ATG ATH TGG
逆プライマー FRG012:CCA DAT CAT IAR YTC RTA
BOX3:GTE(P/C)FTをコードしているプライマー
逆プライマー FRG005:GTR AAN GGY TCR GTR CC
逆プライマー FRG006:GTR AAN GGY TCR GTY CC
逆プライマー FRG007:GTR AAN GGY TCY GTR CC
逆プライマー FRG008:GTR AAN GGY TCY GTY CC
逆プライマー FRG009:GTR AAR CAY TCN GTN CC
PWOポリメラーゼ(Boehringer Mannheim,カタログ番号1644−947)のためのPCR条件は、10マイクロリットルの10X反応緩衝液(10X反応緩衝液は100mMトリス HCl、pH8−8.5;250mM KCl;50 mM (NH4)2SO4;20mM MgSO4を含んでいる);各々0.2mM dATP、dTTP、dGTP、dCTP(最終濃度)、1マイクロリットルの100ナノグラム/マイクロリットル ゲノムDNA、1マイクロリットルのPWO マイクロリットル当たり1単位、500mMプライマー(最終濃度)および水で100マイクロリットルに、から作られた100マイクロリットル溶液から成っている。溶液には鉱物油が層積された。
実施例2
EGIIIおよびEGIII様セルラーゼの温度安定性試験
EGIIIおよびフミコーラ グリセア、フミコーラ インソレンス、エメリセラ デセルトル、フザリウム ジャパニクムおよびメンノニエラ エキナータから誘導されたEGIII様同族体が温度ストレス下での安定性を決定するために試験された。
活性アッセイ:96ウェルマイクロプレートのウェルに、10μlの酵素試料を120μlの基質(4.2mg/ml o−ニトロフェニル セロビオシド)の50mMリン酸カリウム溶液(pH6.7)へ加えた。プレートは40℃で10分間インキュベートし、次に反応を70μlの0.2Mグリシンで停止させた。410nmでの吸光度(基質の酵素的切断により放出されたo−ニトロフェノールによる)をマイクロタイタープレートリーダーで測定した。この終点410nm読みとりは酵素試料中のセルラーゼ活性と比例した。
EGIII様酵素 半減期(分)
H.グリセア 安定
H.インソレンス 安定
E.デセルトル 200
F.ジャパニクム 93
M.エキナータ 192
T.レーセイ(EGIII) 23
”安定”とは200分以内で活性の20%未満の消失を示した。
Claims (19)
- 変異体EGIIIセルラーゼであって、
該変異体EGIIIはトリコデルマ レーセイ(Trichoderma reesei)からのEGIII中の残基T2、S3、A8、F10、S18、A24、S25、F30、G31、V36、L38、A42、A46、D47、Q49、Q61、Q64、I65、A66、Q69、A83、S86、S90、V109、T110、Y111、K123、D126、S133、Q134、G135、V139、T145、Q162、N164、T166、Y168、N174、R180、K183、N186、A188、G189、V192、L193、S205、G206、N209、A211、T214またはI217に対応する1箇所から3箇所の位置での置換または欠失を含む、
変異体EGIIIセルラーゼ。 - 該セルラーゼが真菌、細菌または放線菌類に由来している請求項1に記載のセルラーゼ。
- 該セルラーゼがエンドグルカナーゼである請求項1に記載のセルラーゼ。
- 該真菌が糸状菌である請求項1に記載のセルラーゼ。
- 該糸状菌が真正子嚢菌類に属している請求項4に記載のセルラーゼ。
- 該真正子嚢菌類がアスペルギルスspp.、グリオクラディウムspp.、フザリウムspp.、アクレモニウムspp.、ミセリオフトラspp.、ベルチシリウムspp.、ミロセシウムspp.、ペニシリウムspp.である請求項5に記載のセルラーゼ。
- 請求項1に記載のセルラーゼをコードしているDNA。
- 請求項7のDNAを含んでいるベクター。
- 請求項8のベクターで形質転換された宿主細胞。
- 以下の工程から成るセルラーゼの製造法:(a)セルラーゼを製造するのに適した条件下、適した培養培地中で請求項9に記載の宿主細胞を培養し;(b)該製造されたセルラーゼを得る;および任意に(c)精製されたセルラーゼ製造物を提供するために該セルラーゼを精製する。
- 界面活性剤およびセルラーゼを含んでいる洗浄剤組成物であって、但し該セルラーゼは界面活性剤感受性残基に置換を含んでいる変異体EGIIIセルラーゼから成っている。
- 変異体EGIIIが、トリコデルマ レーセイ(Trichoderma reesei)からのEGIII中の残基T2、S3、A8、F10、S18、A24、S25、F30、G31、V36、L38、A42、A46、D47、Q49、Q61、Q64、I65、A66、Q69、A83、S86、S90、V109、T110、Y111、K123、D126、S133、Q134、G135、V139、T145、Q162、N164、T166、Y168、N174、R180、K183、N186、A188、G189、V192、L193、S205、G206、N209、A211、T214またはI217に対応する1箇所から3箇所の位置での置換または欠失を含む、
変異体EGIIIセルラーゼを含む、請求項11に記載の洗浄剤組成物。 - 該洗浄剤がランドリー洗浄剤である請求項12に記載の洗浄剤組成物。
- 該洗浄剤が皿洗浄剤である請求項12に記載の洗浄剤組成物。
- セルロース含有織物の処理における請求項1に記載の変異体EGIIIセルラーゼの使用。
- 飼料添加物としての請求項1に記載のEGIIIセルラーゼの使用。
- 木材パルプの処理における請求項1に記載のEGIIIセルラーゼの使用。
- グルコースへのバイオマスの減少における請求項1に記載のEGIIIセルラーゼの使用。
- ストーンウォッシングまたはインジゴ染色デニムにおける請求項1に記載のEGIIIセルラーゼの使用。
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Also Published As
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DE69931661T2 (de) | 2007-06-06 |
DK1141336T3 (da) | 2006-10-02 |
EP1141336B1 (en) | 2006-05-31 |
CA2355604A1 (en) | 2000-06-29 |
AU2148100A (en) | 2000-07-12 |
US6268328B1 (en) | 2001-07-31 |
DE69931661D1 (de) | 2006-07-06 |
ES2267310T3 (es) | 2007-03-01 |
EP1141336A2 (en) | 2001-10-10 |
JP2002533071A (ja) | 2002-10-08 |
WO2000037614A3 (en) | 2000-08-03 |
WO2000037614A2 (en) | 2000-06-29 |
ATE328090T1 (de) | 2006-06-15 |
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