JP2018510614A - ラクタムの製造方法 - Google Patents
ラクタムの製造方法 Download PDFInfo
- Publication number
- JP2018510614A JP2018510614A JP2017538309A JP2017538309A JP2018510614A JP 2018510614 A JP2018510614 A JP 2018510614A JP 2017538309 A JP2017538309 A JP 2017538309A JP 2017538309 A JP2017538309 A JP 2017538309A JP 2018510614 A JP2018510614 A JP 2018510614A
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- JP
- Japan
- Prior art keywords
- acid
- lactam
- recombinant microorganism
- beta
- transferase
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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Abstract
Description
1−1:pET30a_his_actベクターの作製
クロストリジウム・プロピオニクム(Clostridium propionicum)菌株由来ベータアラニンコエンザイムAトランスフェラーゼのアミノ酸配列およびこれをコードするact遺伝子の塩基配列は、それぞれ配列番号2および1のようになる。
[配列番号3]ckphisact(NdeI,F):
5’−AGACAGCATATGCACCATCATCATCATCATAAAAGACCCTTGGAAGGTATTCG−3’
[配列番号4]ckpact(SalI,R):
5’−AGACAGGTCGACTTAGATGACATTTTTCTCTTCCAGTGA−3’
ベータアラニンコエンザイムAトランスフェラーゼの精製のために実施例1−1で収得したプラスミドpETa_his_actを大腸菌BL21(DE3)(F−ompT hsdSB(rB− mB−)gal dcm(DE3) a prophage carrying the T7 RNA polymerase gene)(New England Biolabs,米国)に導入した。
Enzyme assayは50mM potassium phosphate buffer(pH7.5)で行った。Enzyme assayに必要な基質および酵素は下記の量で入れた。10mMのGABA、6ACA或いは7AHA、1mMのacetyl−CoA、そして2.5μgの精製されたベータアラニンコエンザイムAトランスフェラーゼを添加して2時間30℃で反応を行って、enzyme assay混合物からcoenzyme A誘導体だけ分離するために、OASIS HLB SPEカートリッジ(Waters,米国)を利用して下記のプロトコルを使用した。
実施例1−3に記述された方法でenzyme assayを行ってGABA coenzyme A、5AVA coenzyme Aおよび6ACA coenzyme Aを製造した。製造したGABA coenzyme A、5AVA coenzyme Aおよび6ACA coenzyme Aを37℃で48時間何の処理なしに放置した後、2−ピロリドン、バレロラクタムおよびカプロラクタムが生成されるか否かHPLC−MSで分析した。
3−1:pTac15k_actベクターの作製
クロストリジウム・プロピオニクム(Clostridium propionicum)菌株の染色体DNAを鋳型にして、配列番号5と6のプライマーでPCRを行って、beta−alanine coenzyme Aをコードするact遺伝子切片を作製した。
[配列番号5]ckpact(EcoRI,F):
5’−AGACAGGAATTCATGAAAAGACCCTTGGAAGGTATT−3’
[配列番号6]ckpact(SacI,R):
5’−AGACAGGTCGACTTAGATGACATTTTTCTCTTCCAGTG−3’
実施例3−1で作製したact切片とtacプロモーターの強い遺伝子発現を行うpEKEx1(Eikmanns et al., Gene. 102, 93-98,1991)プラスミドに制限酵素(EcoRIおよびBamHI)を処理した後、T4 DNAリガーゼを処理して、制限酵素で切断されたact切片およびpEKEx1プラスミドを接合させることによって、組換えプラスミドであるpEKEx_actを作製した(図13)。
大腸菌(Escherichia coli)菌株の染色体DNAを鋳型にして、配列番号8と9のプライマーでPCRを行って、グルタミン酸デカルボキシラーゼをコードするgadB遺伝子切片を作製した。
[配列番号7]ecjgadB(BamHI,RBS,F):
5’−AGACAGGGATCCTTTCACACAGGAAACAATGGATAAGAAGCAAGTAACGGATT−3’
[配列番号8]ecjgadB(SalI,R):
5’−AGACAGGTCGACTCAGGTATGTTTAAAGCTGTTCTGTT−3’
実施例3−2で作製したpEKEx1−actプラスミドおよび実施例3−2で作製したgadB切片に制限酵素(BamHIおよびSalI)を処理した後、T4 DNAリガーゼを処理して、制限酵素で切断されたgadB切片およびpEKEx1_actプラスミドを接合させることによって、組換えプラスミドであるpEKEx_act_gadBを作製した(図15)。
微生物内でbeta−alanine coenzyme A遺伝子をコードするact遺伝子が発現できるよう実施例3−1で作製したpTac15k_actプラスミドを大腸菌WL3110(Lee et al., Mol. Syst. Biol. 3:149 2007)に導入して組換え微生物を製造して(WL3110/pTac15k−act)、空ベクターであるpTac15kが導入された大腸菌(WL3110/pTac15k)を対照群菌株として使用した。
実施例3−5で製造した組換え微生物(WL3110/pTac15k−act)を10mL LB培地に接種して37℃で8時間前培養を行って、前培養した培養液1.5mLを350mLフラスコに50mLの変形MR−1培地に接種して培養した。
この結果から、本発明に係る組換え微生物がGABAを炭素源として利用して2−ピロリドンを成功的に生成することを確認した。
実施例3−5で製造した組換え微生物(WL3110/pTac15k−act)を10mL LB培地に接種して37℃で8時間前培養を行って、前培養した培養液1.5mLを350mLフラスコに50mLの変形MR−2培地に接種して培養した。
この結果から、本発明に係る組換え微生物が5AVAを炭素源として利用してバレロラクタムを成功的に生成することを確認した。
4−1:組換え微生物を利用したグルタミン酸からの2−ピロリドン生成確認
実施例3−5で製造した組換え微生物(WL3110/pTac15k−act)を10mL LB培地に接種して37℃で8時間前培養を行って、前培養した培養液1.5mLを350mLフラスコに50mLの変形M9培地に接種して培養した。
この結果から、本発明に係る組換え微生物がグルタミン酸を炭素源として利用して2−ピロリドンを成功的に生成することを確認した。
実施例3−5で製造した組換え微生物(XQ56/pKE112−davAB/pTac15k−act)を10mL LB培地に接種して37℃で8時間前培養を行って、前培養した培養液1.5mLを350mLフラスコに50mLの変形MR−3培地に接種して培養した。
この結果から、本発明に係る組換え微生物がブドウ糖を炭素源として利用してバレロラクタムを成功的に生成することを確認した。
実施例3−5で製造した組換え微生物(ATCC 13032/pEKEx1_act_gadB)を5mL RG培地(brain heart infusion 40g/L,ブドウ糖10g/L,beef extract 10g/L,sorbitol 30g/L)に接種して30℃で12時間前培養を行って、前培養した培養液1.5mLを350mLフラスコに50mLの変形GP1培地に接種して培養した。
Claims (19)
- ω−アミノ酸生合成代謝経路が内在しているか、ω−アミノ酸生合成代謝経路が導入されている微生物にベータアラニンコエンザイムAトランスフェラーゼをコードする遺伝子が導入されている、ω−アミノ酸からラクタム生成能を有する組換え微生物。
- 前記ベータアラニンコエンザイムAトランスフェラーゼをコードする遺伝子は、クロストリジウム属プロピオニクム(Clostridium propionicum)由来のact遺伝子であることを特徴とする請求項1に記載の組換え微生物。
- 前記ラクタムは、プロピオラクタム(propiolactam)、2−ピロリドン(2−pyrrolidone)、バレロラクタム(valerolactam)、カプロラクタム(caprolactam)、ヘプタノラクタム(heptanolactam)、オクタノラクタム(octanolactam)、ノナノラクタム(nonanolactam)、デカノラクタム(decanolactam)、ウンデカノラクタム(undecanolactam)及びドデカノラクタム(dodecanolactam)で構成された群から選択されることを特徴とする請求項1に記載の組換え微生物。
- 前記ω−アミノ酸は、β−アラニン(beta−alanine)、γ−アミノ酪酸(gamma−aminobutyric acid、GABA)、5−アミノ吉草酸(5−aminovaleric acid、5AVA)、6−アミノカプロン酸(6−aminocaproic acid、6ACA)、7−アミノヘプタン酸(7−aminoheptanoic acid、7AHA)、8−アミノオクタン酸(8−aminooctanoic acid)、9−アミノノナン酸(9−aminonanonoic acid)、10−アミノデカン酸(10−aminodecanoic acid)、11−アミノウンデカン酸(11−aminoundecanoic acid)及び12−アミノドデカン酸(12−aminododecanoic acid)で構成された群から選択されることを特徴とする請求項1に記載の組換え微生物。
- 前記ω−アミノ酸生合成代謝経路は、γ?アミノ酪酸生合成代謝経路であることを特徴とする請求項1に記載の組換え微生物。
- 前記ω−アミノ酸生合成代謝経路は、5−アミノ吉草酸生合成代謝経路であることを特徴とする請求項1に記載の組換え微生物。
- 前記5−アミノ吉草酸生合成代謝経路は、delta−aminovaleramidaseをコードする遺伝子及びlysine 2−monooxygenaseをコードする遺伝子を導入することを特徴とする請求項6に記載の組換え微生物。
- 前記delta−aminovaleramidaseをコードする遺伝子は、シュードモナス・プチダ(Pseudomonas putida)由来のdavA遺伝子であり、前記lysine 2−monooxygenaseをコードする遺伝子は、シュードモナス・プチダ(Pseudomonas putida)由来のdavB遺伝子であることを特徴とする請求項7に記載の組換え微生物。
- 前記ω−アミノ酸は、グルコース、スクロース、ガラクトース、マルトース、キシロース、グリセロール、フルクトース及びサトウキビを含む単糖類、二糖類及び多糖類で構成される群から選択される炭素源から生合成されることを特徴とする請求項1に記載の組換え微生物。
- 前記組換え微生物は、バクテリア、酵母およびカビで構成された群から選択されることを特徴とする請求項1に記載の組換え微生物。
- 下記の段階を含む、ω−アミノ酸からラクタムを製造する方法:
(a)請求項1に記載の組換え微生物をω−アミノ酸の存在下に培養してラクタムを生成する段階;および
(b)前記生成されたラクタムを回収する段階。 - 下記の段階を含む、ベータアラニンコエンザイムAトランスフェラーゼを利用してω−アミノ酸からラクタムを製造する方法:
(a)ω−アミノ酸を含む反応溶液にベータアラニンコエンザイムAトランスフェラーゼを混合した後、反応させてω−アミノアシル−CoAを製造する段階;及び
(b)前記製造されたω−アミノアシル−CoAの環構造形成を介してラクタムを製造する段階。 - 前記ベータアラニンコエンザイムAトランスフェラーゼは、クロストリジウム属プロピオニクム(Clostridium propionicum)由来のact遺伝子によってコードされる酵素であることを特徴とする請求項12に記載のラクタムの製造方法。
- 前記ラクタムは、プロピオラクタム(propiolactam)、2−ピロリドン(2−pyrrolidone)、バレロラクタム(valerolactam)、カプロラクタム(caprolactam)、ヘプタノラクタム(heptanolactam)、オクタノラクタム(octanolactam)、ノナノラクタム(nonanolactam)、デカノラクタム(decanolactam)、ウンデカノラクタム(undecanolactam)及びドデカノラクタム(dodecanolactam)で構成された群から選択されることを特徴とする請求項12に記載のラクタムの製造方法。
- 前記ω−アミノ酸は、β−アラニン(beta−alanine)、γ−アミノ酪酸(gamma−aminobutyric acid、GABA)、5−アミノ吉草酸(5−aminovaleric acid、5AVA)、6−アミノカプロン酸(6−aminocaproic acid、6ACA)、7−アミノヘプタン酸(7−aminoheptanoic acid、7AHA)、8−アミノオクタン酸(8−aminooctanoic acid)、9−アミノノナン酸(9−aminonanonoic acid)、10−アミノデカン酸(10−aminodecanoic acid)、11−アミノウンデカン酸(11−aminoundecanoic acid)及び12−アミノドデカン酸(12−aminododecanoic acid)で構成された群から選択されることを特徴とする請求項12に記載のラクタムの製造方法。
- 下記の段階を含む、ω−アミノ酸からω−アミノアシル−CoAを製造する方法:
(a)請求項1に記載の組換え微生物をω−アミノ酸の存在下に培養してω−アミノアシル−CoAを生成する段階;及び
(b)前記生成されたω−アミノアシル−CoAを回収する段階。 - ω−アミノ酸を含む反応溶液にベータアラニンコエンザイムAトランスフェラーゼを混合した後、反応させて、ω−アミノアシル−CoAを製造する段階を含む、ベータアラニンコエンザイムAトランスフェラーゼを利用してω−アミノ酸からω−アミノアシル−CoAを製造する方法。
- 前記ベータアラニンコエンザイムAトランスフェラーゼは、クロストリジウム属プロピオニクム(Clostridium propionicum)由来のact遺伝子によってコードされる酵素であることを特徴とする請求項17に記載のω−アミノアシル−CoAの製造方法。
- 前記ω−アミノ酸は、β−アラニン(beta−alanine)、γ−アミノ酪酸(gamma−aminobutyric acid、GABA)、5−アミノ吉草酸(5−aminovaleric acid、5AVA)、6−アミノカプロン酸(6−aminocaproic acid、6ACA)、7−アミノヘプタン酸(7−aminoheptanoic acid、7AHA)、8−アミノオクタン酸(8−aminooctanoic acid)、9−アミノノナン酸(9−aminonanonoic acid)、10−アミノデカン酸(10−aminodecanoic acid)、11−アミノウンデカン酸(11−aminoundecanoic acid)及び12−アミノドデカン酸(12−aminododecanoic acid)で構成された群から選択されることを特徴とする請求項17に記載のω−アミノアシル−CoAの製造方法。
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