KR101577134B1 - 젖산 생산이 향상된 미생물 및 이를 이용하여 젖산을 생산하는 방법 - Google Patents
젖산 생산이 향상된 미생물 및 이를 이용하여 젖산을 생산하는 방법 Download PDFInfo
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- KR101577134B1 KR101577134B1 KR1020140055865A KR20140055865A KR101577134B1 KR 101577134 B1 KR101577134 B1 KR 101577134B1 KR 1020140055865 A KR1020140055865 A KR 1020140055865A KR 20140055865 A KR20140055865 A KR 20140055865A KR 101577134 B1 KR101577134 B1 KR 101577134B1
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Abstract
본 발명은 피루베이트 탈탄산효소(pyruvate decarboxylase, PDC)의 활성이 약화되고; 알데히드 탈수소효소(aldehyde dehydrogenase, ALD) 및 acetyl-CoA 합성 효소(acetyl-CoA synthetase, ACS)의 활성이 증진된 젖산을 생산하는 사카로마이세스 속(Saccharomyces sp .) 미생물 및 상기 미생물을 배양하여 그 배양액으로부터 젖산을 생산하는 방법에 관한 것이다.
Description
본 발명은 젖산을 생산하는 재조합 사카로마이세스 속(Saccharomyces sp .) 미생물 및 상기 미생물을 배양하여 그 배양액으로부터 젖산을 생산하는 방법에 관한 것이다.
젖산은 일반적으로 식품 보존제, 향취제 또는 산미제 등의 식품 첨가제로 사용될 뿐만 아니라 화장품, 화학, 금속, 전자, 직물, 염색, 제약 등 산업적으로 광범위하게 이용되는 중요한 유기산이다. 뿐만 아니라 젖산은 생분해성 플라스틱의 일종인 폴리락틱액시드의 원료물질로도 사용되므로, 젖산의 수요가 크게 증가하는 추세이다. 젖산은 폴리락틱액시드 뿐만 아니라 아세트알데히드(acetaldehyde), 폴리프로필렌 글리콜(polypropylene glycol), 아크릴산(acrylic acid), 2,3-펜타디온(2,3-pentathione) 등의 화합물을 생산하는 중요한 원료 물질로도 사용된다. 특히, D형의 젖산은 고내열성 PLA 생산에 필요한 광학적 이성질체로서 이른바 스테레오복합체 PLA (Streocomplex PLA)를 생산하는데 필요한 원료이다.
구체적으로 젖산을 생산하는 방법으로는 전통적인 화학합성법과 생물학적 발효법이 있다. 화학합성법을 이용하여 젖산을 생산할 경우, D형 젖산과 L형 젖산이 50%씩 섞여있는 라세믹(racemic) 혼합물 형태로 생성되고 조성비 조절이 불가능하여 폴리유산을 제조할 경우 용융점이 낮은 무정형의 고분자가 되어 용도 개발 시에도 제한이 많다. 반면, 미생물을 이용한 생물학적 발효법의 경우 사용하는 균주에 따라서 D형 또는 L형의 젖산만을 선택적으로 생산할 수 있어, 상업적으로는 특정 isoform의 젖산을 생산할 수 있는 후자의 생물학적 발효법이 선호된다.
한편, D형 젖산 전환효소의 유전자를 도입함으로써 D형 젖산 생산능이 부여된 사카로마이세스 속 미생물을 기반으로 각종 유전자 조작을 통하여 젖산의 생산율을 높이는 시도가 있어왔다. 구체적으로, 피루베이트 탈탄산효소(pyruvate decarboxylase, PDC), 알데히드 탈수소효소(aldehyde dehydrogenase, ALD) 및/또는 acetyl-CoA 합성 효소(acetyl-CoA synthetase, ACS)를 결손시키고 젖산 탈수소효소(lactate dehydrogenase, LDH)를 강화하여 젖산의 생산을 높이는 시도들이 있어 왔다(미국 공개특허 제2012-021421호, 미국 공개특허 제2010-0248233호, 미국 공개특허 제2006-0148050호). 그러나 상기 젖산 생산 균주는 세포성장이 더뎌짐에 따라 전체적인 발효 생산성이 낮았다.
이에, 본 발명자들은 PDC 역가를 낮추되 세포 성장이 원활하게 이루어져 젖산 생산능이 개선된 미생물을 얻고자 노력한 결과, PDC isotype들의 활성을 조절하고, 알데히드 탈수소효소(aldehyde dehydrogenase, ALD) 및 acetyl-CoA 합성 효소(acetyl-CoA synthetase, ACS)의 활성을 증가시킨 균주에서 젖산 생산 수율이 증가하고 균체 성장이 원활하게 일어나 전체적인 젖산 발효 생산성이 개선되는 것을 확인함으로써, 본 발명을 완성하였다.
본 발명의 하나의 목적은 젖산 생산이 향상된 사카로마이세스 속(Saccharomyces sp .) 미생물을 제공하는 것이다.
본 발명의 다른 목적은 상기 사카로마이세스 속 미생물을 이용하여 젖산을 생산하는 방법을 제공하는 것이다.
상술한 본 발명의 목적을 달성하기 위한 일 양태로서, 본 발명은 (a) 피루베이트 탈탄산효소(pyruvate decarboxylase, PDC)의 활성이 비변이 젖산 생산 균주에 비하여 약화되고; 및 (b) 알데히드 탈수소효소(aldehyde dehydrogenase, ALD) 및 acetyl-CoA 합성 효소(acetyl-CoA synthetase, ACS)의 활성이 비변이 젖산 생산 균주에 비하여 증진된, 젖산 생산이 향상된 사카로마이세스 속(Saccharomyces sp .) 미생물을 제공한다.
일반적으로, 젖산을 생산하는 사카로마이세스 속 미생물은 피루베이트를 기질로 한 젖산 탈수소효소(Lactate lactate dehydrogenase, LDH)를 통하여 생산한다.피루베이트를 공통 기질로 하는 다른 경로들, 대표적으로 알코올 발효 경로(Ethanol ethanol fermentation pathway)와 acetyl-CoA 생성 경로를 차단하였다. 그러나 PDC 활성을 약화하는 것이 젖산 생산과 수율 제고에 도움이 되나 일정 수준을 넘는 정도가 되면 cytosolic acetyl-CoA의 확보가 어려워 세포성장이 불가능하고 따라서 정상적인 발효가 이루어지지 않았다. 이에, 본 발명자들은 최소한의 acetyl-CoA 생성 경로를 유지하는 방법을 통하여 젖산 생산성 수율 증진과 함께 균체 생장율을 유지하여 전체적인 젖산 발효 생산성을 개선함으로써 젖산 생산성이 증가된 사카로마이세스 속 미생물을 개발하였다.
본 발명의 용어, "피루베이트 탈탄산효소(pyruvate decarboxylase, PDC)"는 피루베이트에 작용하여 탄산과 아세트알데히드를 생성하는 반응을 매개하는 활성을 가지는 단백질을 의미하며, 본 발명에서는 상기 활성을 가지는 한 유래나 아형(isotype)에 한정되지 않는다. 상기 단백질은 알코올 발효의 한 단계에 관여하는 것으로 알려져 있으며, 효모나 식물에 주로 존재하는 것으로 알려져 있다. 본 발명의 피루베이트 탈탄산효소는 사카로마이세스 속 미생물에 내재적으로 존재하는 것일 수 있으며, PDC1, PDC5 및/또는 PDC6일 수 있으며, 구체적으로 사카로마이세스 세레비지에의 PDC1, PDC5 및/또는 PDC6일 수 있으나, 이에 한정되지 않는다. 상기 단백질과 생물학적으로 동일하거나 상응하는 활성을 지니는 한, 그의 변이체 또는 유사체 등을 모두 포함할 수 있다. 상기 단백질의 서열은 공지의 데이터 베이스 등에서 얻을 수 있으며, 그 예로 NCBI의 GenBank 등일 수 있으나, 이에 제한되지 않는다. 구체적으로, 상기 PDC1은 서열번호 71의 아미노산 서열, PDC5는 서열번호 72의 아미노산 서열, PDC6는 서열번호 73의 아미노산 서열로 이루어진 것일 수 있으며, 상기 각기 나열된 서열들과 70% 이상의 상동성을 지니는 아미노산 서열, 구체적으로는 80% 이상의 상동성, 보다 구체적으로는 90% 이상의 상동성, 보다 더욱 구체적으로는 95% 이상의 상동성을 가지는 아미노산 서열을 포함한다. 또한, 유전 암호의 축퇴성(genetic code degeneracy)에 기인하여 동일 아미노산 서열을 코딩하는 상기 염기서열들의 변이체 또한 본 발명에 포함된다.
본 발명의 용어, "상동성"이란 다수의 염기서열 또는 다수의 아미노산 서열 사이의 유사한 정도를 나타내기 위한 것으로, 본 발명의 아미노산 서열 또는 염기 서열과 상기와 같은 확률 이상의 동일한 서열을 가지는 서열을 나타내는 단위이다. 이러한 상동성은 두 서열을 육안으로 비교하여 결정할 수도 있으나, 비교대상이 되는 서열을 나란히 배열하여 상동성 정도를 분석해주는 용이하게 이용가능한 서열 비교 프로그램을 사용하여 측정할 수 있다. 당업계에서 용이하게 이용가능한 서열 비교 프로그램은 FASTP, BLAST, BLAST2, PSIBLAST와 CLUSTAL W를 포함하는 소프트웨어 등이 있다.
실제로 가장 주된 역가를 보이는 PDC1을 결손하여 젖산을 생산하는 예는 많이 보고되어 있다 (Appl Microbiol Biotechnol. 2009, 82(5):883-90). 이 경우, PDC6는 거의 발현이 되지 않는다고 여겨지므로 실제 PDC 활성을 가지는 효소는 PDC5 유전자의 발현에 의한 것으로 볼 수 있다. 보고에 따르면 야생형 균주의 경우에서도 PDC1만의 단독 유전자 결손만으로는 세포생장에 대한 저해가 없으며 PDC의 역가도 야생형과 비교하여 60~70% 정도로 유지하고 있기 때문에 균주의 표현형에서의 큰 변화는 없다고 한다 (J Bacteriol. 1990, 172(2):678-685). 한편, 피루베이트에서 PDC와 경쟁하는 LDH 경로로 젖산 생산을 극대화하기 위하여 PDC1, PDC5, PDC6를 동시 결손한 삼중결손균주를 제작할 수 있다. 이 경우, LA 발효수율은 극대화될 수 있겠으나 포도당 존재시 유발되는 기질 제한 효과(catabolite repression) 에 의해 에탄올과 아세트산 등의 대사능이 더욱 제한되어 세포 성장이 저해되고(Curr Genet. 2003, 43(3):139-160) 결국 발효 생산성이 감소된다는 것을 알 수 있다.
PDC6는 거의 발현이 되지 않는다고 여겨지므로 실제 PDC 활성을 가지는 효소는 PDC5 유전자의 발현에 의한 것으로 볼 수 있다. 보고에 따르면 야생형 균주의 경우에서도 PDC1만의 단독 유전자 결손만으로는 세포생장에 대한 저해가 없으며 PDC의 역가도 야생형과 비교하여 60~70% 정도로 유지하고 있기 때문에 균주의 표현형에서의 큰 변화는 없다고 한다 (J Bacteriol. 1990, 172(2):678-685). PDC 활성을 약화할 수 있는 다른 방법으로는 효모에서 주요한 PDC 역가를 담당하는 PDC1, PDC5 유전자가 동시 결손된 이중 결손 균주를 제작할 수 있다. 이 경우에는 아세트산이나 에탄올의 보조기질 없이도 포도당 등의 당원으로 젖산 발효가 가능하나 PDC 역가의 급격한 감소로 균체성장속도가 느려지고 따라서 발효생산성이 감소되는 것을 확인하였다 (Biosci Biotechnol Biochem. 2006,70(5):1148-1153).
구체적으로 본 발명의 피루베이트 탈탄산 효소(PDC)의 약화는 i) PDC1의 활성을 불활성화하고 PDC5의 활성을 약화하거나; 또는 ii) PDC1의 활성을 약화하고 PDC5의 활성을 불활성화하는 것일 수 있다.
본 발명의 구체적인 일 실시예에서는, PDC1을 불활성화한 기반 사카로마이세스 세레비지에 균주를 이용하여, PDC5 유전자의 프로모터를 치환하여 PDC5의 활성을 약화하는 균주, PDC1의 활성을 회복시켜 PDC5를 결손시킨 균주, PDC1 및 PDC5를 이중 결손시킨 균주 및 PDC1, PDC5 및 PDC6를 삼중 결손시킨 균주를 제조하였다. 이 중에 상기 삼중 결손 균주는 균체 생장이 거의 이루어지지 않는 것을 확인하였다.
본 발명의 용어, "알데히드 탈수소효소(aldehyde dehydrogenase, ALD)"는 알데히드를 산화하여 카르복실산 또는 아실기를 생성하는 활성을 가지는 단백질로 주로 아세트알데히드에서 아세트산을 생성하는 활성을 가지는 단백질을 의미하며, 본 발명에서는 상기 활성을 가지는 한 유래나 아형(isotype)에 한정되지 않는다. 본 발명의 알데히드 탈수소효소는 사카로마이세스 속 미생물에서 유래한 것일 수 있으며, ALD2 및/또는 ALD3일 수 있다. 구체적으로는 사카로마이세스 세레비지에의 ALD2 및/또는 ALD3일 수 있으나, 이에 제한되지 않으며, 상기 단백질과 생물학적으로 동일하거나 상응하는 활성을 지니는 한, 그의 변이체 또는 유사체 등을 모두 포함할 수 있다. 상기 단백질의 서열은 공지의 데이터 베이스 등에서 얻을 수 있으며, 그 예로 NCBI의 GenBank 등일 수 있으나, 이에 제한되지 않는다. 구체적으로 상기 ALD2는 서열번호 74의 아미노산 서열, ALD3는 서열번호 75의 아미노산 서열로 이루어진 것일 수 있으며, 상기 각기 나열된 서열들과 70% 이상의 상동성을 지니는 아미노산 서열, 구체적으로는 80% 이상의 상동성, 보다 구체적으로는 90% 이상의 상동성, 보다 더욱 구체적으로는 95% 이상의 상동성을 가지는 아미노산 서열을 포함한다. 또한, 유전 암호의 축퇴성(genetic code degeneracy)에 기인하여 동일 아미노산 서열을 코딩하는 상기 염기서열들의 변이체 또한 본 발명에 포함된다.
본 발명의 용어, "acetyl-CoA 합성 효소(acetyl-CoA synthetase, ACS)"는 ATP 분해 반응과 공역하여 아세트산과 CoA의 티오에스테르화 반응을 촉매하는 활성을 가지는 단백질을 의미하며, 본 발명에서는 상기 활성을 가지는 한 유래나 아형(isotype)에 한정되지 않는다. 미생물, 식물 및 동물 등에도 존재하는 것이 알려져 있다. 본 발명의 알데히드 탈수소효소는 사카로마이세스 속 미생물에서 유래한 것일 수 있으며, ACS1일 수 있다. 구체적으로는, 특히 사카로마이세스 세레비지에의 ACS1일 수 있으나, 이에 제한되지 않으며, 상기 단백질과 생물학적으로 동일하거나 상응하는 활성을 지니는 한, 그의 변이체 또는 유사체 등을 모두 포함할 수 있다. 상기 단백질의 서열은 공지의 데이터 베이스 등에서 얻을 수 있으며, 그 예로 NCBI의 GenBank 등일 수 있으나, 이에 제한되지 않는다. 상기 ACS1은 서열번호 76의 아미노산 서열로 이루어진 것일 수 있으며, 상기 서열과 70% 이상의 상동성을 지니는 아미노산 서열, 구체적으로는 80% 이상의 상동성, 보다 구체적으로는 90% 이상의 상동성, 보다 더욱 구체적으로는 95% 이상의 상동성을 가지는 아미노산 서열을 포함한다. 또한, 유전 암호의 축퇴성(genetic code degeneracy)에 기인하여 동일 아미노산 서열을 코딩하는 상기 염기서열들의 변이체 또한 본 발명에 포함된다.
본 발명의 구체적인 일 실시예에서는, 상기 PDC의 활성을 비변이 미생물보다 약화시킨 균주에 대하여 상기 ALD2 또는 ALD3의 활성을 증진시키고 ACS의 활성을 증진시킨 균주를 제작하였다. 구체적으로는, PDC1을 결손을 통하여 불활성화시키고 PDC5 유전자의 프로모터를 발현능이 낮은 프로모터로 치환하여 PDC5의 활성을 약화시킨 균주를 기반으로 ALD 및 ACS의 활성을 증진시킨 균주를 제작하였다. 더욱 구체적으로는, PDC1의 활성을 불활성화하고 PDC5의 활성을 약화하며, ALD2 및 ALD3로 이루어진 군으로부터 선택된 하나 이상의 활성을 증진시키고, ACS1의 활성을 증진시킨 사카로마이세스 속 미생물을 제작하였다. 이에 따라, 생장 속도, D-젖산 생산량 및 수율이 상당히 개선되는 것을 확인하였다.
본 발명에서 효소 활성의 "불활성화"는 당해 효소의 활성을 불활성화시키는 방법으로 해당 효소가 발현되지 않도록 하거나, 본래의 활성을 발휘할 수 없는 효소가 발현되도록 하는 모든 방법들을 포함한다. 상기 방법들은 상동성 재조합에 의한 유전자 일부 혹은 전체의 결실, 해당 유전자 내부에 외부유래 유전자 삽입에 의한 효소발현 억제, 당해 효소 유전자의 프로모터 서열을 치환 또는 변형시키는 것을 통한 발현 억제이거나, 당해 효소의 치환 또는 변형을 통한 본래 기능을 잃은 불활성 효소로의 변이 등이 있을 수 있으나, 이로 한정되는 것은 아니다.
본 발명에서 효소 활성의 "약화"는 효소의 활성을 약화시키는 방법으로 해당 효소의 발현량을 감소시키거나, 발현되는 효소의 활성을 감소시키는 모든 방법들을 포함한다. 상기 방법들은 당해 효소 유전자의 프로모터 서열을 치환 또는 변형시키는 것을 통한 발현 감소이거나, 당해 효소 치환 또는 변형을 통하여 활성이 감소된 효소로의 변이 등이 있을 수 있으나, 이로 한정되는 것은 아니다.
본 발명에서 효소 활성의 "증진"은 당해 효소의 유전자를 갖는 플라스미드를 도입하거나, 염색체상에서 당해 효소를 코딩하고 있는 유전자의 카피수를 증가시키거나, 당해 효소의 유전자의 프로모터 서열을 치환 또는 변형시키거나, 돌연변이에 의한 효소 활성 증가 등이 있을 수 있을 수 있으나, 이로 한정되는 것은 아니다.
한편, 본 발명의 프로모터는 해당 유전자의 상위 1kb, 터미네이터에 해당하는 하위 1kb까지 포함하는 것일 수 있으나, 이로 한정되는 것은 아니다.
한편, 본 발명의 프로모터는 해당 유전자의 상위 1kb, 터미네이터에 해당하는 하위 1kb까지 포함하는 것일 수 있으나, 이로 한정되는 것은 아니다.
본 발명의 용어, "효모 미생물"은 출아에 의해 증식하는 진균류에 속하는 미생물로, 본 발명의 젖산 생산 경로, 알코올 생산 경로 및/또는 acetyl-CoA 생산 경로를 포함하는 이상 제한되지 않는다. 효모 미생물은 형태에 의해 "사카로마이세스 속", "피치아속", "캔디다 속" 및 "사이카로마이코프시스 속" 등으로 나뉘며, 구체적으로 본 발명에서는 다양한 종을 포함하는 "사카로마이세스 속" 미생물을 활용할 수 있다. 구체적으로 상기 사카로마이세스 속 미생물은 사카로마이세스 바야누스(Saccharomyces bayanus), 사카로마이세스 보울라디(Saccharomyces boulardii), 사카로마이세스 불데리(Saccharomyces bulderi), 사카로마이세스 카리오카누스(Saccharomyces cariocanus), 사카로마이세스 카리오커스(Saccharomyces cariocus), 사카로마이세스 세레비지에(Saccharomyces cerevisiae), 사카로마이세스 시바리에리(Saccharomyces chevalieri), 사카로마이세스 다이레넨시스(Saccharomyces dairenensis), 사카로마이세스 엘립소이더스(Saccharomyces ellipsoideus), 사카로마이세스 유바야누스(Saccharomyces eubayanus), 사카로마이세스 엑시구스(Saccharomyces exiguus), 사카로마이세스 플로렌티누스(Saccharomyces florentinus), 사카로마이세스 클루이베리(Saccharomyces kluyveri), 사카로마이세스 마르티니에(Saccharomyces martiniae), 사카로마이세스 모나센시스(Saccharomyces monacensis), 사카로마이세스 노르벤시스(Saccharomyces norbensis), 사카로마이세스 파라독수스(Saccharomyces paradoxus), 사카로마이세스 파스토리아누그(Saccharomyces pastorianus), 사카로마이세스 스펜세로럼(Saccharomyces spencerorum), 사카로마이세스 츄리센시스(Saccharomyces turicensis), 사카로마이세스 유니스포러스(Saccharomyces unisporus), 사카로마이세스 우바럼(Saccharomyces uvarum), 및 사카로마이세스 조나투스(Saccharomyces zonatus)로 이루어진 군으로부터 선택된 것일 수 있으며, 더욱 구체적으로는 사카로마이세스 세레비지에일 수 있다.
본 발명자들은 사카로마이세스 속 미생물의 대표적인 예로 사카로마이세스 세레비지에에서 PDC의 활성 약화와 ALD 및 ACS 활성이 증진된 미생물을 제조한 결과, 젖산 생산이 크게 증가된 것을 확인하였다.
본 발명의 미생물은 알코올 탈수소효소(alcohol dehydrogenase, ADH)가 추가로 불활성화된 것일 수 있다.
본 발명의 용어, "알코올 탈수소효소(alcohol dehydrogenase)"는 알코올에서 수소를 이탈시켜 알데히드 또는 케톤을 생성하는 반응을 가역적으로 촉매하는 활성을 가지는 단백질을 의미하며, 본 발명에서는 상기 활성을 가지는 한 유래나 아형(isotype)에 한정되지 않는다. 본 발명의 알코올 탈수소효소는 사카로마이세스 속 미생물에서 유래한 것일 수 있으며, ADH1일 수 있다. 구체적으로 사카로마이세스 세레비지에의 ADH1일 수 있으나, 이에 제한되지 않으며, 상기 단백질과 생물학적으로 동일하거나 상응하는 활성을 지니는 한, 그의 변이체 유사체 등을 모두 포함할 수 있다. 상기 단백질의 서열은 공지의 데이터 베이스 등에서 얻을 수 있으며, 그 예로 NCBI의 GenBank 등일 수 있으나, 이에 제한되지 않는다. 상기 ADH1은 서열번호 77의 아미노산 서열로 이루어진 것일 수 있으며, 상기 서열과 70% 이상의 상동성을 지니는 아미노산 서열, 구체적으로는 80% 이상의 상동성, 보다 구체적으로는 90% 이상의 상동성, 보다 더욱 구체적으로는 95% 이상의 상동성을 가지는 아미노산 서열을 포함한다. 또한, 유전 암호의 축퇴성(genetic code degeneracy)에 기인하여 동일 아미노산 서열을 코딩하는 상기 염기서열들의 변이체 또한 본 발명에 포함된다.
본 발명의 미생물은 D-젖산 탈수소효소(d-lactate dehydrogenase, DLD)가 추가로 불활성화된 것일 수 있다.
본 발명의 용어, "D-젖산 탈수소효소(d-lactate dehydrogenase)"는 D-젖산을 탈수소화하여 피루베이트를 생성하는 활성을 가지는 단백질을 의미하며, 본 발명에서는 상기 활성을 가지는 한 유래나 아형(isotype)에 한정되지 않는다.본 발명의 D-젖산 탈수소효소는 사카로마이세스 속 미생물에서 유래한 것일 수 있으며, 구체적으로는 DLD1일 수 있다. 구체적으로는 사카로마이세스 세레비지에의 DLD1일 수 있으나, 이에 제한되지 않으며, 상기 단백질과 생물학적으로 동일하거나 상응하는 활성을 지니는 한, 그의 변이체 유사체 등을 모두 포함할 수 있다. 상기 단백질의 서열은 공지의 데이터 베이스 등에서 얻을 수 있으며, 그 예로 NCBI의 GenBank 등일 수 있으나, 이에 제한되지 않는다. 상기 DLD1은 서열번호 78의 아미노산 서열로 이루어진 것일 수 있으며, 상기 서열과 70% 이상의 상동성을 지니는 아미노산 서열, 구체적으로는 80% 이상의 상동성, 보다 구체적으로는 90% 이상의 상동성, 보다 더욱 구체적으로는 95% 이상의 상동성을 가지는 아미노산 서열을 포함한다. 또한, 유전 암호의 축퇴성(genetic code degeneracy)에 기인하여 동일 아미노산 서열을 코딩하는 상기 염기서열들의 변이체 또한 본 발명에 포함된다.
본 발명에서는, 추가적으로 피루베이트로부터 생성된 알데히드를 기질로 활용하는 알코올 발효 경로에 작용하는 ADH1을 결손시키고, 생성된 D-젖산을 분해하는 효소인 DLD1을 결손시킨 균주를 이용하였으며, 이는 아세트산 생성 경로 조절에 따른 젖산 발효 생성능의 변화를 명확하게 측정하기 위해서이다. 본 발명의 구체적인 실시예에서 제조된 PDC와 ALD 및 ACS의 활성을 조절한 본 발명의 균주들은 현저히 증진된 젖산 발효 생산능을 보였다(표 12).
본 발명의 또 다른 일 양태는, 상기 본 발명의 미생물을 이용하여 젖산을 생산하는 방법을 제공한다.
구체적으로, 본 발명의 구체적 예로 본 발명의 미생물을 배양하는 단계; 및 상기 단계의 배양으로부터 젖산을 회수하는 단계를 포함하는 젖산 생산 방법을 제공한다.
본 발명의 상기 배양과정은 당업계에 알려진 적당한 배지와 배양조건에 따라 이루어질 수 있다. 이러한 배양 과정은 당업자라면 선택되는 균주에 따라 용이하게 조정하여 사용할 수 있다. 상기 배양방법의 예에는 회분식, 연속식 및 유가식 배양이 포함되나, 여기에 한정되는 것은 아니다. 배양에 사용되는 배지는 특정한 균주의 요구 조건을 적절하게 만족시켜야 한다.
본 발명에서 사용되는 배지는 수크로오스 또는 글루코오스를 주 탄소원으로 사용하며, 수크로오스를 다량으로 포함한 당밀 또한 탄소원으로 이용될 수 있으며, 그 외의 적정량의 탄소원은 다양하게 이용될 수 있다. 사용될 수 있는 질소원의 예는 펩톤, 효모 추출물, 육즙, 맥아 추출물, 옥수수 침지액, 및 대두밀과 같은 유기 질소원 및 요소, 황산암모늄, 염화암모늄, 인산암모늄, 탄산안모늄, 및 질산암모늄과 같은 무기질소원이 포함될 수 있다. 이들 질소원은 단독 또는 조합되어 사용될 수 있다. 상기 배지에는 인원으로서 인산이수소칼륨, 인산수소이칼륨 및 대응되는 소듐-함유 염이 포함될 수 있다. 또한, 황산마그네슘 또는 황산 철과 같은 금속염을 포함할 수 있다. 그 외에 아미노산, 비타민 및 적절한 전구체 등이 포함될 수 있다. 이들 배지 또는 전구체는 배양물에 회분식 또는 연속식으로 첨가될 수 있다.
배양 중에 수산화암모늄, 수산화칼륨, 암모니아, 인산 및 황산과 같은 화합물을 배양물에 적절한 방식으로 첨가하여, 배양물의 pH를 조정할 수 있다. 또한 배양 중에는 지방산 폴리클리콜 에스테르와 같은 소포제를 사용하여 기포 생성을 억제할 수 있다. 또한 배양물의 호기 상태를 유지하기 위하여, 배양물 내로 산소 또는 산소 함유 기체를 주입하거나 혐기 및 미호기 상태를 유지하기 위해 기체의 주입 없이 혹은 질소, 수소 또는 이산화탄소 가스를 주입할 수 있다.
배양물의 온도는 보통 20℃ 내지 40℃, 구체적으로는 25℃ 내지 35℃, 더욱 구체적으로는 30℃일 수 있다. 배양 기간은 원하는 유용 물질의 생성량에 도달할 때까지 계속 할 수 있으며, 구체적으로는 10 내지 100 시간일 수 있다.
본 발명의 상기 배양 단계에서 생산된 젖산은 배양방법, 예를 들어 회분식, 연속식 또는 유가식 배양 방법 등에 따라 당해 분야에 공지된 적합한 방법을 이용하여 배양액으로부터 회수될 수 있다.
본 발명은 PDC isotype들의 활성을 조절하고, 알데히드 탈수소효소(aldehyde dehydrogenase, ALD) 및 acetyl-CoA 합성 효소(acetyl-CoA synthetase, ACS)의 활성을 증가시켜 젖산 발효 생산능이 개선된 미생물을 이용에 관한 것으로, 젖산 발효 생산 분야에서 널리 활용될 수 있다.
도 1은 사카로마이세스 속 미생물의 젖산 생산 경로, 알코올 발효 경로 및 acetyl-CoA 생산 경로 간의 관계를 도식화한 도이다.
이하 본 발명을 실시예를 통하여 보다 상세하게 설명한다. 그러나 이들 실시예는 본 발명을 예시적으로 설명하기 위한 것으로, 본 발명의 범위가 이들 실시예에 한정되는 것은 아니다.
실시예
1: 젖산 생산 균주 제작
본 발명의 젖산 생산 균주를 제작하기 위하여, EUROSCARF에서 분양 받은 야생형 효모 중 대표적인 Saccharomyces cerevisiae CEN.PK2-1D에 일련의 유전자 조작을 가하였다.
구체적으로는, 알코올 합성 경로로의 피루베이트의 이탈을 최소화하기 위하여 알코올 탈수소효소 1(alcohol dehydrogenase 1; ADH1) 및 피루베이트 탈탄산효소 1(pyruvate decarboxylase 1; PDC1)을 결손시키고, D형 젖산 분해 경로의 차단을 위해 D-젖산 탈수소효소 1(d-lactate dehydrogenase 1; DLD1)을 결손한 균주를 본 발명의 기반 균주로 사용하였다.
DLD1은 생장 개선에 직접적인 영향을 미치는 요소는 아니나 D형 젖산의 탈수소효소로 NAD+를 이용하여 피루베이트로 전환시키는 주된 효소로 알려져 있다. 따라서, 본 발명에서 제작하고자 하는 D형 젖산 생산 효모의 온전한 발효 생산성 비교를 위하여 생산된 젖산을 소모하는 효소인 DLD1 유전자를 결손한 균주를 기반으로 후속 균주를 제작하여, 발효 생산성을 비교하였다.
본 발명의 유전자 조작은 일반적인 molecular cloning 방법을 이용하였다.
먼저, 효모의 ADH1 및 PDC1 유전자 결손에 관한 실험은 Lee TH, et al.(J. Microbiol. Biotechnol. (2006), 16(6), 979-982) 논문에 개시된 내용을 참고로 하여 pWAL100 및 pWBR100 플라스미드를 이용하였다. 벡터에 삽입한 각 insert는 각각에 해당하는 프라이머(서열번호 1 내지 서열번호 8)를 이용하여 PCR을 통해 제조하였다.
또한, DLD1의 유전자 결손을 위하여 HIS3 마커 유전자를 double crossover로 도입하여 결손시켰다. 이에 사용된 DNA 단편은 서열번호 9 및 서열번호 10의 프라이머를 이용하여 제조하였다.
상기 유전자 조작에 사용한 프라이머를 정리하면 하기 표 1과 같다.
프라이머 | 5'-> 3' 서열 |
ADH1 upstream forward primer (서열번호 1) |
CGGGATCCACTGTAGCCCTAGACTTGATAGCC |
ADH1 upstream reverse primer (서열번호 2) |
ATAAGAATGCGGCCGCTGTATATGAGATAGTTGATTGTATGCTT |
ADH1 downstream forward primer (서열번호 3) |
GACTAGTGCGAATTTCTTATGATTTATGATTTTTATT |
ADH1 downstream reverse primer (서열번호 4) |
ACATGCCATGgAAGCATGCACGTATACACTTGAGTAA |
PDC1 upstream forward primer (서열번호 5) |
CGGGATCCATTATGTATGCTCTTCTGACTTTTCGT |
PDC1 upstream reverse primer (서열번호 6) |
ATAAGAATGCGGCCGCTTTGATTGATTTGACTGTGTTATTTTGC |
PDC1 downstream forward primer (서열번호 7) |
CGGGATCCGCGATTTAATCTCTAATTATTAGTTAAAG |
PDC1 downstream reverse primer (서열번호 8) |
ATAAGAATGCGGCCGCTTTCAATCATTGGAGCAATCATTTTACA |
DLD1-HIS3 upstream linking primer (서열번호 9) |
GCGTAGTTGGCCCCAACTGGTGCAGTAATACGTTTTAAGAGCTTGGTGAG |
DLD1-HIS3 downstream linking primer (서열번호 10) |
CGTGAAGGGTGAAAAAGGAAAATCAGATACCTACATAAGAACACCTTTGG |
상기와 같이 3개의 유전자를 결손시킨 균주를 바탕으로 젖산 생산을 위한 유전자인 D-젖산 탈수소효소(d-lactate dehydrogenase, D-LDH)를 도입하였다. S.cerevisiae 유래의 TEF1 프로모터와 CYC1 터미네이터 사이에 락토바실러스 플란타럼(Lb . plantarum) 유래 ldhD 유전자를 함유하도록 각각 5', 3' 말단에 XhoⅠ과 SpeⅠ의 제한효소 사이트를 가지고 p413TEF1 벡터에 클로닝하였으며 여기서 SacⅠ/PvuⅡ의 이중 절단으로 insert를 준비하였다. 그리고 벡터는 p-δ-neo에서 BamHⅠ/NotⅠ으로 이중 절단된 DNA 절편에서 Mungbean nuclease로 blunt end를 만든 다음, 다시 SacⅠ으로 처리하여 SacⅠ sticky end와 BamHⅠ 유래 blunt end를 갖는 벡터 부분을 만들었다.
상기의 과정으로 수득한 벡터와 insert를 ligation하여 pTL573 벡터를 완성하였다. pTL573 플라스미드는 Lb . plantarum 유래 ldhD 유전자를 포함하고 있으며, S.cerevisiae CEN.PK2-1D pdc1Δ adh1Δ dld1Δ 균주의 retrotransposable element 중 일부 영역인 δ-sequence에 무작위적으로 다수의 카피가 삽입되도록 설계되었다. 해당 유전자의 다중 삽입을 위하여 플라스미드 pTL573을 SalⅠ 제한효소로 절단하여 δ-sequence 상에 single crossover를 유도하는 DNA 단편을 제작하였다. 이를 형질전환으로 모균주 내에 도입하여 최대 5 mg/mL G418 농도의 YPD (1 % yeast extract, 2% bacto-peptone, 2% glucose) 배지에서 다수의 콜로니들을 얻었다. 이렇게 얻어진 균주는 최종적으로 D형 젖산 생산능 부여를 위해 락토바실러스 플란타럼(Lb . plantarum) 유래의 D-LDH가 복수로 삽입되어 있는 것을 확인하였으며, 이를 CC02-0064 균주라 명명하였다.
실시예
2:
PDC5
약화 변이 균주 제조
상기 실시예 1에서 제조한 CC02-0064 균주를 기반으로 PDC5의 프로모터를 치환한 변이 균주를 제조하였다. 이 과정에서 카세트 제작 및 균주 선별 과정은 Lee T. H. et al.(Development of reusable split URA3-marked knockout vectors for budding yeast, Saccharomyces cerevisiae. J Microbiol Biotechnol, 2006, 16:979-982)에 기재된 방법을 사용하였다.
구체적으로는 CC02-0064 균주의 PDC5의 프로모터를 SCO1, SCO2, ACS1, IDP2, FBA1 프로모터로 치환한 총 5개의 신규 균주를 제작하였으며, 이에 서열번호 11 내지 서열번호 36의 프라이머를 이용하여 프로모터 치환 카세트를 제작하였다.
상기 프로모터 치환에 사용한 프라이머를 정리하면 하기 표 2과 같다.
프라이머 | 5'-> 3' 서열 |
F_PDC5_UP_676 (서열번호 11) |
GTCAGCATTGACACGTTCGATT |
R_KlURA3-PDC5_UP (서열번호 12) |
TCTACCCAGAATCACTTCTTTCGAGAGATTGTCATAATC |
F_PDC5_UP-AL_KlURA3 (서열번호 13) |
CAATCTCTCGAAAGAAGTGATTCTGGGTAGAAGATCGG |
R_AL_KlURA3 (서열번호 14) |
GAGCAATGAACCCAATAACGAAATCTT |
F_BR_KlURA3 (서열번호 15) |
CTTGACGTTCGTTCGACTGATGAG |
R_PDC5_DOWN_522 (서열번호 16) |
CAAGTCAACCAAGTTAGCTGGC |
R_SCO1p-BR_KlURA3 (서열번호 17) |
CTCTCCTAATAGACGTGGTGTCACCATGAACGACAATTCTTAA |
F_SCO1p_500 (서열번호 18) |
CGTTCATGGTGACACCACGTCTATTAGGAGAGCCATTC |
R_PDC5_DOWN_500-SCO1p (서열번호 19) |
AAGGTTATTTCAGACATCTTTTCTACGTTTGCTGTTTTTTC |
F_SCO1p-PDC5_DOWN_500 (서열번호 20) |
CAGCAAACGTAGAAAAGATGTCTGAAATAACCTTAGGTAAAT |
R_SCO2p-BR_KlURA3 (서열번호 21) |
ATCGAATAAGTAACAAGCGTGTCACCATGAACGACAATTCTTAA |
F_SCO2p_500 (서열번호 22) |
CGTTCATGGTGACACGCTTGTTACTTATTCGATAACGC |
R_PDC5_DOWN_500-SCO2p (서열번호 23) |
AAGGTTATTTCAGACATTTTACTCTCGCTTCCCAAATTCC |
F_SCO2p-PDC5_DOWN_500 (서열번호 24) |
GGAAGCGAGAGTAAAATGTCTGAAATAACCTTAGGTAAAT |
R_IDP2p-BR_KlURA3 (서열번호 25) |
TAAAAATAAATAGATAGACGTGTGTCACCATGAACGACAATTCTTAA |
F_IDP2p_500 (서열번호 26) |
CGTTCATGGTGACACACGTCTATCTATTTATTTTTATAACTC |
R_PDC5_DOWN_500-IDP2p (서열번호 27) |
AAGGTTATTTCAGACATTACGATTTTATATATATACGTACGTTA |
F_IDP2p-PDC5_DOWN_500 (서열번호 28) |
CGTATATATATAAAATCGTAATGTCTGAAATAACCTTAGGTAAAT |
R_ACS1p-BR_KlURA3 (서열번호 29) |
CTGGACGTATGTGCACAGTGTCACCATGAACGACAATTCTTAA |
F_ACS1p_500 (서열번호 30) |
CGTTCATGGTGACACTGTGCACATACGTCCAGAATGAT |
R_PDC5_DOWN_500-ACS1p (서열번호 31) |
AAGGTTATTTCAGACATAGCACAGTGGGCAATGTCTTTC |
F_ACS1p-PDC5_DOWN_500 (서열번호 32) |
CATTGCCCACTGTGCTATGTCTGAAATAACCTTAGGTAAAT |
R_FBA1p-BR_KlURA3 (서열번호 33) |
TTATTTACGTAATGACCCAGTGTCACCATGAACGACAATTCTTAA |
F_FBA1p_500 (서열번호 34) |
CGTTCATGGTGACACTGGGTCATTACGTAAATAATGATAG |
R_PDC5_DOWN_500-FBA1p (서열번호 35) |
AAGGTTATTTCAGACATTTTGAATATGTATTACTTGGTTATGGT |
F_FBA1p-PDC5_DOWN_500 (서열번호 36) |
CCAAGTAATACATATTCAAAATGTCTGAAATAACCTTAGGTAAAT |
상기와 같이 제작한 신규 균주를 CC02-0167, CC02-0168, CC02-0169, CC02-0170, CC02-0174으로 명명하였다. 해당 균주와 유전 형질을 정리하면 하기 표 3과 같다.
균주명 | 유전형질 |
CC02-0167 | CC02-0064 PDC5 promoter::KlURA3-SCO1 promoter |
CC02-0168 | CC02-0064 PDC5 promoter::KlURA3-SCO2 promoter |
CC02-0169 | CC02-0064 PDC5 promoter::KlURA3-ACS1 promoter |
CC02-0170 | CC02-0064 PDC5 promoter::KlURA3-IDP2 promoter |
CC02-0174 | CC02-0064 PDC5 promoter::KlURA3-FBA1 promoter |
실시예
3:
PDC5
약화 변이 균주의 젖산 발효 평가
상기 실시예 2에서 제작한 PDC5 프로모터 변이 균주에 대하여 젖산 발효 평가를 하였다. 이를 위해서 젖산 발효 평가용 배지를 제작하였다.
구체적으로는, 효모용 제한배지인 SC media(Synthetic Complex media)를 제작하기 위하여 0.67 % yeast nitrogen base without amino acid를 기반으로 여기에 아미노산 dropout mix(Sigma)를 제조사의 프로토콜에 따라 혼합하고 필요에 따라, 제외된 아미노산을 첨가하였다. 류신(leucine)은 380 mg/L, 우라실, 트립토판 및 히스티딘은 76 mg/L가 되게 첨가하였고, 탄소원으로서 포도당 8%와 중화제로서 1% CaCO3를 첨가하였다. 이렇게 제조한 배지를 효모 균주 젖산 발효 평가에 이용하였다.
상기 실시예 2에서 제작한 PDC5 프로모터 변이 균주 중에서 본래 PDC5 프로모터보다 약한 프로모터로 변이된 균주들은 성장을 하지 못하고, 강한 프로모터로 변이된 균주는 더 잘 자랐다. 구체적으로는 본래 PDC5 프로모터보다 약한 프로모터인 SCO1, SCO2, IDP2 또는 ACS1 프로모터로 치환한 균주들은 성장하지 못하였고, FBA1 프로모터로 교체한 균주만이 생장하여 평가가 가능하였다. 상기 측정이 가능한 CC02-0064와 CC02-0174 균주의 젖산 발효 평가한 결과를 정리하면 하기 표 4와 같다.
균주 | 24 시간 | 48 시간 | |||||
OD | 소모당 | 젖산 | OD | 소모당 | 젖산 | 수율(%) | |
CC02-0064 | 3.9 | 15.0 | 10.9 | 8.7 | 63.4 | 41.6 | 65.7 |
CC02-0174 | 5.7 | 25.0 | 19.8 | 9.4 | 69.9 | 47.3 | 67.7 |
상기 젖산 발효 평가에서 확인할 수 있듯이, acetyl-CoA의 생성을 촉진하는 경로 중에서 PDC를 야생형의 PDC5 프로모터에서 FBA1 프로모터로 교체한 균주 CC02-0174로도 본래 균주(CC02-0064)보다 균체 생장 속도 및 젖산 생산성이 향상되는 것을 확인하였다. 그러나 이는 시료를 채취한 24시간 및 48시간에서의 결과를 비교해 볼 때, acetyl-CoA 생성 경로 중에서 하위 ALD와 ACS의 강화 없이 단순히 PDC의 단독 역가 강화만으로는 시간에 따른 균체 생장 속도 및 젖산 생산성의 향상이 지속적으로 감소한다는 것도 확인할 수 있었다. 본 실시예에서 PDC 역가 강화에 의한 포도당 소모능 향상은 10.3%이고 최대 젖산 생산 농도는 47.3 g/l이었다. 결과적으로 이 때의 최종 젖산 생산성 향상은 약 13.7%이었다.
실시예
4 :
PDC5
결손 균주 제작
상기 실시예 2에서 제작한 PDC1을 결손시키고 PDC5를 약화시킨 균주 외에, 반대로 PDC5를 결손시키고 PDC1을 약화시킨 균주를 제작하여, 해당 균주에서도 PDC 경로가 약화되는지를 확인해보고자 하였다.
구체적으로는, CC02-0064 균주를 기반으로 하여 PDC5 유전자의 결손을 위하여 서열번호 37 내지 40의 프라이머를 이용하여 PDC5 결손 카세트를 제작하였으며, 결손 균주는 실시예 1에 명시된 문헌과 동일한 방법으로 제작하였다. 이에 사용된 프라이머를 정리하면 하기 표 5와 같다.
프라이머 | 5'-> 3' 서열 |
F-ALPDC5-BamHI (서열번호 37) |
GAGCTCGGATCCAAGGAAATAAAGCAAATAACAATAACACC |
R-ALPDC5-NotI (서열번호 38) |
ACCATGGCGGCCGCTTTGTTCTTCTTGTTATTGTATTGTGTTG |
F-BRPDC5-SpeI (서열번호 39) |
GGATCCACTAGTGCTAATTAACATAAAACTCATGATTCAACG |
R-BRPDC5-NcoI (서열번호 40) |
CAGCTGCCATGGTATTCTAAATAAGATGTAAGGCCTTGTAAT |
이렇게 제작한 PDC5 결손 균주는 CC02-0450(CC02-0064, pdc5Δ)이라 명명하였다.
실시예
5 :
PDC5
결손 균주 기반
PDC1
프로모터 변이 균주 제작
상기 실시예 4에서 제작한 CC02-0450 균주를 기반으로 하여 PDC1 프로모터를 치환한 균주를 제작하였다. 이를 위하여 PDC1 결손을 회복시킨 비교군 균주인 CC02-0451(CC02-0450, PDC1p-PDC1)을 제작하였으며, 실험군으로 PDC1 약화 균주인 CC02-0452(CC02-0450, IDP1p-PDC1)를 제작하였다.
각 균주는 효모에서의 복제 원점이 없는 pRS406 벡터에 목적 유전자 카세트를 클로닝한 pRS406-PDC1p-PDC1-CYC1t와 pRS406-IDP2p-PDC1-CYC1t 벡터를 삽입한 형태로 제작되었다.
구체적으로는, 효모의 염색체 DNA를 주형으로 하여 서열번호 41, 42의 프라이머를 이용하여 PCR을 수행하여 PDC1 유전자를 포함하는 산물을 얻고, 이를 서열번호 43, 44를 이용하여 CYC1 터미네이터의 서열을 얻었다. 이들 각각을 주형으로 한 PCR을 다시 서열번호 41, 44 프라이머로 수행하여 PDC1과 CYC1 터미네이터가 연결된 DNA 단편을 얻었다. PDC1-CYC1 터미네이터의 DNA 단편과 pRS406 벡터를 pRS406과 SpeI, XhoI 제한효소를 처리한 후 이들을 ligation한 pRS406-PDC1-CYC1t 플라스미드를 얻었다. 한편, 얻어진 플라스미드에 프로모터 영역을 도입하기 위하여 PDC1 프로모터와 IDP2 프로모터를 각각 서열번호 45, 46의 프라이머와 서열번호 47, 48의 프라이머의 조합으로 효모 염색체 DNA를 주형으로 사용한 PCR을 수행하여 얻었다. 각 프로모터를 포함하는 유전자 단편과 플라스미드 pRS406-PDC1-CYC1t를 SacI과 SpeI으로 절단하여 이들을 ligation하여 PDC1 프로모터 및 IDP2 프로모터에 의하여 PDC1 유전자의 발현이 조절되도록 설계된 효모 염색체 삽입용 플라스미드인 pRS406-PDC1p-PDC1-CYC1t 및 pRS406-IDP2p-PDC1-CYC1t를 각각 제작하였다.
상기 과정에서 사용된 프라이머를 정리하면 하기 표 6과 같다.
프라이머 | 5'-> 3' 서열 |
F_PDC1 (서열번호 41) |
ATAACTAGTATGTCTGAAATTACTTTGGGTAAATATTT |
R_PDC1 (서열번호 42) |
CAAAGGAAAAGGGGCCTGTTTATTGCTTAGCGTTGGTAGCAGCA |
F_CYC1t (서열번호 43) |
TACCAACGCTAAGCAATAAACAGGCCCCTTTTCCTTTGTCGAT |
R_CYC1t (서열번호 44) |
ATACTCGAGGCAAATTAAAGCCTTCGAGCGTCC |
F_PDC1p (서열번호 45) |
AAAGAGCTCCATGCGACTGGGTGAGCATATGTT |
R_PDC1p (서열번호 46) |
ATAACTAGTTTTGATTGATTTGACTGTGTTATTTTGC |
F_IDP2p (서열번호 47) |
AAAGAGCTC ACGTCTATCTATTTATTTTTATAACTCC |
R_IDP2p (서열번호 48) |
ATAACTAGT TACGATTTTATATATATACGTACGTTAC |
상기 제작된 두 개의 플라스미드를 StuI으로 각각 절단하여 이를 곧바로 균주에 도입하였고 완성된 균주는 CC02-0451(CC02-0450, PDC1p-PDC1)과 CC02-0452(CC02-0450, IDP2p-PDC1)라고 각각 명명하였다. 제작한 균주와 유전형질을 정리하면 하기 표 7과 같다.
균주 | 유전형질 |
CC02-0450 | CC02-0064 pdc5Δ |
CC02-0451 | CC02-0450 PDC1p-PDC1-CYC1t |
CC02-0452 | CC02-0450 IDP2p-PDC1-CYC1t |
실시예
6 :
PDC
이중 결손 또는 삼중 결손 균주 제작
PDC 패밀리 유전자에서 PDC1 단독 결손, PDC1 및 PDC5 이중 결손 및 PDC1, PDC5 및 PDC6 삼중 결손 균주를 제작하고자 하였다. PDC1 단독 결손 균주로는 상기 실시예 1에서 제작한 기반 균주 CC02-0064를 이용하였다. 서열번호 49 내지 서열번호 56의 프라이머를 이용하여 PDC5 결손 카세트를 제작하고 CC02-0064에 도입하여 PDC1 및 PDC5 이중 결손 균주를 제작하였으며 이를 CC02-0256이라 명명하였다. 또한, 상기 PDC1 및 PDC5 이중 결손 균주인 CC02-0256을 기반으로 서열번호 57 내지 서열번호 64를 이용하여 PDC1, PDC5 및 PDC6 삼중 결손 균주를 제작하고 이를 CC02-0257이라 명명하였다.
상기 결손 카세트 제작 및 균주 선별과정은 실시예 1에 명시된 문헌과 동일한 방법으로 제작하였다. 이에 사용한 프라이머를 정리하면 하기 표 8과 같다.
프라이머 | 5' -> 3' 서열 |
F_BamHI-PDC5_UP (서열번호 49) |
CGGGATCCAGGCCAAGGAAATAAAGCAAATAACAA |
R_NotI-PDC5_UP (서열번호 50) |
ATAAGAATGCGGCCGCTTTGTTCTTCTTGTTATTGTATTGTGTT |
F_BamHI-PDC5_DOWN (서열번호 51) |
CGGGATCCGCTAATTAACATAAAACTCATGATTCAA |
R_NotI-PDC5_DOWN (서열번호 52) |
ATAAGAATGCGGCCGCTATTCTAAATAAGATGTAAGGCCTTGTA |
F_PDC5_UP (서열번호 53) |
AGGCCAAGGAAATAAAGCAAATAACAA |
R_AL_KlURA3 (서열번호 54) |
GAGCAATGAACCCAATAACGAAATCTT |
F_BR_KlURA3 (서열번호 55) |
CTTGACGTTCGTTCGACTGATGAG |
R_PDC5_DOWN (서열번호 56) |
TATTCTAAATAAGATGTAAGGCCTTGTA |
F_BamHI-PDC6_UP (서열번호 57) |
CGGGATCCTGTTATAGAGTTCACACCTTATTCACA |
R_NotI-PDC6_UP (서열번호 58) |
ATAAGAATGCGGCCGCTTTGTTGGCAATATGTTTTTGCTATATTA |
F_BamHI-PDC6_DOWN (서열번호 59) |
CGGGATCCGCCATTAGTAGTGTACTCAAACGAAT |
R_NotI-PDC6_DOWN (서열번호 60) |
ATAAGAATGCGGCCGCGATGCAGAATGAGCACTTGTTATTTAT |
F_PDC6_UP (서열번호 61) |
TGTTATAGAGTTCACACCTTATTCACA |
R_AL_KlURA3 (서열번호 62) |
GAGCAATGAACCCAATAACGAAATCTT |
F_BR_KlURA3 (서열번호 63) |
CTTGACGTTCGTTCGACTGATGAG |
R_PDC6_DOWN (서열번호 64) |
GATGCAGAATGAGCACTTGTTATTTAT |
상기 제작한 균주와 유전형질을 정리하면 하기 표 9와 같다.
균주 | 유전 형질 |
CC02-0256 | CC02-0064 pdc5Δ |
CC02-0257 | CC02-0256 pdc6Δ |
실시예
7 :
ALD
와
ACS1
강화 균주의 제작
ALD와 ACS1이 과발현되는 균주를 제작하기 위하여, ALD2, ALD3 및 ACS1의 과발현 플라스미드를 제작하였다.
구체적으로는, 서열번호 65 및 서열번호 66의 프라이머를 이용하여 ALD2의 ORF를, 서열번호 67 및 서열번호 68의 프라이머를 이용하여 ALD3의 ORF를, 그리고 서열번호 69 및 서열번호 70의 프라이머를 이용하여 ACS1의 ORF를 취하고 SpeI과 XhoI 또는 EcoRI 제한효소를 이용하여 p414ADH, p415ADH 및 p416ADH 플라스미드 기반의 재조합 벡터인 p415ADH-ALD2, p415ADH-ALD3, p414ADH-ACS1 및 p416ADH-ACS1을 제작하였다. 이에 사용한 프라이머를 정리하면 하기 표 10과 같다.
프라이머 | 5'-> 3' 서열 |
F_SpeI_ALD2 (서열번호 65) |
CAAGCTGGCCGCTCTAGAACTAGTATGCCTACCTTGTATACTGATATCGA |
R_XhoI_ALD2 (서열번호 66) |
ACATAACTAATTACATGACTCGAGTTAGTTGTCCAAAGAGAGATTTATGT |
F_SpeI_ALD3 (서열번호 67) |
CAAGCTGGCCGCTCTAGAACTAGTATGCCTACCTTGTATACTGATATCGA |
R_XhoI_ALD3 (서열번호 68) |
ACATAACTAATTACATGACTCGAGTTATTTATCCAATGAAAGATCCACAT |
F_SpeI_ACS1 (서열번호 69) |
TCCAAGCTGGCCGCTCTAGAACTAGTATGTCGCCCTCTGCCGTACA |
R_EcoRI_ACS1 (서열번호 70) |
TATCGATAAGCTTGATATCGAATTCTTACAACTTGACCGAATCAATTAGA |
이렇게 제작된 재조합 플라스미드를 CC02-0064, CC02-0168, CC02-0170, CC02-0256, CC02-0257, CC02-0451, CC02-0452 균주에 p415ADH-ALD2, p414ADH-ACS1 조합, p415ADH-ALD3, p414ADH-ACS1 조합, p415ADH-ALD2, p416ADH-ACS1 조합 또는 p415ADH-ALD3, p416ADH-ACS1 조합으로 효모 형질전환법을 이용하여 도입하였다. 한편, PDC 역가가 없는 삼중 결손 CC02-0257 균주에서는 형질전환체가 확보되지 않았다.
상기 제작한 균주와 유전형질을 정리하면 하기 표 11과 같다.
균주 | 유전형질 |
CC02-0225 | CC02-0064 p415ADH, p416ADH |
CC02-0226 | CC02-0064 p415ADH-ALD2, p416ADH-ACS1 |
CC02-0227 | CC02-0064 p415ADH-ALD3, p416ADH-ACS1 |
CC02-0356 | CC02-0168 p414ADH, p415ADH |
CC02-0275 | CC02-0168 p414ADH-ACS1, p415ADH-ALD2 |
CC02-0276 | CC02-0168 p414ADH-ACS1, p415ADH-ALD3 |
CC02-0357 | CC02-0170 p414ADH, p415ADH |
CC02-0277 | CC02-0170 p414ADH-ACS1, p415ADH-ALD2 |
CC02-0278 | CC02-0170 p414ADH-ACS1, p415ADH-ALD3 |
CC02-0444 | CC02-0256 p415ADH, p416ADH |
CC02-0361 | CC02-0256 p415ADH-ALD2, p416ADH-ACS1 |
CC02-0362 | CC02-0256 p415ADH-ALD3, p416ADH-ACS1 |
CC02-0453 | CC02-0451 p414ADH, p415ADH |
CC02-0454 | CC02-0451 p414ADH-ACS1, p415ADH-ALD2 |
CC02-0455 | CC02-0451 p414ADH-ACS1, p415ADH-ALD3 |
CC02-0456 | CC02-0452 p414ADH, p415ADH |
CC02-0457 | CC02-0452 p414ADH-ACS1, p415ADH-ALD2 |
CC02-0458 | CC02-0452 p414ADH-ACS1, p415ADH-ALD3 |
실시예
8 : 효모 균주의 젖산 발효 평가
상기 실시예 7에서 제작한 ALD와 ACS1 강화 균주의 젖산 발효능을 평가하였다.
구체적으로는 상기 실시예 3에서 제작한 젖산 발효 평가용 배지를 한 플라스크당 25 ㎖로 분주하여 효모균을 접종하고 30 ℃에서 71 시간 동안 호기배양한 뒤 발효액에 존재하는 D형 젖산의 양을 HPLC 분석하고 아세트산(Acetic acid)의 양을 효소 분석(Acetic acid, R-Biopharm, 독일)하였다.
상기 실험의 결과를 정리하면 하기 표 12와 같다.
균주 | 최종 OD | 초기당 (g/L) |
잔존당 (g/L) |
Acetate (g/L) |
D-젖산 (g/L) |
수율 (g/g) |
생산성 (g/l·h) |
CC02-0225 | 9.3 | 88 | 10 | 2.87 | 41.1 | 0.53 | 0.579 |
CC02-0226 | 9.3 | 83 | 10.5 | 2.91 | 42.4 | 0.59 | 0.597 |
CC02-0227 | 10.1 | 84 | 9.5 | 2.91 | 41.8 | 0.56 | 0.589 |
CC02-0356 | 6.9 | 88 | 26 | 0.02 | 27.6 | 0.45 | 0.389 |
CC02-0275 | 11.6 | 88 | 11.5 | 0.01 | 47.6 | 0.62 | 0.670 |
CC02-0276 | 10.6 | 88 | 11 | 0.01 | 46.8 | 0.61 | 0.659 |
CC02-0357 | 12.2 | 88 | 13 | 0.04 | 38.1 | 0.51 | 0.537 |
CC02-0277 | 17.8 | 88 | 1 | 0.03 | 58.6 | 0.67 | 0.825 |
CC02-0278 | 18.8 | 88 | 0 | 0.02 | 56.9 | 0.66 | 0.801 |
CC02-0453 | 9.8 | 88 | 8.5 | 2.2 | 38.9 | 0.49 | 0.548 |
CC02-0454 | 10.2 | 88 | 8.1 | 2.4 | 39.5 | 0.49 | 0.556 |
CC02-0455 | 9.2 | 88 | 8.8 | 2.1 | 40 | 0.51 | 0.563 |
CC02-0456 | 12 | 88 | 10.1 | 0.02 | 38.5 | 0.49 | 0.542 |
CC02-0457 | 18.1 | 88 | 0 | 0.02 | 55.8 | 0.63 | 0.786 |
CC02-0458 | 18.5 | 88 | 0 | 0.02 | 56.5 | 0.64 | 0.800 |
상기 표 12에서 확인할 수 있듯이, PDC5가 IDP2 또는 SCO2 프로모터에서 발현되어 PDC5가 약화된 균주는 그렇지 않은 균주에 비해 아세테이트 부산물 축적이 현저히 감소하여 거의 검출되지 않음을 확인하였다. 이 경우에 ALD, ACS를 강화하지 않은 균주들의 최종 세포농도는 PDC5 프로모터 교체에 따른 감소 경향을 나타내었다. 그러나 PDC5의 발현을 감소하고 ALD, ACS를 강화한 균주들에서는 반대로 최종 세포농도가 증가하였으며 따라서 세포 생장이 개선되었음을 확인하였다. 특히, PDC5의 프로모터를 IDP2 프로모터로 바꾼 CC02-0170 균주 기반에서 ALD, ACS를 강화한 CC02-0277, CC02-0278 균주는 ALD, ACS를 강화함에 따라 생장속도, D-젖산 생산 생산 농도, 수율, 발효 생산성이 향상됨을 확인하였다.
요약하면, PDC5를 IDP2 프로모터로 약화 발현한 균주는 PDC5가 정상 발현되는 균주에 비해 아세테이트 부산물 축적이 감소하고, 최종 OD가 1.3배 증가하는 것을 확인하였으며, 추가적으로 ALD, ACS를 ADH1 프로모터의 조절 하에서 동시 발현시 당소모량과 당소모 속도가 증가하고 최종적으로 수율이 56% 또는 59%에서 66% 또는 67%로 증가되었음을 확인하였다.
구체적으로 PDC5 약화 발현에 적용된 2종의 프로모터를 비교하면 SCO2 프로모터 적용 균주와 IDP2 프로모터를 적용한 균주에서 모두 젖산 생산성이 향상되는 것을 확인하였다. 그러나 최종 세포농도와 당소모량과 당소모 속도의 측면에서 IDP2 프로모터를 적용한 경우가 보다 최적화된 형태임을 알 수 있었다.
실시예
9 :
PDC1
및
PDC5
가 이중
결손되고
ALD
및
ACS
강화된 효모 균주의 젖산 발효 평가
PDC5의 약화에 의한 생장 및 수율 개선의 효과가 뚜렷함에 따라 PDC를 추가적으로 결손한 균주에서의 젖산 생성 효과를 확인하고자 하였다. 각 균주의 평가 방법은 상기 실시예 8에서와 동일하며 배양은 74 시간 동안 진행하였다.
상기 실험을 진행한 결과는 하기 표 13과 같다.
균주 | 최종 OD | 초기당 (g/L) |
잔존당 (g/L) |
Acetate (g/L) |
D-젖산 (g/L) |
수율 (g/g) |
생산성 (g/l·h) |
CC02-0444 | 3.2 | 78.5 | 52 | 0.10 | 20.8 | 78.5 | 0.281 |
CC02-0361 | 3.9 | 78.5 | 49 | 0.05 | 25.4 | 86.3 | 0.343 |
CC02-0362 | 3.8 | 78.5 | 51 | 0.08 | 22.8 | 82.8 | 0.308 |
상기 표 13에서 확인할 수 있듯이, PDC1 및 PDC5가 이중 결손된 균주는 아세트산의 감소가 뚜렷하였으나, 세포 성장 및 당소모량의 감소로 인한 젖산 생산 농도의 감소가 관찰되었다. 또한 PDC1 및 PDC5가 이중 결손되어 PDC 경로가 거의 불활성화된 균주에서는 ALD와 ACS를 강화하여도 세포 성장과 당소모 및 생산성이 개선되지 않은 것을 확인할 수 있었다.
실시예
10 :
PDC
경로 약화 균주의 수크로오스를 이용한 젖산 발효 평가
PDC 경로가 약화된 젖산 생산 효모의 수크로오스를 이용한 발효 평가를 위해 실시예 8 및 실시예 9에서 평가한 동일한 균주를 탄소원으로서 포도당 대신 수크로오스로 대체하여 젖산 생성 효과를 확인하고자 하였다. 평가 방법은 실시예 8에서와 동일하게 진행하였다.
상기 실험을 진행한 결과는 하기 표 14와 같다.
균주 | 최종 OD | 초기당 (g/L) |
잔존당 (g/L) |
Acetate (g/L) |
D-젖산 (g/L) |
수율 (g/g) |
생산성 (g/l·h) |
CC02-0225 | 5.15 | 91.5 | 27.5 | 1.95 | 25.19 | 39.36 | 0.34 |
CC02-0226 | 6.9 | 91.5 | 15 | 1.92 | 30.89 | 40.38 | 0.42 |
CC02-0227 | 6.18 | 91.5 | 15 | 1.98 | 29.59 | 38.68 | 0.40 |
CC02-0356 | 1.6 | 91.5 | 26.75 | 0.02 | 11.72 | 18.11 | 0.16 |
CC02-0275 | 1.88 | 91.5 | 21.75 | 0.02 | 13.79 | 19.77 | 0.19 |
CC02-0276 | 2.2 | 91.5 | 18.25 | 0.01 | 16.04 | 21.9 | 0.22 |
CC02-0357 | 2.78 | 91.5 | 22 | 0.03 | 17.08 | 24.58 | 0.23 |
CC02-0277 | 12.15 | 91.5 | 7.75 | 0.02 | 44.65 | 53.31 | 0.60 |
CC02-0278 | 11.88 | 91.5 | 6.25 | 0.01 | 43.84 | 51.43 | 0.60 |
CC02-0444 | 2.45 | 91.5 | 37 | 0.02 | 21.94 | 40.25 | 0.30 |
CC02-0361 | 2.5 | 91.5 | 18.25 | 0.02 | 21.73 | 29.66 | 0.29 |
CC02-0362 | 3.08 | 91.5 | 15.25 | 0.02 | 24.92 | 32.67 | 0.34 |
실시예 8, 9에서와 동일한 균주에 포도당 대신 수크로오스를 이용하게 한 결과 PDC 경로가 약화된 균주에서의 ALD, ACS의 강화에 의한 생장 및 수율 개선의 효과가 상기 실시예 8의 포도당을 사용한 발효 평가의 결과와 동일한 패턴임을 확인하였다. 따라서, 본 발명에서 확인하였던 PDC 약화 및 ALD, ACS 강화에 의한 수율 및 생장 개선의 효과가 사용한 당의 종류에 국한되지 않음을 확인하였다.
상기 결과들을 종합하면, 본 발명의 피루베이트 탈탄산효소(PDC) 경로가 약화되고 알데히드 탈수소효소(ALD)의 활성 및 acetyl-CoA 합성 효소(ACS)들의 활성이 비변이 균주에 비하여 향상되도록 변형한 균주는 젖산 생산 수율이 증진됨과 동시에 생장률 또한 유지되는 것을 확인하였다.
이상의 설명으로부터, 본 발명이 속하는 기술분야의 당업자는 본 발명이 그 기술적 사상이나 필수적 특징을 변경하지 않고서 다른 구체적인 형태로 실시될 수 있다는 것을 이해할 수 있을 것이다. 이와 관련하여, 이상에서 기술한 실시 예들은 모든 면에서 예시적인 것이며 한정적인 것이 아닌 것으로서 이해해야만 한다. 본 발명의 범위는 상기 상세한 설명, 특허 청구범위의 의미 및 범위 그리고 그 등가 개념으로부터 도출되는 모든 변경 또는 변형된 형태가 본 발명의 범위에 포함되는 것으로 해석되어야 한다.
<110> CJ CheilJedang Corporation
<120> A microorganism having enhanced productivity of lactic acid and a
process for producing lactic acid using the same
<130> PA131227/KR
<160> 78
<170> KopatentIn 2.0
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<211> 32
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<220>
<223> ADH1 upstream forward primer
<400> 1
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<223> ADH1 upstream reverse primer
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<223> ADH1 downstream forward primer
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<211> 37
<212> DNA
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<220>
<223> ADH1 downstream reverse primer
<400> 4
acatgccatg gaagcatgca cgtatacact tgagtaa 37
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<211> 35
<212> DNA
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<223> PDC1 upstream forward primer
<400> 5
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<223> PDC1 upstream reverse primer
<400> 6
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<223> PDC1 downstream forward primer
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<223> PDC1 downstream reverse primer
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<220>
<223> DLD1-HIS3 upstream linking primer
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<212> DNA
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<223> DLD1-HIS3 downstream linking primer
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<223> F_PDC5_UP_676
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gtcagcattg acacgttcga tt 22
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<223> R_KlURA3-PDC5_UP
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<213> Artificial Sequence
<220>
<223> F_PDC5_UP-AL_KlURA3
<400> 13
caatctctcg aaagaagtga ttctgggtag aagatcgg 38
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<211> 27
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<213> Artificial Sequence
<220>
<223> R_AL_KlURA3
<400> 14
gagcaatgaa cccaataacg aaatctt 27
<210> 15
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<212> DNA
<213> Artificial Sequence
<220>
<223> F_BR_KlURA3
<400> 15
cttgacgttc gttcgactga tgag 24
<210> 16
<211> 22
<212> DNA
<213> Artificial Sequence
<220>
<223> R_PDC5_DOWN_522
<400> 16
caagtcaacc aagttagctg gc 22
<210> 17
<211> 43
<212> DNA
<213> Artificial Sequence
<220>
<223> R_SCO1p-BR_KlURA3
<400> 17
ctctcctaat agacgtggtg tcaccatgaa cgacaattct taa 43
<210> 18
<211> 38
<212> DNA
<213> Artificial Sequence
<220>
<223> F_SCO1p_500
<400> 18
cgttcatggt gacaccacgt ctattaggag agccattc 38
<210> 19
<211> 41
<212> DNA
<213> Artificial Sequence
<220>
<223> R_PDC5_DOWN_500-SCO1p
<400> 19
aaggttattt cagacatctt ttctacgttt gctgtttttt c 41
<210> 20
<211> 42
<212> DNA
<213> Artificial Sequence
<220>
<223> F_SCO1p-PDC5_DOWN_500
<400> 20
cagcaaacgt agaaaagatg tctgaaataa ccttaggtaa at 42
<210> 21
<211> 44
<212> DNA
<213> Artificial Sequence
<220>
<223> R_SCO2p-BR_KlURA3
<400> 21
atcgaataag taacaagcgt gtcaccatga acgacaattc ttaa 44
<210> 22
<211> 38
<212> DNA
<213> Artificial Sequence
<220>
<223> F_SCO2p_500
<400> 22
cgttcatggt gacacgcttg ttacttattc gataacgc 38
<210> 23
<211> 40
<212> DNA
<213> Artificial Sequence
<220>
<223> R_PDC5_DOWN_500-SCO2p
<400> 23
aaggttattt cagacatttt actctcgctt cccaaattcc 40
<210> 24
<211> 40
<212> DNA
<213> Artificial Sequence
<220>
<223> F_SCO2p-PDC5_DOWN_500
<400> 24
ggaagcgaga gtaaaatgtc tgaaataacc ttaggtaaat 40
<210> 25
<211> 47
<212> DNA
<213> Artificial Sequence
<220>
<223> R_IDP2p-BR_KlURA3
<400> 25
taaaaataaa tagatagacg tgtgtcacca tgaacgacaa ttcttaa 47
<210> 26
<211> 42
<212> DNA
<213> Artificial Sequence
<220>
<223> F_IDP2p_500
<400> 26
cgttcatggt gacacacgtc tatctattta tttttataac tc 42
<210> 27
<211> 44
<212> DNA
<213> Artificial Sequence
<220>
<223> R_PDC5_DOWN_500-IDP2p
<400> 27
aaggttattt cagacattac gattttatat atatacgtac gtta 44
<210> 28
<211> 45
<212> DNA
<213> Artificial Sequence
<220>
<223> F_IDP2p-PDC5_DOWN_500
<400> 28
cgtatatata taaaatcgta atgtctgaaa taaccttagg taaat 45
<210> 29
<211> 43
<212> DNA
<213> Artificial Sequence
<220>
<223> R_ACS1p-BR_KlURA3
<400> 29
ctggacgtat gtgcacagtg tcaccatgaa cgacaattct taa 43
<210> 30
<211> 38
<212> DNA
<213> Artificial Sequence
<220>
<223> F_ACS1p_500
<400> 30
cgttcatggt gacactgtgc acatacgtcc agaatgat 38
<210> 31
<211> 39
<212> DNA
<213> Artificial Sequence
<220>
<223> R_PDC5_DOWN_500-ACS1p
<400> 31
aaggttattt cagacatagc acagtgggca atgtctttc 39
<210> 32
<211> 41
<212> DNA
<213> Artificial Sequence
<220>
<223> F_ACS1p-PDC5_DOWN_500
<400> 32
cattgcccac tgtgctatgt ctgaaataac cttaggtaaa t 41
<210> 33
<211> 45
<212> DNA
<213> Artificial Sequence
<220>
<223> R_FBA1p-BR_KlURA3
<400> 33
ttatttacgt aatgacccag tgtcaccatg aacgacaatt cttaa 45
<210> 34
<211> 40
<212> DNA
<213> Artificial Sequence
<220>
<223> F_FBA1p_500
<400> 34
cgttcatggt gacactgggt cattacgtaa ataatgatag 40
<210> 35
<211> 44
<212> DNA
<213> Artificial Sequence
<220>
<223> R_PDC5_DOWN_500-FBA1p
<400> 35
aaggttattt cagacatttt gaatatgtat tacttggtta tggt 44
<210> 36
<211> 45
<212> DNA
<213> Artificial Sequence
<220>
<223> F_FBA1p-PDC5_DOWN_500
<400> 36
ccaagtaata catattcaaa atgtctgaaa taaccttagg taaat 45
<210> 37
<211> 41
<212> DNA
<213> Artificial Sequence
<220>
<223> F-ALPDC5-BamHI
<400> 37
gagctcggat ccaaggaaat aaagcaaata acaataacac c 41
<210> 38
<211> 43
<212> DNA
<213> Artificial Sequence
<220>
<223> R-ALPDC5-NotI
<400> 38
accatggcgg ccgctttgtt cttcttgtta ttgtattgtg ttg 43
<210> 39
<211> 42
<212> DNA
<213> Artificial Sequence
<220>
<223> F-BRPDC5-SpeI
<400> 39
ggatccacta gtgctaatta acataaaact catgattcaa cg 42
<210> 40
<211> 42
<212> DNA
<213> Artificial Sequence
<220>
<223> R-BRPDC5-NcoI
<400> 40
cagctgccat ggtattctaa ataagatgta aggccttgta at 42
<210> 41
<211> 38
<212> DNA
<213> Artificial Sequence
<220>
<223> F_PDC1
<400> 41
ataactagta tgtctgaaat tactttgggt aaatattt 38
<210> 42
<211> 44
<212> DNA
<213> Artificial Sequence
<220>
<223> R_PDC1
<400> 42
caaaggaaaa ggggcctgtt tattgcttag cgttggtagc agca 44
<210> 43
<211> 43
<212> DNA
<213> Artificial Sequence
<220>
<223> F_CYC1t
<400> 43
taccaacgct aagcaataaa caggcccctt ttcctttgtc gat 43
<210> 44
<211> 33
<212> DNA
<213> Artificial Sequence
<220>
<223> R_CYC1t
<400> 44
atactcgagg caaattaaag ccttcgagcg tcc 33
<210> 45
<211> 33
<212> DNA
<213> Artificial Sequence
<220>
<223> F_PDC1p
<400> 45
aaagagctcc atgcgactgg gtgagcatat gtt 33
<210> 46
<211> 37
<212> DNA
<213> Artificial Sequence
<220>
<223> R_PDC1p
<400> 46
ataactagtt ttgattgatt tgactgtgtt attttgc 37
<210> 47
<211> 37
<212> DNA
<213> Artificial Sequence
<220>
<223> F_IDP2p
<400> 47
aaagagctca cgtctatcta tttattttta taactcc 37
<210> 48
<211> 37
<212> DNA
<213> Artificial Sequence
<220>
<223> R_IDP2p
<400> 48
ataactagtt acgattttat atatatacgt acgttac 37
<210> 49
<211> 35
<212> DNA
<213> Artificial Sequence
<220>
<223> F_BamHI-PDC5_UP
<400> 49
cgggatccag gccaaggaaa taaagcaaat aacaa 35
<210> 50
<211> 44
<212> DNA
<213> Artificial Sequence
<220>
<223> R_NotI-PDC5_UP
<400> 50
ataagaatgc ggccgctttg ttcttcttgt tattgtattg tgtt 44
<210> 51
<211> 36
<212> DNA
<213> Artificial Sequence
<220>
<223> F_BamHI-PDC5_DOWN
<400> 51
cgggatccgc taattaacat aaaactcatg attcaa 36
<210> 52
<211> 44
<212> DNA
<213> Artificial Sequence
<220>
<223> R_NotI-PDC5_DOWN
<400> 52
ataagaatgc ggccgctatt ctaaataaga tgtaaggcct tgta 44
<210> 53
<211> 27
<212> DNA
<213> Artificial Sequence
<220>
<223> F_PDC5_UP
<400> 53
aggccaagga aataaagcaa ataacaa 27
<210> 54
<211> 27
<212> DNA
<213> Artificial Sequence
<220>
<223> R_AL_KlURA3
<400> 54
gagcaatgaa cccaataacg aaatctt 27
<210> 55
<211> 24
<212> DNA
<213> Artificial Sequence
<220>
<223> F_BR_KlURA3
<400> 55
cttgacgttc gttcgactga tgag 24
<210> 56
<211> 28
<212> DNA
<213> Artificial Sequence
<220>
<223> R_PDC5_DOWN
<400> 56
tattctaaat aagatgtaag gccttgta 28
<210> 57
<211> 35
<212> DNA
<213> Artificial Sequence
<220>
<223> F_BamHI-PDC6_UP
<400> 57
cgggatcctg ttatagagtt cacaccttat tcaca 35
<210> 58
<211> 45
<212> DNA
<213> Artificial Sequence
<220>
<223> R_NotI-PDC6_UP
<400> 58
ataagaatgc ggccgctttg ttggcaatat gtttttgcta tatta 45
<210> 59
<211> 34
<212> DNA
<213> Artificial Sequence
<220>
<223> F_BamHI-PDC6_DOWN
<400> 59
cgggatccgc cattagtagt gtactcaaac gaat 34
<210> 60
<211> 43
<212> DNA
<213> Artificial Sequence
<220>
<223> R_NotI-PDC6_DOWN
<400> 60
ataagaatgc ggccgcgatg cagaatgagc acttgttatt tat 43
<210> 61
<211> 27
<212> DNA
<213> Artificial Sequence
<220>
<223> F_PDC6_UP
<400> 61
tgttatagag ttcacacctt attcaca 27
<210> 62
<211> 27
<212> DNA
<213> Artificial Sequence
<220>
<223> R_AL_KlURA3
<400> 62
gagcaatgaa cccaataacg aaatctt 27
<210> 63
<211> 24
<212> DNA
<213> Artificial Sequence
<220>
<223> F_BR_KlURA3
<400> 63
cttgacgttc gttcgactga tgag 24
<210> 64
<211> 27
<212> DNA
<213> Artificial Sequence
<220>
<223> R_PDC6_DOWN
<400> 64
gatgcagaat gagcacttgt tatttat 27
<210> 65
<211> 50
<212> DNA
<213> Artificial Sequence
<220>
<223> F_SpeI_ALD2
<400> 65
caagctggcc gctctagaac tagtatgcct accttgtata ctgatatcga 50
<210> 66
<211> 50
<212> DNA
<213> Artificial Sequence
<220>
<223> R_XhoI_ALD2
<400> 66
acataactaa ttacatgact cgagttagtt gtccaaagag agatttatgt 50
<210> 67
<211> 50
<212> DNA
<213> Artificial Sequence
<220>
<223> F_SpeI_ALD3
<400> 67
caagctggcc gctctagaac tagtatgcct accttgtata ctgatatcga 50
<210> 68
<211> 50
<212> DNA
<213> Artificial Sequence
<220>
<223> R_XhoI_ALD3
<400> 68
acataactaa ttacatgact cgagttattt atccaatgaa agatccacat 50
<210> 69
<211> 46
<212> DNA
<213> Artificial Sequence
<220>
<223> F_SpeI_ACS1
<400> 69
tccaagctgg ccgctctaga actagtatgt cgccctctgc cgtaca 46
<210> 70
<211> 50
<212> DNA
<213> Artificial Sequence
<220>
<223> R_EcoRI_ACS1
<400> 70
tatcgataag cttgatatcg aattcttaca acttgaccga atcaattaga 50
<210> 71
<211> 563
<212> PRT
<213> Saccharomyces cerevisiae PDC1
<400> 71
Met Ser Glu Ile Thr Leu Gly Lys Tyr Leu Phe Glu Arg Leu Lys Gln
1 5 10 15
Val Asn Val Asn Thr Val Phe Gly Leu Pro Gly Asp Phe Asn Leu Ser
20 25 30
Leu Leu Asp Lys Ile Tyr Glu Val Glu Gly Met Arg Trp Ala Gly Asn
35 40 45
Ala Asn Glu Leu Asn Ala Ala Tyr Ala Ala Asp Gly Tyr Ala Arg Ile
50 55 60
Lys Gly Met Ser Cys Ile Ile Thr Thr Phe Gly Val Gly Glu Leu Ser
65 70 75 80
Ala Leu Asn Gly Ile Ala Gly Ser Tyr Ala Glu His Val Gly Val Leu
85 90 95
His Val Val Gly Val Pro Ser Ile Ser Ala Gln Ala Lys Gln Leu Leu
100 105 110
Leu His His Thr Leu Gly Asn Gly Asp Phe Thr Val Phe His Arg Met
115 120 125
Ser Ala Asn Ile Ser Glu Thr Thr Ala Met Ile Thr Asp Ile Ala Thr
130 135 140
Ala Pro Ala Glu Ile Asp Arg Cys Ile Arg Thr Thr Tyr Val Thr Gln
145 150 155 160
Arg Pro Val Tyr Leu Gly Leu Pro Ala Asn Leu Val Asp Leu Asn Val
165 170 175
Pro Ala Lys Leu Leu Gln Thr Pro Ile Asp Met Ser Leu Lys Pro Asn
180 185 190
Asp Ala Glu Ser Glu Lys Glu Val Ile Asp Thr Ile Leu Ala Leu Val
195 200 205
Lys Asp Ala Lys Asn Pro Val Ile Leu Ala Asp Ala Cys Cys Ser Arg
210 215 220
His Asp Val Lys Ala Glu Thr Lys Lys Leu Ile Asp Leu Thr Gln Phe
225 230 235 240
Pro Ala Phe Val Thr Pro Met Gly Lys Gly Ser Ile Asp Glu Gln His
245 250 255
Pro Arg Tyr Gly Gly Val Tyr Val Gly Thr Leu Ser Lys Pro Glu Val
260 265 270
Lys Glu Ala Val Glu Ser Ala Asp Leu Ile Leu Ser Val Gly Ala Leu
275 280 285
Leu Ser Asp Phe Asn Thr Gly Ser Phe Ser Tyr Ser Tyr Lys Thr Lys
290 295 300
Asn Ile Val Glu Phe His Ser Asp His Met Lys Ile Arg Asn Ala Thr
305 310 315 320
Phe Pro Gly Val Gln Met Lys Phe Val Leu Gln Lys Leu Leu Thr Thr
325 330 335
Ile Ala Asp Ala Ala Lys Gly Tyr Lys Pro Val Ala Val Pro Ala Arg
340 345 350
Thr Pro Ala Asn Ala Ala Val Pro Ala Ser Thr Pro Leu Lys Gln Glu
355 360 365
Trp Met Trp Asn Gln Leu Gly Asn Phe Leu Gln Glu Gly Asp Val Val
370 375 380
Ile Ala Glu Thr Gly Thr Ser Ala Phe Gly Ile Asn Gln Thr Thr Phe
385 390 395 400
Pro Asn Asn Thr Tyr Gly Ile Ser Gln Val Leu Trp Gly Ser Ile Gly
405 410 415
Phe Thr Thr Gly Ala Thr Leu Gly Ala Ala Phe Ala Ala Glu Glu Ile
420 425 430
Asp Pro Lys Lys Arg Val Ile Leu Phe Ile Gly Asp Gly Ser Leu Gln
435 440 445
Leu Thr Val Gln Glu Ile Ser Thr Met Ile Arg Trp Gly Leu Lys Pro
450 455 460
Tyr Leu Phe Val Leu Asn Asn Asp Gly Tyr Thr Ile Glu Lys Leu Ile
465 470 475 480
His Gly Pro Lys Ala Gln Tyr Asn Glu Ile Gln Gly Trp Asp His Leu
485 490 495
Ser Leu Leu Pro Thr Phe Gly Ala Lys Asp Tyr Glu Thr His Arg Val
500 505 510
Ala Thr Thr Gly Glu Trp Asp Lys Leu Thr Gln Asp Lys Ser Phe Asn
515 520 525
Asp Asn Ser Lys Ile Arg Met Ile Glu Ile Met Leu Pro Val Phe Asp
530 535 540
Ala Pro Gln Asn Leu Val Glu Gln Ala Lys Leu Thr Ala Ala Thr Asn
545 550 555 560
Ala Lys Gln
<210> 72
<211> 563
<212> PRT
<213> Saccharomyces cerevisiae PDC5
<400> 72
Met Ser Glu Ile Thr Leu Gly Lys Tyr Leu Phe Glu Arg Leu Ser Gln
1 5 10 15
Val Asn Cys Asn Thr Val Phe Gly Leu Pro Gly Asp Phe Asn Leu Ser
20 25 30
Leu Leu Asp Lys Leu Tyr Glu Val Lys Gly Met Arg Trp Ala Gly Asn
35 40 45
Ala Asn Glu Leu Asn Ala Ala Tyr Ala Ala Asp Gly Tyr Ala Arg Ile
50 55 60
Lys Gly Met Ser Cys Ile Ile Thr Thr Phe Gly Val Gly Glu Leu Ser
65 70 75 80
Ala Leu Asn Gly Ile Ala Gly Ser Tyr Ala Glu His Val Gly Val Leu
85 90 95
His Val Val Gly Val Pro Ser Ile Ser Ser Gln Ala Lys Gln Leu Leu
100 105 110
Leu His His Thr Leu Gly Asn Gly Asp Phe Thr Val Phe His Arg Met
115 120 125
Ser Ala Asn Ile Ser Glu Thr Thr Ala Met Ile Thr Asp Ile Ala Asn
130 135 140
Ala Pro Ala Glu Ile Asp Arg Cys Ile Arg Thr Thr Tyr Thr Thr Gln
145 150 155 160
Arg Pro Val Tyr Leu Gly Leu Pro Ala Asn Leu Val Asp Leu Asn Val
165 170 175
Pro Ala Lys Leu Leu Glu Thr Pro Ile Asp Leu Ser Leu Lys Pro Asn
180 185 190
Asp Ala Glu Ala Glu Ala Glu Val Val Arg Thr Val Val Glu Leu Ile
195 200 205
Lys Asp Ala Lys Asn Pro Val Ile Leu Ala Asp Ala Cys Ala Ser Arg
210 215 220
His Asp Val Lys Ala Glu Thr Lys Lys Leu Met Asp Leu Thr Gln Phe
225 230 235 240
Pro Val Tyr Val Thr Pro Met Gly Lys Gly Ala Ile Asp Glu Gln His
245 250 255
Pro Arg Tyr Gly Gly Val Tyr Val Gly Thr Leu Ser Arg Pro Glu Val
260 265 270
Lys Lys Ala Val Glu Ser Ala Asp Leu Ile Leu Ser Ile Gly Ala Leu
275 280 285
Leu Ser Asp Phe Asn Thr Gly Ser Phe Ser Tyr Ser Tyr Lys Thr Lys
290 295 300
Asn Ile Val Glu Phe His Ser Asp His Ile Lys Ile Arg Asn Ala Thr
305 310 315 320
Phe Pro Gly Val Gln Met Lys Phe Ala Leu Gln Lys Leu Leu Asp Ala
325 330 335
Ile Pro Glu Val Val Lys Asp Tyr Lys Pro Val Ala Val Pro Ala Arg
340 345 350
Val Pro Ile Thr Lys Ser Thr Pro Ala Asn Thr Pro Met Lys Gln Glu
355 360 365
Trp Met Trp Asn His Leu Gly Asn Phe Leu Arg Glu Gly Asp Ile Val
370 375 380
Ile Ala Glu Thr Gly Thr Ser Ala Phe Gly Ile Asn Gln Thr Thr Phe
385 390 395 400
Pro Thr Asp Val Tyr Ala Ile Val Gln Val Leu Trp Gly Ser Ile Gly
405 410 415
Phe Thr Val Gly Ala Leu Leu Gly Ala Thr Met Ala Ala Glu Glu Leu
420 425 430
Asp Pro Lys Lys Arg Val Ile Leu Phe Ile Gly Asp Gly Ser Leu Gln
435 440 445
Leu Thr Val Gln Glu Ile Ser Thr Met Ile Arg Trp Gly Leu Lys Pro
450 455 460
Tyr Ile Phe Val Leu Asn Asn Asn Gly Tyr Thr Ile Glu Lys Leu Ile
465 470 475 480
His Gly Pro His Ala Glu Tyr Asn Glu Ile Gln Gly Trp Asp His Leu
485 490 495
Ala Leu Leu Pro Thr Phe Gly Ala Arg Asn Tyr Glu Thr His Arg Val
500 505 510
Ala Thr Thr Gly Glu Trp Glu Lys Leu Thr Gln Asp Lys Asp Phe Gln
515 520 525
Asp Asn Ser Lys Ile Arg Met Ile Glu Val Met Leu Pro Val Phe Asp
530 535 540
Ala Pro Gln Asn Leu Val Lys Gln Ala Gln Leu Thr Ala Ala Thr Asn
545 550 555 560
Ala Lys Gln
<210> 73
<211> 563
<212> PRT
<213> Saccharomyces cerevisiae PDC6
<400> 73
Met Ser Glu Ile Thr Leu Gly Lys Tyr Leu Phe Glu Arg Leu Lys Gln
1 5 10 15
Val Asn Val Asn Thr Ile Phe Gly Leu Pro Gly Asp Phe Asn Leu Ser
20 25 30
Leu Leu Asp Lys Ile Tyr Glu Val Asp Gly Leu Arg Trp Ala Gly Asn
35 40 45
Ala Asn Glu Leu Asn Ala Ala Tyr Ala Ala Asp Gly Tyr Ala Arg Ile
50 55 60
Lys Gly Leu Ser Val Leu Val Thr Thr Phe Gly Val Gly Glu Leu Ser
65 70 75 80
Ala Leu Asn Gly Ile Ala Gly Ser Tyr Ala Glu His Val Gly Val Leu
85 90 95
His Val Val Gly Val Pro Ser Ile Ser Ala Gln Ala Lys Gln Leu Leu
100 105 110
Leu His His Thr Leu Gly Asn Gly Asp Phe Thr Val Phe His Arg Met
115 120 125
Ser Ala Asn Ile Ser Glu Thr Thr Ser Met Ile Thr Asp Ile Ala Thr
130 135 140
Ala Pro Ser Glu Ile Asp Arg Leu Ile Arg Thr Thr Phe Ile Thr Gln
145 150 155 160
Arg Pro Ser Tyr Leu Gly Leu Pro Ala Asn Leu Val Asp Leu Lys Val
165 170 175
Pro Gly Ser Leu Leu Glu Lys Pro Ile Asp Leu Ser Leu Lys Pro Asn
180 185 190
Asp Pro Glu Ala Glu Lys Glu Val Ile Asp Thr Val Leu Glu Leu Ile
195 200 205
Gln Asn Ser Lys Asn Pro Val Ile Leu Ser Asp Ala Cys Ala Ser Arg
210 215 220
His Asn Val Lys Lys Glu Thr Gln Lys Leu Ile Asp Leu Thr Gln Phe
225 230 235 240
Pro Ala Phe Val Thr Pro Leu Gly Lys Gly Ser Ile Asp Glu Gln His
245 250 255
Pro Arg Tyr Gly Gly Val Tyr Val Gly Thr Leu Ser Lys Gln Asp Val
260 265 270
Lys Gln Ala Val Glu Ser Ala Asp Leu Ile Leu Ser Val Gly Ala Leu
275 280 285
Leu Ser Asp Phe Asn Thr Gly Ser Phe Ser Tyr Ser Tyr Lys Thr Lys
290 295 300
Asn Val Val Glu Phe His Ser Asp Tyr Val Lys Val Lys Asn Ala Thr
305 310 315 320
Phe Leu Gly Val Gln Met Lys Phe Ala Leu Gln Asn Leu Leu Lys Val
325 330 335
Ile Pro Asp Val Val Lys Gly Tyr Lys Ser Val Pro Val Pro Thr Lys
340 345 350
Thr Pro Ala Asn Lys Gly Val Pro Ala Ser Thr Pro Leu Lys Gln Glu
355 360 365
Trp Leu Trp Asn Glu Leu Ser Lys Phe Leu Gln Glu Gly Asp Val Ile
370 375 380
Ile Ser Glu Thr Gly Thr Ser Ala Phe Gly Ile Asn Gln Thr Ile Phe
385 390 395 400
Pro Lys Asp Ala Tyr Gly Ile Ser Gln Val Leu Trp Gly Ser Ile Gly
405 410 415
Phe Thr Thr Gly Ala Thr Leu Gly Ala Ala Phe Ala Ala Glu Glu Ile
420 425 430
Asp Pro Asn Lys Arg Val Ile Leu Phe Ile Gly Asp Gly Ser Leu Gln
435 440 445
Leu Thr Val Gln Glu Ile Ser Thr Met Ile Arg Trp Gly Leu Lys Pro
450 455 460
Tyr Leu Phe Val Leu Asn Asn Asp Gly Tyr Thr Ile Glu Lys Leu Ile
465 470 475 480
His Gly Pro His Ala Glu Tyr Asn Glu Ile Gln Thr Trp Asp His Leu
485 490 495
Ala Leu Leu Pro Ala Phe Gly Ala Lys Lys Tyr Glu Asn His Lys Ile
500 505 510
Ala Thr Thr Gly Glu Trp Asp Ala Leu Thr Thr Asp Ser Glu Phe Gln
515 520 525
Lys Asn Ser Val Ile Arg Leu Ile Glu Leu Lys Leu Pro Val Phe Asp
530 535 540
Ala Pro Glu Ser Leu Ile Lys Gln Ala Gln Leu Thr Ala Ala Thr Asn
545 550 555 560
Ala Lys Gln
<210> 74
<211> 506
<212> PRT
<213> Saccharomyces cerevisiae ALD2
<400> 74
Met Pro Thr Leu Tyr Thr Asp Ile Glu Ile Pro Gln Leu Lys Ile Ser
1 5 10 15
Leu Lys Gln Pro Leu Gly Leu Phe Ile Asn Asn Glu Phe Cys Pro Ser
20 25 30
Ser Asp Gly Lys Thr Ile Glu Thr Val Asn Pro Ala Thr Gly Glu Pro
35 40 45
Ile Thr Ser Phe Gln Ala Ala Asn Glu Lys Asp Val Asp Lys Ala Val
50 55 60
Lys Ala Ala Arg Ala Ala Phe Asp Asn Val Trp Ser Lys Thr Ser Ser
65 70 75 80
Glu Gln Arg Gly Ile Tyr Leu Ser Asn Leu Leu Lys Leu Ile Glu Glu
85 90 95
Glu Gln Asp Thr Leu Ala Ala Leu Glu Thr Leu Asp Ala Gly Lys Pro
100 105 110
Tyr His Ser Asn Ala Lys Gly Asp Leu Ala Gln Ile Leu Gln Leu Thr
115 120 125
Arg Tyr Phe Ala Gly Ser Ala Asp Lys Phe Asp Lys Gly Ala Thr Ile
130 135 140
Pro Leu Thr Phe Asn Lys Phe Ala Tyr Thr Leu Lys Val Pro Phe Gly
145 150 155 160
Val Val Ala Gln Ile Val Pro Trp Asn Tyr Pro Leu Ala Met Ala Cys
165 170 175
Trp Lys Leu Gln Gly Ala Leu Ala Ala Gly Asn Thr Val Ile Ile Lys
180 185 190
Pro Ala Glu Asn Thr Ser Leu Ser Leu Leu Tyr Phe Ala Thr Leu Ile
195 200 205
Lys Lys Ala Gly Phe Pro Pro Gly Val Val Asn Ile Val Pro Gly Tyr
210 215 220
Gly Ser Leu Val Gly Gln Ala Leu Ala Ser His Met Asp Ile Asp Lys
225 230 235 240
Ile Ser Phe Thr Gly Ser Thr Lys Val Gly Gly Phe Val Leu Glu Ala
245 250 255
Ser Gly Gln Ser Asn Leu Lys Asp Val Thr Leu Glu Cys Gly Gly Lys
260 265 270
Ser Pro Ala Leu Val Phe Glu Asp Ala Asp Leu Asp Lys Ala Ile Asp
275 280 285
Trp Ile Ala Ala Gly Ile Phe Tyr Asn Ser Gly Gln Asn Cys Thr Ala
290 295 300
Asn Ser Arg Val Tyr Val Gln Ser Ser Ile Tyr Asp Lys Phe Val Glu
305 310 315 320
Lys Phe Lys Glu Thr Ala Lys Lys Glu Trp Asp Val Ala Gly Lys Phe
325 330 335
Asp Pro Phe Asp Glu Lys Cys Ile Val Gly Pro Val Ile Ser Ser Thr
340 345 350
Gln Tyr Asp Arg Ile Lys Ser Tyr Ile Glu Arg Gly Lys Arg Glu Glu
355 360 365
Lys Leu Asp Met Phe Gln Thr Ser Glu Phe Pro Ile Gly Gly Ala Lys
370 375 380
Gly Tyr Phe Ile Pro Pro Thr Ile Phe Thr Asp Val Pro Gln Thr Ser
385 390 395 400
Lys Leu Leu Gln Asp Glu Ile Phe Gly Pro Val Val Val Val Ser Lys
405 410 415
Phe Thr Asn Tyr Asp Asp Ala Leu Lys Leu Ala Asn Asp Thr Cys Tyr
420 425 430
Gly Leu Ala Ser Ala Val Phe Thr Lys Asp Val Lys Lys Ala His Met
435 440 445
Phe Ala Arg Asp Ile Lys Ala Gly Thr Val Trp Ile Asn Ser Ser Asn
450 455 460
Asp Glu Asp Val Thr Val Pro Phe Gly Gly Phe Lys Met Ser Gly Ile
465 470 475 480
Gly Arg Glu Leu Gly Gln Ser Gly Val Asp Thr Tyr Leu Gln Thr Lys
485 490 495
Ala Val His Ile Asn Leu Ser Leu Asp Asn
500 505
<210> 75
<211> 506
<212> PRT
<213> Saccharomyces cerevisiae ALD3
<400> 75
Met Pro Thr Leu Tyr Thr Asp Ile Glu Ile Pro Gln Leu Lys Ile Ser
1 5 10 15
Leu Lys Gln Pro Leu Gly Leu Phe Ile Asn Asn Glu Phe Cys Pro Ser
20 25 30
Ser Asp Gly Lys Thr Ile Glu Thr Val Asn Pro Ala Thr Gly Glu Pro
35 40 45
Ile Thr Ser Phe Gln Ala Ala Asn Glu Lys Asp Val Asp Lys Ala Val
50 55 60
Lys Ala Ala Arg Ala Ala Phe Asp Asn Val Trp Ser Lys Thr Ser Ser
65 70 75 80
Glu Gln Arg Gly Ile Tyr Leu Ser Asn Leu Leu Lys Leu Ile Glu Glu
85 90 95
Glu Gln Asp Thr Leu Ala Ala Leu Glu Thr Leu Asp Ala Gly Lys Pro
100 105 110
Phe His Ser Asn Ala Lys Gln Asp Leu Ala Gln Ile Ile Glu Leu Thr
115 120 125
Arg Tyr Tyr Ala Gly Ala Val Asp Lys Phe Asn Met Gly Glu Thr Ile
130 135 140
Pro Leu Thr Phe Asn Lys Phe Ala Tyr Thr Leu Lys Val Pro Phe Gly
145 150 155 160
Val Val Ala Gln Ile Val Pro Trp Asn Tyr Pro Leu Ala Met Ala Cys
165 170 175
Arg Lys Met Gln Gly Ala Leu Ala Ala Gly Asn Thr Val Ile Ile Lys
180 185 190
Pro Ala Glu Asn Thr Ser Leu Ser Leu Leu Tyr Phe Ala Thr Leu Ile
195 200 205
Lys Lys Ala Gly Phe Pro Pro Gly Val Val Asn Val Ile Pro Gly Tyr
210 215 220
Gly Ser Val Val Gly Lys Ala Leu Gly Thr His Met Asp Ile Asp Lys
225 230 235 240
Ile Ser Phe Thr Gly Ser Thr Lys Val Gly Gly Ser Val Leu Glu Ala
245 250 255
Ser Gly Gln Ser Asn Leu Lys Asp Ile Thr Leu Glu Cys Gly Gly Lys
260 265 270
Ser Pro Ala Leu Val Phe Glu Asp Ala Asp Leu Asp Lys Ala Ile Glu
275 280 285
Trp Val Ala Asn Gly Ile Phe Phe Asn Ser Gly Gln Ile Cys Thr Ala
290 295 300
Asn Ser Arg Val Tyr Val Gln Ser Ser Ile Tyr Asp Lys Phe Val Glu
305 310 315 320
Lys Phe Lys Glu Thr Ala Lys Lys Glu Trp Asp Val Ala Gly Lys Phe
325 330 335
Asp Pro Phe Asp Glu Lys Cys Ile Val Gly Pro Val Ile Ser Ser Thr
340 345 350
Gln Tyr Asp Arg Ile Lys Ser Tyr Ile Glu Arg Gly Lys Lys Glu Glu
355 360 365
Lys Leu Asp Met Phe Gln Thr Ser Glu Phe Pro Ile Gly Gly Ala Lys
370 375 380
Gly Tyr Phe Ile Pro Pro Thr Ile Phe Thr Asp Val Pro Glu Thr Ser
385 390 395 400
Lys Leu Leu Arg Asp Glu Ile Phe Gly Pro Val Val Val Val Ser Lys
405 410 415
Phe Thr Asn Tyr Asp Asp Ala Leu Lys Leu Ala Asn Asp Thr Cys Tyr
420 425 430
Gly Leu Ala Ser Ala Val Phe Thr Lys Asp Val Lys Lys Ala His Met
435 440 445
Phe Ala Arg Asp Ile Lys Ala Gly Thr Val Trp Ile Asn Gln Thr Asn
450 455 460
Gln Glu Glu Ala Lys Val Pro Phe Gly Gly Phe Lys Met Ser Gly Ile
465 470 475 480
Gly Arg Glu Ser Gly Asp Thr Gly Val Asp Asn Tyr Leu Gln Ile Lys
485 490 495
Ser Val His Val Asp Leu Ser Leu Asp Lys
500 505
<210> 76
<211> 713
<212> PRT
<213> Saccharomyces cerevisiae ACS1
<400> 76
Met Ser Pro Ser Ala Val Gln Ser Ser Lys Leu Glu Glu Gln Ser Ser
1 5 10 15
Glu Ile Asp Lys Leu Lys Ala Lys Met Ser Gln Ser Ala Ala Thr Ala
20 25 30
Gln Gln Lys Lys Glu His Glu Tyr Glu His Leu Thr Ser Val Lys Ile
35 40 45
Val Pro Gln Arg Pro Ile Ser Asp Arg Leu Gln Pro Ala Ile Ala Thr
50 55 60
His Tyr Ser Pro His Leu Asp Gly Leu Gln Asp Tyr Gln Arg Leu His
65 70 75 80
Lys Glu Ser Ile Glu Asp Pro Ala Lys Phe Phe Gly Ser Lys Ala Thr
85 90 95
Gln Phe Leu Asn Trp Ser Lys Pro Phe Asp Lys Val Phe Ile Pro Asp
100 105 110
Pro Lys Thr Gly Arg Pro Ser Phe Gln Asn Asn Ala Trp Phe Leu Asn
115 120 125
Gly Gln Leu Asn Ala Cys Tyr Asn Cys Val Asp Arg His Ala Leu Lys
130 135 140
Thr Pro Asn Lys Lys Ala Ile Ile Phe Glu Gly Asp Glu Pro Gly Gln
145 150 155 160
Gly Tyr Ser Ile Thr Tyr Lys Glu Leu Leu Glu Glu Val Cys Gln Val
165 170 175
Ala Gln Val Leu Thr Tyr Ser Met Gly Val Arg Lys Gly Asp Thr Val
180 185 190
Ala Val Tyr Met Pro Met Val Pro Glu Ala Ile Ile Thr Leu Leu Ala
195 200 205
Ile Ser Arg Ile Gly Ala Ile His Ser Val Val Phe Ala Gly Phe Ser
210 215 220
Ser Asn Ser Leu Arg Asp Arg Ile Asn Asp Gly Asp Ser Lys Val Val
225 230 235 240
Ile Thr Thr Asp Glu Ser Asn Arg Gly Gly Lys Val Ile Glu Thr Lys
245 250 255
Arg Ile Val Asp Asp Ala Leu Arg Glu Thr Pro Gly Val Arg His Val
260 265 270
Leu Val Tyr Arg Lys Thr Asn Asn Pro Ser Val Ala Phe His Ala Pro
275 280 285
Arg Asp Leu Asp Trp Ala Thr Glu Lys Lys Lys Tyr Lys Thr Tyr Tyr
290 295 300
Pro Cys Thr Pro Val Asp Ser Glu Asp Pro Leu Phe Leu Leu Tyr Thr
305 310 315 320
Ser Gly Ser Thr Gly Ala Pro Lys Gly Val Gln His Ser Thr Ala Gly
325 330 335
Tyr Leu Leu Gly Ala Leu Leu Thr Met Arg Tyr Thr Phe Asp Thr His
340 345 350
Gln Glu Asp Val Phe Phe Thr Ala Gly Asp Ile Gly Trp Ile Thr Gly
355 360 365
His Thr Tyr Val Val Tyr Gly Pro Leu Leu Tyr Gly Cys Ala Thr Leu
370 375 380
Val Phe Glu Gly Thr Pro Ala Tyr Pro Asn Tyr Ser Arg Tyr Trp Asp
385 390 395 400
Ile Ile Asp Glu His Lys Val Thr Gln Phe Tyr Val Ala Pro Thr Ala
405 410 415
Leu Arg Leu Leu Lys Arg Ala Gly Asp Ser Tyr Ile Glu Asn His Ser
420 425 430
Leu Lys Ser Leu Arg Cys Leu Gly Ser Val Gly Glu Pro Ile Ala Ala
435 440 445
Glu Val Trp Glu Trp Tyr Ser Glu Lys Ile Gly Lys Asn Glu Ile Pro
450 455 460
Ile Val Asp Thr Tyr Trp Gln Thr Glu Ser Gly Ser His Leu Val Thr
465 470 475 480
Pro Leu Ala Gly Gly Val Thr Pro Met Lys Pro Gly Ser Ala Ser Phe
485 490 495
Pro Phe Phe Gly Ile Asp Ala Val Val Leu Asp Pro Asn Thr Gly Glu
500 505 510
Glu Leu Asn Thr Ser His Ala Glu Gly Val Leu Ala Val Lys Ala Ala
515 520 525
Trp Pro Ser Phe Ala Arg Thr Ile Trp Lys Asn His Asp Arg Tyr Leu
530 535 540
Asp Thr Tyr Leu Asn Pro Tyr Pro Gly Tyr Tyr Phe Thr Gly Asp Gly
545 550 555 560
Ala Ala Lys Asp Lys Asp Gly Tyr Ile Trp Ile Leu Gly Arg Val Asp
565 570 575
Asp Val Val Asn Val Ser Gly His Arg Leu Ser Thr Ala Glu Ile Glu
580 585 590
Ala Ala Ile Ile Glu Asp Pro Ile Val Ala Glu Cys Ala Val Val Gly
595 600 605
Phe Asn Asp Asp Leu Thr Gly Gln Ala Val Ala Ala Phe Val Val Leu
610 615 620
Lys Asn Lys Ser Ser Trp Ser Thr Ala Thr Asp Asp Glu Leu Gln Asp
625 630 635 640
Ile Lys Lys His Leu Val Phe Thr Val Arg Lys Asp Ile Gly Pro Phe
645 650 655
Ala Ala Pro Lys Leu Ile Ile Leu Val Asp Asp Leu Pro Lys Thr Arg
660 665 670
Ser Gly Lys Ile Met Arg Arg Ile Leu Arg Lys Ile Leu Ala Gly Glu
675 680 685
Ser Asp Gln Leu Gly Asp Val Ser Thr Leu Ser Asn Pro Gly Ile Val
690 695 700
Arg His Leu Ile Asp Ser Val Lys Leu
705 710
<210> 77
<211> 348
<212> PRT
<213> Saccharomyces cerevisiae ADH1
<400> 77
Met Ser Ile Pro Glu Thr Gln Lys Gly Val Ile Phe Tyr Glu Ser His
1 5 10 15
Gly Lys Leu Glu Tyr Lys Asp Ile Pro Val Pro Lys Pro Lys Ala Asn
20 25 30
Glu Leu Leu Ile Asn Val Lys Tyr Ser Gly Val Cys His Thr Asp Leu
35 40 45
His Ala Trp His Gly Asp Trp Pro Leu Pro Val Lys Leu Pro Leu Val
50 55 60
Gly Gly His Glu Gly Ala Gly Val Val Val Gly Met Gly Glu Asn Val
65 70 75 80
Lys Gly Trp Lys Ile Gly Asp Tyr Ala Gly Ile Lys Trp Leu Asn Gly
85 90 95
Ser Cys Met Ala Cys Glu Tyr Cys Glu Leu Gly Asn Glu Ser Asn Cys
100 105 110
Pro His Ala Asp Leu Ser Gly Tyr Thr His Asp Gly Ser Phe Gln Gln
115 120 125
Tyr Ala Thr Ala Asp Ala Val Gln Ala Ala His Ile Pro Gln Gly Thr
130 135 140
Asp Leu Ala Gln Val Ala Pro Ile Leu Cys Ala Gly Ile Thr Val Tyr
145 150 155 160
Lys Ala Leu Lys Ser Ala Asn Leu Met Ala Gly His Trp Val Ala Ile
165 170 175
Ser Gly Ala Ala Gly Gly Leu Gly Ser Leu Ala Val Gln Tyr Ala Lys
180 185 190
Ala Met Gly Tyr Arg Val Leu Gly Ile Asp Gly Gly Glu Gly Lys Glu
195 200 205
Glu Leu Phe Arg Ser Ile Gly Gly Glu Val Phe Ile Asp Phe Thr Lys
210 215 220
Glu Lys Asp Ile Val Gly Ala Val Leu Lys Ala Thr Asp Gly Gly Ala
225 230 235 240
His Gly Val Ile Asn Val Ser Val Ser Glu Ala Ala Ile Glu Ala Ser
245 250 255
Thr Arg Tyr Val Arg Ala Asn Gly Thr Thr Val Leu Val Gly Met Pro
260 265 270
Ala Gly Ala Lys Cys Cys Ser Asp Val Phe Asn Gln Val Val Lys Ser
275 280 285
Ile Ser Ile Val Gly Ser Tyr Val Gly Asn Arg Ala Asp Thr Arg Glu
290 295 300
Ala Leu Asp Phe Phe Ala Arg Gly Leu Val Lys Ser Pro Ile Lys Val
305 310 315 320
Val Gly Leu Ser Thr Leu Pro Glu Ile Tyr Glu Lys Met Glu Lys Gly
325 330 335
Gln Ile Val Gly Arg Tyr Val Val Asp Thr Ser Lys
340 345
<210> 78
<211> 587
<212> PRT
<213> Saccharomyces cerevisiae DLD1
<400> 78
Met Leu Trp Lys Arg Thr Cys Thr Arg Leu Ile Lys Pro Ile Ala Gln
1 5 10 15
Pro Arg Gly Arg Leu Val Arg Arg Ser Cys Tyr Arg Tyr Ala Ser Thr
20 25 30
Gly Thr Gly Ser Thr Asp Ser Ser Ser Gln Trp Leu Lys Tyr Ser Val
35 40 45
Ile Ala Ser Ser Ala Thr Leu Phe Gly Tyr Leu Phe Ala Lys Asn Leu
50 55 60
Tyr Ser Arg Glu Thr Lys Glu Asp Leu Ile Glu Lys Leu Glu Met Val
65 70 75 80
Lys Lys Ile Asp Pro Val Asn Ser Thr Leu Lys Leu Ser Ser Leu Asp
85 90 95
Ser Pro Asp Tyr Leu His Asp Pro Val Lys Ile Asp Lys Val Val Glu
100 105 110
Asp Leu Lys Gln Val Leu Gly Asn Lys Pro Glu Asn Tyr Ser Asp Ala
115 120 125
Lys Ser Asp Leu Asp Ala His Ser Asp Thr Tyr Phe Asn Thr His His
130 135 140
Pro Ser Pro Glu Gln Arg Pro Arg Ile Ile Leu Phe Pro His Thr Thr
145 150 155 160
Glu Glu Val Ser Lys Ile Leu Lys Ile Cys His Asp Asn Asn Met Pro
165 170 175
Val Val Pro Phe Ser Gly Gly Thr Ser Leu Glu Gly His Phe Leu Pro
180 185 190
Thr Arg Ile Gly Asp Thr Ile Thr Val Asp Leu Ser Lys Phe Met Asn
195 200 205
Asn Val Val Lys Phe Asp Lys Leu Asp Leu Asp Ile Thr Val Gln Ala
210 215 220
Gly Leu Pro Trp Glu Asp Leu Asn Asp Tyr Leu Ser Asp His Gly Leu
225 230 235 240
Met Phe Gly Cys Asp Pro Gly Pro Gly Ala Gln Ile Gly Gly Cys Ile
245 250 255
Ala Asn Ser Cys Ser Gly Thr Asn Ala Tyr Arg Tyr Gly Thr Met Lys
260 265 270
Glu Asn Ile Ile Asn Met Thr Ile Val Leu Pro Asp Gly Thr Ile Val
275 280 285
Lys Thr Lys Lys Arg Pro Arg Lys Ser Ser Ala Gly Tyr Asn Leu Asn
290 295 300
Gly Leu Phe Val Gly Ser Glu Gly Thr Leu Gly Ile Val Thr Glu Ala
305 310 315 320
Thr Val Lys Cys His Val Lys Pro Lys Ala Glu Thr Val Ala Val Val
325 330 335
Ser Phe Asp Thr Ile Lys Asp Ala Ala Ala Cys Ala Ser Asn Leu Thr
340 345 350
Gln Ser Gly Ile His Leu Asn Ala Met Glu Leu Leu Asp Glu Asn Met
355 360 365
Met Lys Leu Ile Asn Ala Ser Glu Ser Thr Asp Arg Cys Asp Trp Val
370 375 380
Glu Lys Pro Thr Met Phe Phe Lys Ile Gly Gly Arg Ser Pro Asn Ile
385 390 395 400
Val Asn Ala Leu Val Asp Glu Val Lys Ala Val Ala Gln Leu Asn His
405 410 415
Cys Asn Ser Phe Gln Phe Ala Lys Asp Asp Asp Glu Lys Leu Glu Leu
420 425 430
Trp Glu Ala Arg Lys Val Ala Leu Trp Ser Val Leu Asp Ala Asp Lys
435 440 445
Ser Lys Asp Lys Ser Ala Lys Ile Trp Thr Thr Asp Val Ala Val Pro
450 455 460
Val Ser Gln Phe Asp Lys Val Ile His Glu Thr Lys Lys Asp Met Gln
465 470 475 480
Ala Ser Lys Leu Ile Asn Ala Ile Val Gly His Ala Gly Asp Gly Asn
485 490 495
Phe His Ala Phe Ile Val Tyr Arg Thr Pro Glu Glu His Glu Thr Cys
500 505 510
Ser Gln Leu Val Asp Arg Met Val Lys Arg Ala Leu Asn Ala Glu Gly
515 520 525
Thr Cys Thr Gly Glu His Gly Val Gly Ile Gly Lys Arg Glu Tyr Leu
530 535 540
Leu Glu Glu Leu Gly Glu Ala Pro Val Asp Leu Met Arg Lys Ile Lys
545 550 555 560
Leu Ala Ile Asp Pro Lys Arg Ile Met Asn Pro Asp Lys Ile Phe Lys
565 570 575
Thr Asp Pro Asn Glu Pro Ala Asn Asp Tyr Arg
580 585
Claims (7)
- (a) 피루베이트 탈탄산효소(pyruvate decarboxylase, PDC)의 활성이 비변이 젖산 생산 균주에 비하여 약화되고;
(b) 알데히드 탈수소효소(aldehyde dehydrogenase, ALD) 및 acetyl-CoA 합성 효소(acetyl-CoA synthetase, ACS)의 활성이 비변이 젖산 생산 균주에 비하여 증진되도록 변이되고; 및
(c) 젖산 탈수소 효소(lactate dehydrogenase, LDH)가 도입된, 젖산 생산이 향상된 사카로마이세스 세레비지에(Saccharomyces cerevisiae) 미생물.
- 제1항에 있어서, 상기 피루베이트 탈탄산효소는 PDC1, PDC5 및 PDC6로 이루어진 군에서 선택된 하나 이상인 것인, 젖산 생산이 향상된 사카로마이세스 세레비지에 미생물.
- 제2항에 있어서, 상기 미생물은
i) PDC1의 활성을 불활성화하고 PDC5의 활성을 약화하거나; 또는
ii) PDC1의 활성을 약화하고 PDC5의 활성을 불활성화하는 것인, 젖산 생산이 향상된 사카로마이세스 세레비지에 미생물.
- 제1항에 있어서, 상기 알데히드 탈수소효소는 ALD2 및 ALD3로 이루어진 군으로부터 선택된 하나 이상인 것이며, 상기 acetyl-CoA 합성 효소는 ACS1인 것인, 젖산 생산이 향상된 사카로마이세스 세레비지에 미생물.
- 제1항에 있어서, 알코올 탈수소효소(alcohol dehydrogenase, ADH)가 추가로 불활성화된 것인, 젖산 생산이 향상된 사카로마이세스 세레비지에 미생물.
- 제1항에 있어서, D-젖산 탈수소효소(d-lactate dehydrogenase, DLD)가 추가로 불활성화된 것인, 젖산 생산이 향상된 사카로마이세스 세레비지에 미생물.
- (a) 제1항 내지 제6항 중 어느 한 항의 미생물을 배양하는 단계; 및
(b) 상기 (a) 단계의 배양액으로부터 젖산을 회수하는 단계를 포함하는 젖산 생산 방법.
Priority Applications (14)
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KR1020140055865A KR101577134B1 (ko) | 2014-05-09 | 2014-05-09 | 젖산 생산이 향상된 미생물 및 이를 이용하여 젖산을 생산하는 방법 |
BR112016026286-7A BR112016026286B1 (pt) | 2014-05-09 | 2015-05-08 | Micro-organismo com produtividade aumentada de ácido láctico e processo para produzir ácido láctico utilizando o mesmo |
CN201580030614.7A CN106459881B (zh) | 2014-05-09 | 2015-05-08 | 乳酸生产率提高的微生物和使用其生产乳酸的方法 |
MYPI2016001969A MY172440A (en) | 2014-05-09 | 2015-05-08 | A microorganism having enhanced productivity of lactic acid and a process for producing lactic acid using the same |
PL15739495T PL2960326T3 (pl) | 2014-05-09 | 2015-05-08 | Mikroorganizm zdolny do zwiększenia wytwarzania kwasu mlekowego i sposób wytwarzania kwasu mlekowego przy jego użyciu |
PCT/KR2015/004600 WO2015170914A1 (ko) | 2014-05-09 | 2015-05-08 | 젖산 생산이 향상된 미생물 및 이를 이용하여 젖산을 생산하는 방법 |
RU2015130528A RU2636467C2 (ru) | 2014-05-09 | 2015-05-08 | Микроорганизм, имеющий повышенную продуктивность в отношении молочной кислоты, и способ получения молочной кислоты с использованием данного микроорганизма |
EP15739495.8A EP2960326B1 (en) | 2014-05-09 | 2015-05-08 | Microorganism capable of enhancing lactic acid production and method for producing lactic acid using same |
US14/783,012 US20170175150A1 (en) | 2014-05-09 | 2015-05-08 | Microorganism having enhanced productivity of lactic acid and a process for producing lactic acid using the same |
SG11201609397WA SG11201609397WA (en) | 2014-05-09 | 2015-05-08 | A microorganism having enhanced productivity of lactic acid and a process for producing lactic acid using the same |
AU2015249090A AU2015249090B2 (en) | 2014-05-09 | 2015-05-08 | A microorganism having enhanced productivity of lactic acid and a process for producing lactic acid using the same. |
JP2015563134A JP6087451B2 (ja) | 2014-05-09 | 2015-05-08 | 乳酸生産が向上した微生物及びこれを用いて乳酸を生産する方法 |
UAA201507617A UA118022C2 (uk) | 2014-05-09 | 2015-08-05 | Рекомбінантний мікроорганізм saccharomyces cerevisiae, який має підвищену здатність до продукування молочної кислоти, та спосіб продукування молочної кислоти |
US15/918,995 US20180201960A1 (en) | 2014-05-09 | 2018-03-12 | Microorganism having enhanced productivity of lactic acid and a process for producing lactic acid using the same |
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KR1020140055865A KR101577134B1 (ko) | 2014-05-09 | 2014-05-09 | 젖산 생산이 향상된 미생물 및 이를 이용하여 젖산을 생산하는 방법 |
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US (2) | US20170175150A1 (ko) |
EP (1) | EP2960326B1 (ko) |
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AU (1) | AU2015249090B2 (ko) |
MY (1) | MY172440A (ko) |
PL (1) | PL2960326T3 (ko) |
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FI20195716A1 (en) * | 2019-08-30 | 2021-03-01 | Finnfoam Oy | Genetically modified fungi and related methods and uses |
KR102460532B1 (ko) * | 2020-02-18 | 2022-10-31 | 주식회사 피코엔텍 | 글루타치온과 알데하이드탈수소효소를 생산하는 사카로마이세스 세레비지에 권피1,2,3 |
KR102460570B1 (ko) * | 2020-02-18 | 2022-10-28 | 주식회사 피코엔텍 | 신규한 돌연변이 효모를 함유하는 아토피 억제 조성물 |
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2018
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SG11201609397WA (en) | 2016-12-29 |
MY172440A (en) | 2019-11-26 |
UA118022C2 (uk) | 2018-11-12 |
WO2015170914A1 (ko) | 2015-11-12 |
RU2015130528A (ru) | 2017-05-17 |
AU2015249090B2 (en) | 2017-04-06 |
EP2960326A4 (en) | 2016-11-30 |
BR112016026286A2 (pt) | 2018-02-20 |
KR20150129266A (ko) | 2015-11-19 |
AU2015249090A1 (en) | 2015-11-26 |
EP2960326A1 (en) | 2015-12-30 |
CN106459881A (zh) | 2017-02-22 |
US20170175150A1 (en) | 2017-06-22 |
PL2960326T3 (pl) | 2019-09-30 |
RU2636467C2 (ru) | 2017-11-23 |
CN106459881B (zh) | 2020-08-25 |
JP6087451B2 (ja) | 2017-03-01 |
EP2960326B1 (en) | 2019-04-03 |
US20180201960A1 (en) | 2018-07-19 |
JP2016521115A (ja) | 2016-07-21 |
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