KR20220135401A - 과당 제조용 조성물 및 제조 방법 - Google Patents
과당 제조용 조성물 및 제조 방법 Download PDFInfo
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- KR20220135401A KR20220135401A KR1020210041008A KR20210041008A KR20220135401A KR 20220135401 A KR20220135401 A KR 20220135401A KR 1020210041008 A KR1020210041008 A KR 1020210041008A KR 20210041008 A KR20210041008 A KR 20210041008A KR 20220135401 A KR20220135401 A KR 20220135401A
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Abstract
본 발명은 자당 인산화 효소 또는 이를 발현하는 미생물; 또는 상기 미생물의 배양물 또는 분쇄물;을 포함함으로써, 저비용, 고수율로 과당을 제조할 수 있는 조성물 및 과당 제조 방법에 관한 것이다.
Description
본 발명은 과당 제조용 조성물 및 제조 방법에 관한 것이다.
과당은 과일 속에 주로 포함된 당의 하나로 포도당과 함께 대표적인 단당류에 속한다. 사탕수수, 사탕무, 옥수수로부터 주로 생산되며, 자당(설탕)의 1.2-1.8배에 달하는 단맛으로 당류 중 가장 강한 감미를 가져 상업적 감미료로써 널리 이용되고 있다. 과당은 산업적으로 전분으로부터 이소머화효소(Glucose isomerase)를 통해 생산되거나 자당으로부터 자당분해효소(Invertase)를 통해 생산된다. 하지만 포도당과 함께 생산되거나 기질로 사용된 포도당이 잔존함으로써 6탄당의 유사한 특성으로 인해 과당의 고순도 분리를 어렵게 하여 생산 공정의 비용을 상승시킨다.
본 발명에서는 과당의 고순도 분리를 용이하게 하기 위함과 동시에 과당 생산 공정의 비용을 절감하고자 자당으로부터 자당 인산화효소(Sucrose phosphorylase, SPase)를 통해 과당을 생산하는 반응을 이용하였다. 추가적 기질 글리세롤과 함께 기질로 사용된 자당은 전환 반응을 통해 과당과 함께 부가적으로 글루코실글리세롤을 생산한다. 글루코실글리세롤은 포도당과 글리세롤이 글리코시드 결합으로 형성되어 있는 당 복합체로 수분 유지 기능이 뛰어나 피부 보습을 향상시키며, 피부의 각질층에 투과하여 수분 손실을 차단하고 피부 탄력은 향상 시키는 것으로 알려져, 현재 다양한 세계적 화장품 회사의 노화방지, 보습을 위한 기초 화장품의 고기능성 원료로 이용되고 있다. 더불어 자당의 55%에 달하는 단맛을 가지지만 충치를 유발하지 않고, 섭취양의 19% 만이 장에서 이용되기 때문에 저칼로리 감미료로써 이용 가능하며, 프리바이오틱스로써의 기능 또한 가지고 있는 것으로 알려져 있다. 글루코실글리세롤과의 혼합액으로부터 과당의 분리는 쉽게 가능하며, 글루코실글리세롤은 고가의 기능성 물질이기 때문에 부수적 부가 가치를 얻을 수 있으며, 이를 통해 과당의 생산 비용 절감 또한 가능하다.
과당을 분리하지 않고 생산된 과당을 기질로 하여 순차적인 기능성 당류 생산 공정을 적용할 수 있다. 자연계에 극소량 존재하는 희귀당 사이코스는 과당의 세 번째 탄소가 에피머화된 형태를 가지며, 자당의 70%에 달하는 감미를 가지지만 섭취 시 대부분 배출되기 때문에 오직 자당의 5-10%에 달하는 0에 가까운 칼로리를 가져 자당 대체 감미료로써 각광받고 있다. 또한 복부지방 생성 효소의 활성 억제로 복부 지방을 감소시키며, 장내에서 포도당의 흡수를 저해하고 췌장의 섬 베타 세포를 보호하며 인슐린 감수성을 향상시키기 때문에 체중 조절을 위함 감미료 또는 당뇨병 환자를 위한 대체 감미료로써 이용 가능하다. 이즈모리에 의해 개발된 효소 전환 방법을 통해 과당으로부터 사이코스 에피머화효소(D-Psicose 3-epimerase, DPE)를 이용해 사이코스로의 전환이 가능하다. 이를 적용하여 생산된 과당을 사이코스로 전환하는, 글루코실글리세롤과 사이코스를 생산하는 순차적 기능성 당류 생산 공정을 적용하였다.
또한 과당의 부수적 부가 가치 창출과 사이코스의 분리 용이를 위해 사이코스 전환 반응 이후 잔존하는 과당을 만니톨로 전환하는 공정을 적용하였다. 현재까지 과당을 기질로 하여 사이코스를 생산하는 데 사용되는 사이코스 에피머화효소(Psicose 3-epimerase, DPE)는 반응 평형이 30% 전후에 미쳐 반응 이후에도 다량의 과당이 잔존하게 된다. 이는 과당과 사이코스의 유사한 물성으로 사이코스의 분리를 어렵게 한다. 당 알코올인 만니톨은 과당의 두 번째 탄소가 수소화된 형태를 가지며, 자당과 유사한 단맛을 가지지만 자당보다 낮은 1.6 kcal/g의 칼로리를 가지고 혈당 수치를 상승시키지 않기 때문에 당뇨병 환자를 위한 대체 감미료로써 이용되고 있다. 또한 충치를 유발하지 않으며, 강한 냉각 효과를 가져 식품에 민트 향과 맛을 내는데 이용되고 있으며, 낮은 흡습성을 가지기 때문에 껌이나 사탕, 건조과일의 코팅제로써 또한 이용되고 있다. 또한 안압 및 두개압을 낮추거나 삼투압성 이뇨제로써 작용해 의약용으로도 사용되고 있다. 만니톨은 과당을 기질로 하여 만니톨 탈수소효소(Mannitol 2-dehydrogenase, MDH)를 통해 생산 가능하다. 더불어 만니톨 탈수소효소가 보조인자로써 사용하는 NADH의 원활한 재생을 위해 포름산의 산화를 통해 NAD+를 환원하는 포름산 탈수소효소(Formate dehydrogenase, FDH)를 함께 도입해주었다. 사이코스 전환 반응 이후 잔존하는 다량의 과당을 다른 기능성 당 알코올인 만니톨로 전환해주면서 사이코스의 분리는 용이하며 과당의 부가 가치 또한 상승한다.
순차적으로 기능성 당류를 생산하는 공정을 적용함으로써 최종적으로 글루코실글리세롤, 사이코스, 만니톨이 생산된다. 현재까지 두 가지 이상의 기능성 당류를 순차적으로 생산하는 공정은 연구된 적 없는 첫 발명 사례이다. 기질의 부가 가치를 최대한으로 창출하는 저비용 고효율의 순차적 기능성 당류 생산 공정을 개발하여 고가 기능성 물질의 상업적 이용 가능성을 높이고자 본 발명을 고안하였다.
본 발명은 생산 수율이 우수한 과당 제조용 조성물 및 제조 방법을 제공하는 것을 목적으로 한다.
1. 자당 인산화 효소 또는 이를 발현하는 미생물; 또는 상기 미생물의 배양물 또는 분쇄물;을 포함하는 과당 제조용 조성물.
2. 위 1에 있어서, 상기 자당 인산화 효소는 서열번호 1 내지 4 중 어느 하나의 서열로 이루어지거나, 이와 서열 상동성이 80% 이상인 서열로 이루어진 것인 과당 제조용 조성물.
3. 위 1에 있어서, 상기 미생물은 내재적 또는 외인적으로 상기 효소를 발현하는 것인 과당 제조용 조성물.
4. 위 1에 있어서, 상기 미생물은 에셰리키아 속 또는 코리네박테리움 속 미생물인 과당 제조용 조성물.
5. 위 1에 있어서, 상기 미생물은 휴면 세포를 갖도록 유도된 것인 과당 제조용 조성물.
6. 위 1의 조성물; 및
과당을 기질로 사용하는 당류 생산 경로의 효소, 이를 발현하는 미생물, 상기 미생물의 배양물 또는 분쇄물을 더 포함하는 당류 제조용 조성물.
7. 위 6에 있어서, 상기 과당을 기질로 사용하는 당류 생산 경로는 사이코스 생산 경로, 만니톨 생산 경로, 타가토스 생산 경로, 소르비톨 생산 경로인 당류 제조용 조성물.
8. 위 6에 있어서, 자당 인산화 효소를 발현하는 미생물이 과당을 기질로 사용하는 당류 생산 경로의 효소도 발현하는 것인 당류 제조용 조성물.
9. 자당 및 글리세롤을 위 1 내지 5 중 어느 한 항의 조성물과 반응시키는 단계를 포함하는 과당의 제조 방법.
10. 위 9에 있어서, 반응액에서 과당을 분리하는 단계를 더 포함하는 과당의 제조 방법.
11. 위 9에 있어서, 상기 조성물은 상기 미생물을 포함하는 것이고, 상기 각 반응은 상기 미생물 내에서 수행되는 것인 과당의 제조 방법.
12. 위 11에 있어서, 상기 자당과 자당 인산화 효소의 반응 전에 상기 미생물을 생육배지에서 배양하여 휴면 세포를 갖도록 유도하는 단계를 더 포함하는 과당의 제조 방법.
13. 위 9에 있어서, 상기 반응은 버퍼를 포함하지 않는 반응액에서 수행되는 것인 과당의 제조 방법.
14. 자당 및 글리세롤을 위 6 내지 8 중 어느 한 항의 조성물과 반응시키는 단계를 포함하는 당류의 제조 방법.
15. 위 14에 있어서, 상기 당류는 사이코스, 만니톨, 타가토스 또는 소르비톨이고, 상기 조성물은 상기 당류 합성 경로의 효소, 이를 발현하는 미생물, 상기 미생물의 배양물 또는 분쇄물을 포함하는 것인 당류의 제조 방법.
본 발명은 높은 수율로 과당을 제조할 수 있다.
본 발명은 과당 제조 비용을 절감할 수 있다.
도 1은 효소 반응을 통해 자당으로부터 과당 또는 그 이후 경로의 당류가 제조되는 과정을 나타낸 것이다.
도 2는 재조합 대장균을 이용한 과당 생산 공정 구축 및 효소의 활성 비교 결과이다. 도 2A는 자당인산화효소에 따른 과당 생산 결과를 나타낸 것이며, 도 2B는 글루코실글리세롤 생산 결과를 나타낸 것이며, 도 2C, 2D는 자당 및 글리세롤 소모 결과를 나타낸 것이다. 알로스카르도비아 크리세티 유래 자당 인산화효소는 Ac, 비피도박테리움 아돌레센티스 유래 자당 인산화효소는 Ba, 비피도박테리움 슈도롱검 유래 자당 인산화효소는 Bp, 써마내로쓰릭스 닥센시스 유래 자당 인산화효소는 Td로 표시되었다.
도 3은 버퍼 유무에 따른 자당 인산화효소의 생산성 비교 결과이다. 도 3A는 버퍼 유무에 따른 과당 생산성을 나타낸 것이며, 도 3B는 버퍼 유무에 따른 pH 변화를 나타낸 것이다. 알로스카르도비아 크리세티 유래 자당 인산화효소는 Ac, 비피도박테리움 아돌레센티스 유래 자당 인산화효소는 Ba, 비피도박테리움 슈도롱검 유래 자당 인산화효소는 Bp, 써마내로쓰릭스 닥센시스 유래 자당 인산화효소는 Td로 표시되었고, O는 버퍼를 사용한 경우, X는 사용하지 않은 경우를 나타낸 것이다.
도 4는 대장균을 전세포로 한 자당 인산화효소의 활성 비교 결과를 도표로 나타낸 것이다. 도 4A는 자당인산화효소에 따른 과당 생산성 비교 결과를 나타낸 것이며, 도 4B는 자당 인산화효소에 따른 글루코실글리세롤 생산성 비교 결과를 나타낸 것이며, 도 4C는 자당 인산화효소에 따른 자당 소모 결과를 나타낸 것이며, 도 4D는 자당 인산화효소에 따른 글리세롤 소모 결과를 나타낸 것이다. 알로스카르도비아 크리세티 유래 자당 인산화효소는 Ac, 비피도박테리움 아돌레센티스 유래 자당 인산화효소는 Ba, 비피도박테리움 슈도롱검 유래 자당 인산화효소는 Bp, 써마내로쓰릭스 닥센시스 유래 자당 인산화효소는 Td로 표시되었다.
도 5는 순차적 기능성 당류 생산 공정에서 사용되거나 생산되는 물질의 고성능액체크로마토그래피 크로마토그램을 나타낸 것이다.
도 6은 당 리파이너리를 이용한 기능성 당류 생산 결과를 도표로 나타낸 것이다. 첫 번째 공정은 과당 및 글루코실글리세롤 생산 공정 결과를 나타낸 것이며, 두 번째 공정은 사이코스 생산 공정 결과를 나타낸 것이며, 세 번째 공정은 만니톨 생산 공정 결과를 나타낸 것이다.
도 2는 재조합 대장균을 이용한 과당 생산 공정 구축 및 효소의 활성 비교 결과이다. 도 2A는 자당인산화효소에 따른 과당 생산 결과를 나타낸 것이며, 도 2B는 글루코실글리세롤 생산 결과를 나타낸 것이며, 도 2C, 2D는 자당 및 글리세롤 소모 결과를 나타낸 것이다. 알로스카르도비아 크리세티 유래 자당 인산화효소는 Ac, 비피도박테리움 아돌레센티스 유래 자당 인산화효소는 Ba, 비피도박테리움 슈도롱검 유래 자당 인산화효소는 Bp, 써마내로쓰릭스 닥센시스 유래 자당 인산화효소는 Td로 표시되었다.
도 3은 버퍼 유무에 따른 자당 인산화효소의 생산성 비교 결과이다. 도 3A는 버퍼 유무에 따른 과당 생산성을 나타낸 것이며, 도 3B는 버퍼 유무에 따른 pH 변화를 나타낸 것이다. 알로스카르도비아 크리세티 유래 자당 인산화효소는 Ac, 비피도박테리움 아돌레센티스 유래 자당 인산화효소는 Ba, 비피도박테리움 슈도롱검 유래 자당 인산화효소는 Bp, 써마내로쓰릭스 닥센시스 유래 자당 인산화효소는 Td로 표시되었고, O는 버퍼를 사용한 경우, X는 사용하지 않은 경우를 나타낸 것이다.
도 4는 대장균을 전세포로 한 자당 인산화효소의 활성 비교 결과를 도표로 나타낸 것이다. 도 4A는 자당인산화효소에 따른 과당 생산성 비교 결과를 나타낸 것이며, 도 4B는 자당 인산화효소에 따른 글루코실글리세롤 생산성 비교 결과를 나타낸 것이며, 도 4C는 자당 인산화효소에 따른 자당 소모 결과를 나타낸 것이며, 도 4D는 자당 인산화효소에 따른 글리세롤 소모 결과를 나타낸 것이다. 알로스카르도비아 크리세티 유래 자당 인산화효소는 Ac, 비피도박테리움 아돌레센티스 유래 자당 인산화효소는 Ba, 비피도박테리움 슈도롱검 유래 자당 인산화효소는 Bp, 써마내로쓰릭스 닥센시스 유래 자당 인산화효소는 Td로 표시되었다.
도 5는 순차적 기능성 당류 생산 공정에서 사용되거나 생산되는 물질의 고성능액체크로마토그래피 크로마토그램을 나타낸 것이다.
도 6은 당 리파이너리를 이용한 기능성 당류 생산 결과를 도표로 나타낸 것이다. 첫 번째 공정은 과당 및 글루코실글리세롤 생산 공정 결과를 나타낸 것이며, 두 번째 공정은 사이코스 생산 공정 결과를 나타낸 것이며, 세 번째 공정은 만니톨 생산 공정 결과를 나타낸 것이다.
이하 본 발명을 상세히 설명한다.
본 발명은 과당 제조용 조성물에 관한 것이다.
본 발명의 조성물은 자당 인산화 효소 또는 이를 발현하는 미생물; 또는 상기 미생물의 배양물 또는 분쇄물;을 포함한다.
자당 인산화 효소(Sucrose phosphorylase, SPase)는 자당을 기질로 사용하여 이를 인산화시키는 효소이다.
구체적으로, 자당 인산화 효소는 자당 및 글리세롤을 함께 기질로 사용하여, 과당 및 글루코실글리세롤을 생산할 수 있다.
글리세롤, 글루코실글리세롤은 과당과 용해도 등의 물성 차이가 크므로 그 혼합액에서 과당을 고순도로 쉽게 분리해낼 수 있다.
자당 인산화 효소로는 자당 인산화 효소로 알려진 것, 그 외에 서열 상동성 등을 고려하여 동일한 기능을 할 수 있는 모든 단백질을 제한 없이 사용할 수 있으며, 예를 들면 서열번호 1 내지 4 중 어느 하나의 서열로 이루어지거나, 이와 서열 상동성이 80% 이상인 서열로 이루어진 펩티드를 사용할 수 있다.
자당 인산화 효소를 발현하는 미생물은 내재적 또는 외인적으로 상기 펩티드를 발현하는 것일 수 있다.
상기 펩티드를 외인적으로 발현하는 경우, 상기 미생물은 상기 펩티드를 코딩하는 유전자가 도입된 것일 수 있다.
유전자의 도입은 당 분야에 공지된 플라스미드, 레트로바이러스, 아데노바이러스 등의 바이러스성 벡터, 비바이러스성 벡터 등을 제한 없이 사용하여 수행된 것일 수 있다.
미생물은 원핵 세포 또는 진핵 세포로 액체 배지에서 배양될 수 있으면서, 전술한 고온의 온도에서 배양이 가능한 것일 수 있다. 상기 미생물은 예를 들면, 박테리아, 곰팡이, 또는 이들의 조합일 수 있다. 박테리아는 그람 양성 박테리아, 그람 음성 박테리아, 또는 이들의 조합일 수 있으며, 과당 생산성 증가의 측면에서 바람직하게는 그람 양성 박테리아일 수 있다. 그람 음성 박테리아는 에세리키아 (Escherichia) 속일 수 있다. 그람 양성 박테리아는 바실러스 속, 코리네박테리움 속, 액티노마이세스 속, 유산균 또는 이들의 조합일 수 있다. 곰팡이는 효모, 클루베로마이세스 속, 또는 이들의 조합일 수 있다.
미생물은 휴면 세포를 갖도록 유도된 것일 수 있다.
휴면 세포를 갖도록 하는 유도는 상기 미생물을 정지기(stationary phase)까지 배양함으로써 수행될 수 있다.
정지기까지의 배양은 기질을 포함하거나 포함하지 않는 배지에서 수행될 수 있고, 기질을 포함한 배지에서 배양하는 것이 미생물을 기질에 적응시킨다는 측면에서 바람직할 수 있다.
정지기까지의 배양은 생육배지에서 배양하여 수행될 수 있고, 이는 해당 미생물의 배양을 위해 공지된 성분들을 제한 없이 포함하는 것일 수 있다.
본 명세서에서 휴면세포(resting cell)는 더 이상 증식하지 않는 상태의 배양 세포를 의미한다. 본 명세서에서 정지기(stationary phase)는 세포를 배양하는 경우 대수기(exponential phase)를 지나 세포의 분열 및 증식이 정지하여 세포 개체 수의 증가가 나타나지 않으며, 세포 성분의 합성과 분해가 균형을 이룬 상태를 의미한다.
따라서, 본 발명에 따른 휴면 세포는 성장이 완료되고, 세포 내에서 상기 단백질의 발현이 충분히 이루어진 상태의 세포를 의미하는 것으로서, 미생물이 휴면 세포를 갖도록 유도되는 경우 자당 인산화효소의 발현량이 최대치를 나타내는 바, 과당 생산을 극대화할 수 있다.
미생물의 배양물은 배양 후 미생물을 포함한 배지, 배양 후 미생물은 분리된 배지 또는 배양 중 미생물이 분비한 물질 등을 포함하는 것일 수 있다. 배지는 고체 배지 또는 액체 배지일 수 있다.
미생물의 분쇄물은 sonication 등을 통한 미생물의 분쇄물로서, 상기 미생물 내의 상기 단백질을 포함하는 것일 수 있다.
또한, 본 발명은 당류 제조용 조성물에 관한 것이다.
당류 제조용 조성물은 상기 과당 제조용 조성물을 포함하고, 과당 이후 경로의 당류 제조에 필요한 물질을 더 포함한다.
상기 과당 제조용 조성물의 사용에 의해 자당으로부터 과당이 제조될 수 있는 바, 그 이후 경로 당류 제조에 필요한 물질을 더 포함하는 경우, 과당 제조 이후의 경로가 순차적으로 더 진행될 수 있다.
과당 이후 경로의 당류 제조에 필요한 물질은 과당을 기질로 사용하는 당류 생산 경로의 효소, 이를 발현하는 미생물, 상기 미생물의 배양물 또는 분쇄물일 수 있다.
제조 대상인 당류는 과당을 기질로 사용하여 제조될 수 있는 모든 당류에 제한 없이 적용될 수 있다. 예를 들면 사이코스 생산 경로, 만니톨 생산 경로, 타가토스 생산 경로, 소르비톨 생산 경로 등일 수 있다.
그 당류 생산 경로의 효소는 과당을 기질로 사용하는 효소부터 최종 목적 당류 생산까지에 사용되는 모든 효소를 포함하는 것으로서, 다양한 당류 생산 경로는 공지되어 있고, 그 생산에 참여하는 효소들도 공지되어 있는 바, 그러한 공지된 경로의 공지된 효소를 사용할 수 있다. 해당 효소들은 다양한 미생물 유래의 효소일 수 있다.
구체적인 예를 들자면, 생산하고자 하는 당류가 사이코스인 경우, 사이코스 에피머화 효소를 사용할 수 있고, 예를 들면 클로스트리디움 힐레모내(Clostridium hylemonae) 유래 사이코스 에피머화효소(GenBank ID: EEG74378.1, 서열번호 21)를 사용할 수 있다. 생산하고자 하는 당류가 만니톨인 경우, 이에 추가로 만니톨 탈수소 효소 및 포름산 탈수소 효소를 사용할 수 있다. 만니톨 탈수소 효소는 락토바실러스 루테리(Lactobacillus reuteri) 유래 만니톨 탈수소효소(GenBank ID: WP_003669358, 서열번호 22), 포름산 탈수소효소는 미코박테리움 바케에(Mycobacterium vaccae) 유래 포름산 탈수소효소(GenBank ID: BAB69476.1, 서열번호 23, MvFDH)를 사용할 수 있으나, 이에 제한되는 것은 아니다.
과당을 기질로 사용하는 당류 생산 경로의 효소에 추가로 필요한 기질이 있다면, 본 발명의 당류 제조용 조성물은 그러한 기질을 더 포함할 수 있다. 예를 들어, 당류가 만니톨인 경우, 포름산 탈수소 효소의 기질인 나트륨 포름산을 더 사용할 수 있다.
본 발명의 당류 제조용 조성물이 미생물, 그 배양물 또는 분쇄물을 포함하는 경우, 해당 미생물은 자당 인산화 효소를 발현하는 미생물 외에 별도로 포함될 수도 있고, 자당 인산화 효소를 발현하는 미생물이 과당을 기질로 사용하는 당류 생산 경로의 효소도 추가로 발현하는 것일 수 있다.
효소를 발현하는 미생물은 내재적 또는 외인적으로 상기 펩티드를 발현하는 것일 수 있다.
상기 펩티드를 외인적으로 발현하는 경우, 상기 미생물은 상기 펩티드를 코딩하는 유전자가 도입된 것일 수 있다.
유전자의 도입은 당 분야에 공지된 플라스미드, 레트로바이러스, 아데노바이러스 등의 바이러스성 벡터, 비바이러스성 벡터 등을 제한 없이 사용하여 수행된 것일 수 있다.
미생물은 원핵 세포 또는 진핵 세포로 액체 배지에서 배양될 수 있으면서, 전술한 고온의 온도에서 배양이 가능한 것일 수 있다. 상기 미생물은 예를 들면, 박테리아, 곰팡이, 또는 이들의 조합일 수 있다. 박테리아는 그람 양성 박테리아, 그람 음성 박테리아, 또는 이들의 조합일 수 있으며, 글루코실글리세롤 생산성 증가의 측면에서 바람직하게는 그람 양성 박테리아일 수 있다. 그람 음성 박테리아는 에세리키아 (Escherichia) 속일 수 있다. 그람 양성 박테리아는 바실러스 속, 코리네박테리움 속, 액티노마이세스 속, 유산균 또는 이들의 조합일 수 있다. 곰팡이는 효모, 클루베로마이세스 속, 또는 이들의 조합일 수 있다.
미생물은 휴면 세포를 갖도록 유도된 것일 수 있다.
또한, 본 발명은 과당의 제조 방법에 관한 것이다.
본 발명의 과당의 제조 방법은 자당 및 글리세롤을 상기 과당 제조용 조성물과 반응시키는 단계를 포함한다.
본 발명의 조성물이 자당 인산화 효소 또는 이를 발현하는 미생물; 또는 상기 미생물의 배양물 또는 분쇄물;을 포함하는 것이므로, 상기 반응은 예를 들면 미생물 내에서 수행될 수 있다.
상기 반응은 예를 들면 온도 30℃ 내지 90℃ 조건에서 수행될 수 있으나, 이에 제한되는 것은 아니다. 상기 범위 내에서 30℃ 내지 90℃, 30℃ 내지 80℃, 30℃ 내지 70℃, 40℃ 내지 80℃, 40℃ 내지 70℃, 45℃ 내지 70℃, 50℃ 내지 70℃ 등의 조건으로 수행될 수 있다.
반응시에 기질인 자당과 글리세롤의 비율은 특별히 한정되지 않으며, 예를 들면 몰비가 1: 0.1 내지 10일 수 있다. 상기 범위 내에서 1: 0.1 내지 10, 1: 0.1 내지 8, 1: 0.5 내지 8, 1: 1 내지 8, 1: 1 내지 5 등일 수 있다.
본 발명에 따른 조성물이 상기 미생물, 배양물 또는 분쇄물을 포함하는 경우, 본 발명의 방법은 상기 반응 이전에, 상기 미생물을 휴면 세포를 갖도록 유도하는 단계를 더 포함할 수 있다. 그러한 경우 과당의 생산을 극대화할 수 있다.
휴면 세포를 갖도록 하는 유도는 상기 미생물을 정지기(stationary phase)까지 배양함으로써 수행될 수 있다.
정지기까지의 배양은 기질을 포함하거나 포함하지 않는 배지에서 수행될 수 있고, 기질을 포함한 배지에서 배양하는 것이 미생물을 기질에 적응시킨다는 측면에서 바람직할 수 있다.
정지기까지의 배양은 생육배지에서 배양하여 수행될 수 있고, 이는 해당 미생물의 배양을 위해 공지된 성분들을 제한 없이 포함하는 것일 수 있다.
상기 반응은 예를 들면 버퍼를 포함하지 않는 반응액에서 수행되는 것일 수 있다. 효소 또는 미생물을 사용한 목적 산물의 생산 시에 통상 버퍼를 사용하여 pH를 일정 범위로 유지하고, 그렇지 않으면 효소 활성이 저하되어 생산 수율이 크게 저하된다. 본 발명의 방법은 버퍼를 포함하지 않는 반응액에서 반응을 수행하는 경우에도 우수한 생산 수율을 나타내어, 과당의 제조에 소요되는 시간, 비용 등을 줄일 수 있다.
자당 및 글리세롤을 상기 과당 제조용 조성물과 반응시키면 과당과 글루코실글리세롤의 혼합물이 얻어질 수 있고, 과당은 글리세롤, 글루코실글리세롤과 용해도 등의 물성 차이가 크므로, 글리세롤, 글루코실글리세롤로부터 쉽게 분리해낼 수 있다. 이에 본 발명의 방법은 반응 혼합액에서 과당을 분리하는 단계를 더 포함할 수 있다.
또한, 본 발명은 당류의 제조 방법에 관한 것이다.
본 발명의 당류의 제조 방법은 자당 및 글리세롤을 상기 당류 제조용 조성물과 반응시키는 단계를 포함한다.
당류 제조용 조성물은 상기 과당 제조용 조성물을 포함하므로, 자당 및 글리세롤이 과당 제조용 조성물과 반응하여 과당이 제조될 수 있고, 과당 이후 경로의 당류 제조에 필요한 물질을 더 포함하므로, 과당을 기질로 사용하여 제조될 수 있는 이후 경로의 당류 제조 반응이 추가로 진행될 수 있다.
상기 반응은 예를 들면 미생물 내에서 수행될 수 있다.
본 발명에 따른 조성물이 상기 미생물, 배양물 또는 분쇄물을 포함하는 경우, 본 발명의 방법은 상기 반응 이전에, 상기 미생물을 휴면 세포를 갖도록 유도하는 단계를 더 포함할 수 있다. 그러한 경우 과당의 생산을 극대화할 수 있다.
휴면 세포를 갖도록 하는 유도는 상기 미생물을 정지기(stationary phase)까지 배양함으로써 수행될 수 있다.
정지기까지의 배양은 기질을 포함하거나 포함하지 않는 배지에서 수행될 수 있고, 기질을 포함한 배지에서 배양하는 것이 미생물을 기질에 적응시킨다는 측면에서 바람직할 수 있다.
정지기까지의 배양은 생육배지에서 배양하여 수행될 수 있고, 이는 해당 미생물의 배양을 위해 공지된 성분들을 제한 없이 포함하는 것일 수 있다.
상기 반응은 예를 들면 버퍼를 포함하지 않는 반응액에서 수행되는 것일 수 있다. 효소 또는 미생물을 사용한 목적 산물의 생산시에 통상 버퍼를 사용하여 pH를 일정 범위로 유지하고, 그렇지 않으면 효소 활성이 저하되어 생산 수율이 크게 저하된다. 본 발명의 방법은 버퍼를 포함하지 않는 반응액에서 반응을 수행하는 경우에도 우수한 생산 수율을 나타내어, 당류의 제조에 소요되는 시간, 비용 등을 줄일 수 있다.
이하 실시예를 통해 본 발명을 보다 구체적으로 설명한다.
실시예
1. 재조합 대장균을 이용한 과당 생산 공정 구축 및 효소의 활성 비교
기존 사용하던 고온 고활성의 비피도박테리움 아돌레센티스(Bifidobacterium adolescentis) 유래 자당 인산화효소(GenBank ID: AAO33821.1, 서열번호 1, BaSPase)의 아미노산 서열을 주형으로 NCBI의 BLAST (https://blast.ncbi.nlm.nih.gov/Blast.cgi)를 이용해 상동성에 따른 다양한 균주 유래 아미노산 서열 결과를 얻었다. 그 중 비피도박테리움 아돌레센티스 유래 자당 인산화효소와 83.8%의 상동성을 가지는 비피도박테리움 슈도롱검(Bifidobacterium pseudolongum) 유래 자당 인산화효소(GenBank ID: WP_026643821.1, 서열번호 2, BpSPase), 76.2%의 상동성을 가지는 알로스카르도비아 크리세티(Alloscardovia criceti) 유래 자당 인산화효소(GenBank ID: WP_018142968.1, 서열번호 3, AcSPase), 55.1%의 상동성을 가지는 써마내로쓰릭스 닥센시스(Thermanaerothrix daxensis) 유래 자당 인산화효소(GenBank ID: WP_054521739.1, 서열번호 4, TdSPase)를 선별하였다. 알로스카르도비아 크리세티와 비피도박테리움 슈도롱검은 Korean Collection for Type Cultures (KCTC)로부터 KCTC 5819와 KCTC 3234를 분양 받아 사용하였으며, 써마내로쓰릭스 닥센시스는 German Collection of Microorganisms and Cell Cultures GmbH (DSMZ)의 DSM 23592를 분양 받아 사용하였다.
분양받은 균주의 게놈을 정제하여 각각의 자당 인산화효소 코딩 유전자 서열을 포함하도록 PCR을 수행하였다. 서열번호 5의 비피도박테리움 슈도롱검 유래 자당 인산화효소 코딩 유전자 서열의 PCR을 수행하기 위해 서열번호 6 및 7의 프라이머 쌍을 이용하였으며, 서열번호 8의 알로스카르도비아 크리세티 유래 자당 인산화효소 코딩 유전자 서열의 PCR을 수행하기 위해 서열번호 9 및 10의 프라이머 쌍을 이용하였으며, 서열번호 11의 써마내로쓰릭스 닥센시스 유래 자당 인산화효소 유래 자당 인산화효소 코딩 유전자 서열의 PCR을 수행하기 위해 서열번호 12 및 13의 프라이머 쌍을 이용하였다. 프라이머는 BIONEER (한국)에 의뢰하였으며, ThermoFisher SCIENTIFIC (미국)의 Phusion DNA Polymerase를 중합효소로 사용해 권장 조건에 따라 TaKaRa (일본)의 PCR Thermal Cycler Dice를 이용하여 PCR 진행하였다.
얻어진 PCR 산물은 NEW ENGLAND BioLabs (NEB, 영국)의 KpnI과 XbaI의 제한 효소를 사용해 trc 프로모터를 포함하는 대장균의 발현 벡터 pTrc99A에 도입하였으며, 그 결과 재조합 벡터 pT-AcSPase, pT-BpSPase 및 pT-TdSPase를 얻었다. 재조합 벡터는 글리세롤 인산화효소(Glucose kinase, glpk)가 결손된 대장균 BW 25113 △glpk 균주에 Sambrook 등의 Molecular Cloning 3rd (2001)를 참고한 화학적 방법으로 도입하였다. 형질 전환된 재조합 대장균은 -80℃에 보관하여 사용하였다.
플라스크를 통한 재조합 대장균을 대량 생육하였으며, OD 40의 세포 농도로 확보해 전세포 전환반응의 생촉매로 사용하였으며, 200 g/L 자당과 200 g/L 글리세롤을 함유하는 250 mM 피페스 (pH 7.0)를 전환 용액으로 하여 60℃의 전환 온도에서 180 rpm의 교반 속도로 6시간동안 전환 반응 진행하여 각 효소의 활성 비교하였다. 당은 SHIMADZU (일본)의 고성능액체크로마토그래피(High Performance Liquid Chromatography, HPLC)를 이용하여 분석하였으며, 85% 아세토니트릴을 이동상으로 하여 Kromasil (스웨덴)의 KR100-5NH2 (250Х4.6mm, 5μm) 칼럼과 굴절지수검출기(Reflective Index detector, RID)를 사용하였다. 결과는 도 2에 나타내었다.
도 2A의 과당 생산 결과를 참조해 보면, 알로스카르도비아 크리세티 유래 자당 인산화효소를 도입한 재조합 대장균이 2시간 이내에 반응 평형에 도달하여 생산 속도가 가장 빠를 뿐만 아니라, 최종 105.8 g/L의 과당을 생산하여 생산량 또한 가장 많았다. 비피도박테리움 슈도롱검 유래 자당 인산화효소와 써마내로쓰릭스 닥센시스 유래 자당 인산화효소를 도입한 재조합 대장균은 기존 사용하던 비피도박테리움 아돌레센티스 유래 자당 인산화효소와 유사한 과당 생산성을 보였으며, 모두 3시간 내에 반응 평형에 도달하였다.
도 2B의 글루코실글리세롤 결과를 참조해보면, 과당 생산 결과와 유사한 양상을 보여 알로스카르도비아 크리세티 유래 자당 인산화효소를 도입한 재조합 대장균이 가장 좋은 생산성을 보였으며, 최종 107.3 g/L의 글루코실글리세롤을 생산하였다.
도 2C와 2D의 자당 및 글리세롤 소모 결과를 보면 200 g/L의 자당은 모두 소모되는 반면, 200 g/L의 글리세롤은 200 g/L의 자당 몰 비율과 동일한 양 소모되어 약 50 g/L가 소모되고 150 g/L 가량이 잔존하였다. 글리세롤 또한 과당과의 물성 차이가 확연하기 때문에 과당의 고순도 분리에는 어떠한 영향을 주지 않을 것으로 생각된다.
모든 효소는 고유의 최적 활성 pH를 가지지만, pH를 유지하게 위해 사용하는 버퍼는 고가이기 때문에 최종 생산 비용을 상승시키고 반응액의 불순도를 높여 생산물의 고순도 분리를 어렵게 한다. 이러한 문제점은 산업적 공정으로의 발전을 어렵게 하기 때문에 pH 의존성이 낮은 효소의 발굴이 유리하다. 본 발명에서도 이를 적용하기 위해 새롭게 발굴한 자당 인산화효소의 pH에 따른 활성을 비교해 보았다. 상기 전환 반응에서는 자당 인산화효소의 최적 활성 pH로 알려진 pH 7.0을 유지하기 위해 250 mM 피페스 버퍼를 사용하였으며, 동일한 조건에서 버퍼를 첨가하지 않은 반응액을 사용하여 자당 인산화효소의 생산성을 비교해 보았다. 앞선 실험과 동일한 균주 및 생산 조건에서 피페스 버퍼를 포함하는 것과 포함하지 않는 것으로 나누어 앞서 선별한 모든 자당 인산화효소의 pH 의존도를 비교해 보았다. 결과는 도 3에 나타내었다.
버퍼 유무에 따른 과당 생산성을 나타낸 도 3A를 참조해보면, 비피도박테리움 슈도롱검 유래 자당 인산화효소는 버퍼를 사용하지 않았을 때, 버퍼를 사용하였을 때와 비교해 오히려 향상된 생산성을 보였다. 알로스카르도비아 크리세티 및 써마내로쓰릭스 닥센시스 유래 자당 인산화효소는 버퍼를 사용하지 않았을 때, 버퍼를 사용하였을 때와 유사한 생산성을 보였다. 하지만 비피도박테리움 아돌레센티스 유래 자당 인산화효소는 버퍼를 사용하지 않은 경우, 버퍼를 사용하였을 때와 비교해 32% 감소한 생산성을 보여 pH에 따른 활성 차이가 가장 크게 나타났다.
버퍼 유무에 따른 pH 변화를 나타낸 도 3B를 참조해보면, 250 mM 피페스(pH 7.0)을 사용하였을 때 자당 인산화효소의 유래에 상관 없이 전환 반응 동안 pH 6.6-6.8 사이를 유지하는 것으로 나타났지만, 버퍼를 사용하지 않은 경우에서는 1시간의 전환 반응 후 pH 5.4-5.8 사이로 하락해 이후 전환 반응 동안 유지되는 것으로 나타났다. 결과적으로 비피도박테리움 아돌레센티스 유래 자당 인산화효소는 pH 변화에 따른 활성 저하가 큰 것으로 나타나 효율적인 생산 효소로써 사용될 수 없는 것으로 보였지만, 새롭게 발굴한 알로스카르도비아 크리세티, 비피도박테리움 슈도롱검, 써마내로쓰릭스 닥센시스 유래 자당 인산화효소는 pH에 의존적이지 않은 것으로 보여 향후 효율적이고 경제적인 산업적 공정을 위한 생산 효소로써의 가치를 확인하였다.
2. 재조합 코리네박테리움을 이용한 과당 생산 공정 구축 및 효소의 활성 비교
고온에 유리한 공정을 구축하기 위해, 그람 양성균으로 두터운 세포벽을 가져 열에 안정적이며 GRAS 균주로 안전한 코리네박테리움을 이용해 신규 자당 인산화효소의 활성을 비교해 보았다. 정제한 각 균주의 게놈을 주형으로 자당 인산화효소 코딩 유전자 서열을 포함하도록 PCR을 수행하였다. BamHI과 NotI을 제한 효소로 사용하기 위하여 알로스카르도비아 크리세티 유래 자당 인산화효소 코딩 유전자 내 BamHI과 NotI 자리인 유전자 서열을 치환한 서열번호 14의 서열을 포함하도록 서열번호 15 및 16의 프라이머 쌍을 이용해 PCR 하였다. 서열번호 5의 비피도박테리움 슈도롱검 유래 자당 인산화효소 코딩 유전자를 포함하도록 서열번호 17 및 18의 프라이머 쌍을 이용하였으며, 서열번호 11의 써마내로쓰릭스 닥센시스 유래 자당 인산화효소 코딩 유전자를 포함하도록 서열번호 19 및 20의 프라이머 쌍을 이용하여 PCR 하였다. 얻어진 PCR 산물은 BamHI과 NotI의 제한 효소를 사용해 코리네박테리움용 강력 합성 프로모터 H30을 포함하는 대장균-코리네박테리움 셔틀 벡터 pCES-H30 (Yim SS, et al., 2013. Isolation of fully synthetic promoters for high-level gene expression in corynebacterium glutamicum)에 도입해 재조합 벡터 pCES-H30-AcSPase, pCES-H30-BpSPase 및 pCES-H30-TdSPase를 얻었다. 재조합 벡터는 야생형 코리네박테리움 글루타미쿰 ATCC 1302에 Eggeling 등의 Handbook of Corynebacterium glutamicum (2005)를 참고한 전기적 방법으로 도입하였다. 형질 전환된 재조합 코리네박테리움은 -80℃에 보관하여 사용하였다. pCES-H30-AcSPase, pCES-H30-BaSPase, pCES-H30-BpSPase 및 pCES-H30-TdSPase를 도입한 재조합 야생형 코리네박테리움 글루타미쿰 ATCC 13032 균주를 OD 40의 세포 농도로 확보하여 전세포 전환반응의 생촉매로 사용하였으며, 대장균을 이용한 전세포 전환반응과 동일한 전환 조건으로 과당 생산 전환 반응 진행하였다. 결과는 도 4에 나타내었다.
도 4A의 과당 생산성 결과를 참조해보면, 대장균에서의 결과와 동일하게 알로스카르도비아 크리세티 유래 자당 인산화효소를 도입한 코리네박테리움에서 가장 좋은 생산성을 나타내어 6시간의 전환 반응 후 101.6 g/L의 과당을 생산하여 대장균에서보다 코리네박테리움에서의 글루코실글리세롤 생산 속도가 현저히 감소함을 확인하였다.
도 4B의 글루코실글리세롤 생산 결과를 참조해보면, 과당 생산 결과와 유사한 양상을 보여 알로스카르도비아 크리세티 유래 자당 인산화효소를 도입한 재조합 코리네박테리움이 가장 좋은 생산성을 보였으며, 최종 6시간의 전환 반응 이후 85.9 g/L의 글루코실글리세롤을 생산하였다.
도 4C 및 도 4D의 자당 및 글리세롤 소모 결과를 참조해보면, 각 자당 인산화효소의 과당 생산량과 반비례하여 자당과 글리세롤이 소모됨을 확인 할 수 있었다.
코리네박테리움을 과당 생산 균주로 사용 시 대장균에 비해 저하된 생산성을 나타내었지만, 코리네박테리움에서의 자당 인산화효소 발현량을 증대시킨다면 대장균과 생산성은 유사하지만 더욱 고온에 안정적인 균주의 구축으로 과당 생산 공정의 생산성 및 생산 비용의 효율성을 극대화 한 고온 과당 생산 공정 적용이 가능할 것이다.
3. 자당으로부터 사이코스 및 만니톨의 순차적 생산 공정 개발
자당으로부터 과당을 생산하는 공정이 성공적으로 구축됨을 확인하여 이전의 연구에서 개발하였던 사이코스 및 만니톨 생산 공정을 순차적으로 적용해보았다.
상기 효소의 비교에서 가장 좋은 생산성을 보였던 알로스카르도비아 크리세티 유래 자당 인산화효소를 도입한 재조합 대장균을 OD 40의 세포 농도로 하여 200 g/L 자당과 200 g/L 글리세롤을 기질로 하는 250 mM PIPES (pH 7.0) 전환 용액을 사용해 60℃의 전환 온도, 180 rpm의 교반 속도에서 2시간 전세포 전환반응을 진행하였다. 이후 3,500 rpm에서 15분의 원심분리를 통해 세포와 반응액을 분리하였으며, 분리한 반응액을 두 번째 공정인 사이코스 생산 공정의 기질 및 반응 용액으로 사용하였다.
클로스트리디움 힐레모내(Clostridium hylemonae) 유래 사이코스 에피머화효소(GenBank ID: EEG74378.1, 서열번호 21, ChDPE)를 코딩하는 유전자를 도입한 재조합 코리네박테리움 글루타미쿰을 OD 40의 세포 농도로 확보해 생촉매로 사용하였으며, 효소의 활성 보조 인자인 망간을 0.12 mM 첨가해 주었다. 전세포 전환반응은 60℃의 전환 온도, 180 rpm의 교반 속도에서 1시간 진행하였다. 반응 이후 동일한 방법으로 분리한 반응액을 세 번째 만니톨 생산 공정의 기질 및 반응 용액으로 사용하였다.
락토바실러스 루테리(Lactobacillus reuteri) 유래 만니톨 탈수소효소(GenBank ID: WP_003669358, 서열번호 22, LrMDH)를 코딩하는 유전자 및 미코박테리움 바케에(Mycobacterium vaccae) 유래 포름산 탈수소효소(GenBank ID: BAB69476.1, 서열번호 23, MvFDH)를 코딩하는 유전자를 도입한 재조합 코리네박테리움 글루타미쿰을 OD 40의 세포 농도로 확보해 생촉매로 사용하였으며, 포름산 탈수소효소의 기질로 사용되는 나트륨포름산을 예상 잔존 과당 농도와 동일 몰 농도로 첨가해 주었다. 또한 만니톨 전환 반응은 초기 pH 6.0에서 좋은 활성을 보이기 때문에 50% 포름산을 이용해 pH를 보정해 주었으며, 45℃의 전환 온도, 180 rpm의 교반 속도에서 12시간 전환반응 진행하였다.
본 연구에서 현재까지 개발한 각 전환반응의 전환 수율은 과당 생산 공정은 자당의 농도 대비 100%, 사이코스 생산 공정의 전환 수율은 과당 대비 30%, 만니톨 생산 공정의 전환 수율은 과당 대비 60%이다. 각 물질의 고성능액체크로마토그래피 크로마토그램은 도 5에 나타내었으며, 전환 반응 결과는 도 6에 나타내었다.
도 6을 참조해보면, 첫 번째 공정인 과당 전환 반응 결과, 자당을 모두 사용하여 전환 수율에 따라 100 g/L 의 과당을 생산하였으며, 반응의 부산물로써 101 g/L의 글루코실글리세롤을 함께 생산하고 155 g/L 글리세롤이 잔존하였다. 이후 원심분리를 통해 세포와 반응액을 분리하는 과정 중 전세포로 사용한 대장균이 열에 장시간 노출됨에 따라 세포막이 물러지며 반응액에 섞여 당 농도가 희석되었고, 과당의 농도는 93 g/L, 글루코실글리세롤의 농도는 84 g/L, 글리세롤의 농도는 134 g/L가 되었다. 두 번째 전환 공정인 사이코스 전환 반응 후, 이론 수율과 유사한 62 g/L의 과당이 잔존하여 이론과 동일한 양의 과당이 사용된 것으로 보였지만, 예상 농도인 28 g/L보다 낮은 19 g/L의 사이코스가 생산되었다. 사이코스의 생산량이 감소한 것은 본래 사이코스 생산 공정에서 사용하던 400 g/L 보다 낮은 93 g/L를 사용함에 따라 전환 속도가 감소한 것으로 추정된다. 세 번째 전환 공정인 만니톨 전환 반응에서는 추가적인 기질인 포름산의 첨가 및 pH 보정에 따라 초기 당 농도가 과당 44 g/L, 글루코실글리세롤 66 g/L, 글리세롤 110 g/L, 사이코스 15 g/L로 희석되었다. 만니톨 전환 반응 이후 이론 수율과 같은 27 g/L의 만니톨이 생산되었으며, 14 g/L의 과당이 잔존하였고, 글리세롤과 글루코실글리세롤, 사이코스는 모두 반응 전과 동일양 유지되었다. 종합해보면, 200 g/L의 자당과 200 g/L의 글리세롤로부터 최종 세 가지의 기능성 당류, 글루코실글리세롤, 사이코스, 만니톨이 각각 68 g/L, 15 g/L, 27 g/L 생산되었다. 하지만 각 전환 반응으로 전환 시, 필요한 물질의 첨가보다 이외의 요인에 의해 더 많이 희석되었기 때문에 희석 배수를 곱해주어 원래의 반응 농도에 따른 생산량을 계산하여 나타내었다. 희석 배수는 첫 번째 반응 이후의 글리세롤과 글루코실글리세롤 양을 최종 반응 이후 남아있는 양과 비교하여 계산하였다. 희석 배수를 곱해준 결과로 최종 글루코실글리세롤, 사이코스, 만니톨이 99 g/L, 22 g/L, 39 g/L 생산됨을 확인하였다.
이로써 순차적 기능성 당류 생산 공정 적용을 통해 자당으로부터 세 가지의 기능성 당류를 차례로 생산하는 당 리파이너리의 개념이 실제 작동 가능하며, 성공적으로 구축됨을 확인할 수 있었다. 이는 저렴한 자당으로부터 부가 가치를 극대로 창출하는 고효율의 당 리파이너리이다.
<110> INDUSTRY-ACADEMIC COOPERATION FOUNDATION GYEONGSANG NATIONAL UNIVERSITY
<120> COMPOSITION AND METHOD FOR PREPARING FRUCTOSE
<130> 01003
<160> 23
<170> KoPatentIn 3.0
<210> 1
<211> 504
<212> PRT
<213> Bifidobacterium adolescentis
<400> 1
Met Lys Asn Lys Val Gln Leu Ile Thr Tyr Ala Asp Arg Leu Gly Asp
1 5 10 15
Gly Thr Ile Lys Ser Met Thr Asp Ile Leu Arg Thr Arg Phe Asp Gly
20 25 30
Val Tyr Asp Gly Val His Ile Leu Pro Phe Phe Thr Pro Phe Asp Gly
35 40 45
Ala Asp Ala Gly Phe Asp Pro Ile Asp His Thr Lys Val Asp Glu Arg
50 55 60
Leu Gly Ser Trp Asp Asp Val Ala Glu Leu Ser Lys Thr His Asn Ile
65 70 75 80
Met Val Asp Ala Ile Val Asn His Met Ser Trp Glu Ser Lys Gln Phe
85 90 95
Gln Asp Val Leu Ala Lys Gly Glu Glu Ser Glu Tyr Tyr Pro Met Phe
100 105 110
Leu Thr Met Ser Ser Val Phe Pro Asn Gly Ala Thr Glu Glu Asp Leu
115 120 125
Ala Gly Ile Tyr Arg Pro Arg Pro Gly Leu Pro Phe Thr His Tyr Lys
130 135 140
Phe Ala Gly Lys Thr Arg Leu Val Trp Val Ser Phe Thr Pro Gln Gln
145 150 155 160
Val Asp Ile Asp Thr Asp Ser Asp Lys Gly Trp Glu Tyr Leu Met Ser
165 170 175
Ile Phe Asp Gln Met Ala Ala Ser His Val Ser Tyr Ile Arg Leu Asp
180 185 190
Ala Val Gly Tyr Gly Ala Lys Glu Ala Gly Thr Ser Cys Phe Met Thr
195 200 205
Pro Lys Thr Phe Lys Leu Ile Ser Arg Leu Arg Glu Glu Gly Val Lys
210 215 220
Arg Gly Leu Glu Ile Leu Ile Glu Val His Ser Tyr Tyr Lys Lys Gln
225 230 235 240
Val Glu Ile Ala Ser Lys Val Asp Arg Val Tyr Asp Phe Ala Leu Pro
245 250 255
Pro Leu Leu Leu His Ala Leu Ser Thr Gly His Val Glu Pro Val Ala
260 265 270
His Trp Thr Asp Ile Arg Pro Asn Asn Ala Val Thr Val Leu Asp Thr
275 280 285
His Asp Gly Ile Gly Val Ile Asp Ile Gly Ser Asp Gln Leu Asp Arg
290 295 300
Ser Leu Lys Gly Leu Val Pro Asp Glu Asp Val Asp Asn Leu Val Asn
305 310 315 320
Thr Ile His Ala Asn Thr His Gly Glu Ser Gln Ala Ala Thr Gly Ala
325 330 335
Ala Ala Ser Asn Leu Asp Leu Tyr Gln Val Asn Ser Thr Tyr Tyr Ser
340 345 350
Ala Leu Gly Cys Asn Asp Gln His Tyr Ile Ala Ala Arg Ala Val Gln
355 360 365
Phe Phe Leu Pro Gly Val Pro Gln Val Tyr Tyr Val Gly Ala Leu Ala
370 375 380
Gly Lys Asn Asp Met Glu Leu Leu Arg Lys Thr Asn Asn Gly Arg Asp
385 390 395 400
Ile Asn Arg His Tyr Tyr Ser Thr Ala Glu Ile Asp Glu Asn Leu Lys
405 410 415
Arg Pro Val Val Lys Ala Leu Asn Ala Leu Ala Lys Phe Arg Asn Glu
420 425 430
Leu Asp Ala Phe Asp Gly Thr Phe Ser Tyr Thr Thr Asp Asp Asp Thr
435 440 445
Ser Ile Ser Phe Thr Trp Arg Gly Glu Thr Ser Gln Ala Thr Leu Thr
450 455 460
Phe Glu Pro Lys Arg Gly Leu Gly Val Asp Asn Thr Thr Pro Val Ala
465 470 475 480
Met Leu Glu Trp Glu Asp Ser Ala Gly Asp His Arg Ser Asp Asp Leu
485 490 495
Ile Ala Asn Pro Pro Val Val Ala
500
<210> 2
<211> 505
<212> PRT
<213> Bifidobacterium pseudolongum
<400> 2
Met Lys Asn Lys Val Gln Leu Ile Thr Tyr Ala Asp Arg Val Gly Asp
1 5 10 15
Gly Asn Leu Ala Ser Leu Thr Asp Ile Leu Arg Thr Arg Phe Ala Gly
20 25 30
Val Tyr Glu Gly Val His Ile Leu Pro Phe Phe Thr Pro Phe Asp Gly
35 40 45
Ala Asp Ala Gly Phe Asp Pro Ile Asp His Thr Lys Val Asp Pro Arg
50 55 60
Leu Gly Asp Trp Asp Asp Ile Ala Glu Leu Ser Lys Thr His Asp Ile
65 70 75 80
Met Val Asp Ala Ile Val Asn His Met Ser Trp Gln Ser Arg Gln Phe
85 90 95
Gln Asp Val Leu Lys His Gly Glu Glu Ser Glu Tyr Tyr Pro Met Phe
100 105 110
Leu Thr Met Ser Ser Val Phe Pro Asp Gly Ala Thr Glu Glu Glu Leu
115 120 125
Ala Gly Ile Tyr Arg Pro Arg Pro Gly Leu Pro Phe Thr His Tyr Thr
130 135 140
Phe Ala Gly Lys Thr Arg Leu Val Trp Val Thr Phe Thr Pro Gln Gln
145 150 155 160
Val Asp Ile Asp Thr Asp Ser Ala Glu Gly Trp Ala Tyr Leu Met Ser
165 170 175
Ile Phe Asp Arg Met Gly Thr Ser His Val Lys Tyr Ile Arg Leu Asp
180 185 190
Ala Val Gly Tyr Gly Ala Lys Glu Ala Gly Thr Ser Cys Phe Met Thr
195 200 205
Pro Lys Thr Phe Ala Leu Ile Ser Arg Leu Arg Glu Glu Gly Ala Lys
210 215 220
Arg Gly Leu Glu Ile Leu Ile Glu Val His Ser Tyr Tyr Lys Lys Gln
225 230 235 240
Val Glu Ile Ala Ala Lys Val Asp Arg Val Tyr Asp Phe Ala Leu Pro
245 250 255
Pro Leu Leu Leu His Ser Leu Phe Thr Gly Arg Val Asp Ala Leu Ala
260 265 270
His Trp Thr Glu Ile Arg Pro Asn Asn Ala Val Thr Val Leu Asp Thr
275 280 285
His Asp Gly Ile Gly Val Ile Asp Ile Gly Ser Asp Gln Leu Asp Arg
290 295 300
Ser Leu Lys Gly Leu Val Pro Asp Glu Asp Val Asp Ala Met Val Glu
305 310 315 320
Thr Ile Ala Lys Asn Thr His Gly Glu Ser Lys Ala Ala Thr Gly Ala
325 330 335
Ala Ala Ser Asn Leu Asp Leu Tyr Gln Val Asn Ser Thr Tyr Tyr Ser
340 345 350
Ala Leu Gly Gly Asn Asp Gln His Tyr Ile Ala Ala Arg Ala Val Gln
355 360 365
Phe Phe Leu Pro Gly Val Pro Gln Val Tyr Tyr Val Gly Ala Leu Ala
370 375 380
Gly Ser Asn Asp Met Glu Leu Leu Lys Arg Thr Asn Val Gly Arg Asp
385 390 395 400
Ile Asn Arg His Tyr Tyr Thr Thr Ala Glu Ile Asp Ala Asn Leu Glu
405 410 415
Arg Pro Val Val Arg Ala Leu Asn Ala Leu Ala Lys Phe Arg Asn Glu
420 425 430
Leu Pro Ala Phe Asp Gly Gly Phe Asn Tyr Ala Val Asp Gly Glu Thr
435 440 445
Met Ser Phe Thr Trp Asn Asp Gly Ala Thr Ser Ala Thr Leu Arg Phe
450 455 460
Thr Pro Ser Arg Gly Met Gly Ala Asp Asn Ala Gln Pro Val Ala Val
465 470 475 480
Leu Thr Trp Ala Asp Ala Ala Gly Glu His Thr Ser Asp Asp Leu Ile
485 490 495
Ala Asn Pro Pro Val Val His Met Asp
500 505
<210> 3
<211> 500
<212> PRT
<213> Unknown
<220>
<223> Alloscardovia criceti
<400> 3
Met Lys Asn Lys Val Gln Leu Ile Thr Tyr Ala Asp Arg Leu Gly Asp
1 5 10 15
Gly Thr Leu Gln Ser Met Thr Glu Thr Ile Arg Lys His Phe Asp Gly
20 25 30
Val Tyr Glu Gly Val His Ile Leu Pro Phe Phe Thr Pro Phe Asp Gly
35 40 45
Ala Asp Ala Gly Phe Asp Pro Val Asp His Thr Gln Val Asp Pro Arg
50 55 60
Leu Gly Ser Trp Asp Asp Val Ala Glu Leu Ser Lys Thr His Asp Ile
65 70 75 80
Met Val Asp Thr Ile Val Asn His Met Ser Trp Glu Ser Lys Gln Phe
85 90 95
Gln Asp Val Met Ala Lys Gly Glu Glu Ser Glu Tyr Tyr Pro Met Phe
100 105 110
Leu Thr Met Ser Ser Ile Phe Pro Asp Gly Val Thr Glu Glu Asp Leu
115 120 125
Thr Ala Ile Tyr Arg Pro Arg Pro Gly Leu Pro Phe Thr His Tyr Thr
130 135 140
Trp Gly Gly Lys Thr Arg Leu Val Trp Thr Thr Phe Thr Pro Gln Gln
145 150 155 160
Val Asp Ile Asp Thr Asp Ser Glu Met Gly Trp Asn Tyr Leu Leu Thr
165 170 175
Ile Leu Asp Gln Leu Ser Gln Ser His Val Ser Gln Ile Arg Leu Asp
180 185 190
Ala Val Gly Tyr Gly Ala Lys Glu Lys Asn Ser Ser Cys Phe Met Thr
195 200 205
Pro Lys Thr Phe Lys Leu Ile Glu Arg Ile Lys Ala Glu Gly Glu Lys
210 215 220
Arg Gly Leu Glu Thr Leu Ile Glu Val His Ser Tyr Tyr Lys Lys Gln
225 230 235 240
Ile Glu Ile Ala Ser Lys Val Asp Arg Val Tyr Asp Phe Ala Ile Pro
245 250 255
Gly Leu Leu Leu His Ala Leu Glu Phe Gly Lys Thr Asp Ser Leu Ala
260 265 270
Lys Trp Ile Glu Val Arg Pro His Asn Ala Val Asn Val Leu Asp Thr
275 280 285
His Asp Gly Ile Gly Val Ile Asp Ile Gly Ser Asp Gln Met Asp Arg
290 295 300
Ser Leu Leu Gly Leu Val Pro Asp Glu Glu Val Asp Ala Leu Val Glu
305 310 315 320
Ser Ile His Arg Asn Ser Asn Gly Glu Ser Gln Glu Ala Thr Gly Ala
325 330 335
Ala Ala Ser Asn Leu Asp Leu Tyr Gln Val Asn Cys Thr Tyr Tyr Ser
340 345 350
Ala Leu Gly Ser Asp Asp Gln Lys Tyr Ile Ala Ala Arg Ala Val Gln
355 360 365
Phe Phe Met Pro Gly Val Pro Gln Val Tyr Tyr Val Gly Ala Leu Ala
370 375 380
Gly Lys Asn Asp Met Glu Leu Leu Lys Asn Thr Asn Val Gly Arg Asp
385 390 395 400
Ile Asn Arg His Tyr Tyr Ser Ala Ala Glu Val Ala Gln Glu Val Glu
405 410 415
Arg Pro Val Val Lys Ala Leu Asn Ala Leu Gly Arg Phe Arg Asn Thr
420 425 430
Leu Ser Ala Phe Asp Gly Glu Phe Ser Tyr Thr Glu Ala Asp Gly Val
435 440 445
Leu Thr Met Thr Trp Ala Asp Asp Ala Thr Ser Ala Lys Leu Thr Phe
450 455 460
Ala Pro Gln Ala Gly Ala His Asp Val Ser Val Ala Arg Leu Glu Trp
465 470 475 480
Lys Asp Ser Ala Gly Glu His Ala Thr Asp Asp Leu Ile Ala Asn Pro
485 490 495
Pro Val Val Ala
500
<210> 4
<211> 504
<212> PRT
<213> Unknown
<220>
<223> Thermanaerothrix daxensis
<400> 4
Met Lys Asn Gln Val Gln Leu Ile Thr Tyr Val Asp Arg Leu Gly Ser
1 5 10 15
Gly Asn Ile Lys Thr Leu His Gln Leu Leu Arg Gly Pro Leu Ala Gly
20 25 30
Leu Phe Gly Gly Val His Leu Leu Pro Phe Tyr Tyr Pro Ile Lys Gly
35 40 45
Ala Asp Ala Gly Phe Asp Pro Ile Asp His Thr Arg Val Asp Pro Cys
50 55 60
Leu Gly Ser Trp Glu Asp Ile Arg Ala Leu Gly Gln Asp Val Asp Leu
65 70 75 80
Met Ala Asp Leu Ile Val Asn His Ile Ser Ser Ser Ser Pro Gln Phe
85 90 95
Leu Asp Tyr Leu Glu Lys Gly Asp Asp Ser Ile Tyr Lys Asp Leu Phe
100 105 110
Leu Thr Met Ser Ser Val Phe Pro Asn Gly Ala Thr Glu Ala Asp Leu
115 120 125
Leu Thr Ile Tyr Arg Pro Arg Pro Gly Leu Pro Phe Ser Tyr Ile Thr
130 135 140
Leu Lys Asn Gly Gln Lys Arg Leu Leu Trp Thr Thr Phe Ser Arg Gln
145 150 155 160
Gln Ile Asp Ile Asn Val Leu His Pro Met Gly Arg Glu Tyr Leu His
165 170 175
Ser Val Leu Arg Thr Leu His Glu Asn Gly Ile Arg Met Val Arg Leu
180 185 190
Asp Ala Val Gly Tyr Ala Val Lys Lys Ala Gly Thr Thr Cys Phe Met
195 200 205
Ile Pro Glu Thr Phe Asp Phe Ile Glu Asn Leu Thr His Gln Ala Gln
210 215 220
Glu Leu Gly Met Glu Val Leu Val Glu Ile His Ser His Tyr Arg Lys
225 230 235 240
Gln Ile Glu Ile Ala Arg Gln Val Asp Arg Val Tyr Asp Phe Ala Leu
245 250 255
Pro Pro Leu Val Leu His Ala Ile Phe Asn Arg Thr Ala Tyr Tyr Leu
260 265 270
Lys Gln Trp Leu Ser Ile Ser Pro Arg Asn Ala Ile Thr Val Leu Asp
275 280 285
Thr His Asp Gly Ile Gly Val Ile Asp Ile Gly Ala Asp Ser Ser Asp
290 295 300
Pro Gln Asn Tyr Pro Gly Leu Ile Pro Pro Glu Glu Leu Glu Ala Leu
305 310 315 320
Val Glu Gln Ile His Leu Asn Ser Asn Gly Gln Ser Arg Leu Ala Ser
325 330 335
Gly Ala Ala Ala Ser Asn Leu Asp Leu Tyr Gln Val Asn Cys Thr Phe
340 345 350
Tyr Asp Ala Leu Gly Arg Asn Asp Arg Asp Tyr Leu Leu Ala Arg Ala
355 360 365
Ile Gln Phe Phe Ser Pro Gly Ile Pro Gln Val Tyr Tyr Val Gly Leu
370 375 380
Leu Ala Gly Glu Asn Asp Met Asp Leu Leu Ala Arg Thr Gly Val Gly
385 390 395 400
Arg Asp Ile Asn Arg His Tyr Tyr Thr Leu Glu Glu Ile Ala Gln Ala
405 410 415
Ile Gln Arg Pro Val Val Gln Ser Leu Phe Arg Leu Ile Arg Phe Arg
420 425 430
Asn Gln His Pro Ala Phe Asn Gly Ala Phe Ser Met Pro Glu Ser Pro
435 440 445
Asp Ser Arg Leu Ile Leu Arg Trp Asp Asn Gly Ala Ala Trp Ala Val
450 455 460
Leu Glu Val Asp Phe Ala Ala Gly Thr Phe Ser Ile Ser Gly Ser Pro
465 470 475 480
Leu Glu Gly Ala Glu Pro Ile Glu Ala Leu Pro Gly Ala His Pro Asp
485 490 495
Asn Arg Tyr Gly Gly Ile Ala Thr
500
<210> 5
<211> 1518
<212> DNA
<213> Bifidobacterium pseudolongum
<400> 5
gtgaagaaca aagtgcagct catcacctat gcggaccgag tgggcgatgg caatctcgca 60
tccctgaccg acatcctgcg cacccgtttc gccggcgtgt atgaaggcgt gcatatcctg 120
ccgttcttca cgccgttcga cggcgccgac gctggcttcg accccatcga ccacacgaaa 180
gtcgacccgc gcctcggtga ttgggatgac atcgccgagc tctccaagac acacgacatc 240
atggtcgacg cgatcgtcaa ccacatgagc tggcagtcgc gccagttcca ggatgtgctc 300
aagcacggcg aagagtccga gtattacccg atgttcctga cgatgagctc ggtcttcccg 360
gacggtgcga ccgaagagga gctcgccggg atctaccgcc cgcgcccggg cctgccgttc 420
acccactaca ccttcgccgg caagacgcgc ctggtgtggg tcacgttcac gccgcagcag 480
gtggacatcg acaccgactc cgccgaaggc tgggcgtacc tgatgtcgat cttcgaccgg 540
atgggcacat cgcacgtcaa gtacattcgc ctcgatgccg tcggttatgg cgcaaaagag 600
gccggcacga gctgcttcat gacacccaag accttcgctc tgatctcccg tttgcgcgag 660
gagggcgcca agcgcggact cgagatcctc atcgaggtgc actcgtacta caagaagcag 720
gtggagatcg ccgcgaaggt ggaccgcgtc tatgacttcg cgctgccccc gctgctgctg 780
cattcgctgt tcaccggccg tgtggacgcg ctcgcgcact ggaccgagat ccgcccgaac 840
aacgccgtca ccgtgctgga cacgcacgat ggcatcggcg tcatcgacat cggctccgac 900
cagctcgacc gctcgctcaa gggcctcgtt cccgacgagg acgtcgacgc catggtcgag 960
acgatcgcga agaacacgca cggcgagtcg aaggctgcga ccggcgccgc cgcgtcgaac 1020
ctcgacctgt accaggtgaa ctccacgtat tattccgcgc tcggcggcaa cgaccagcac 1080
tacatcgctg cgcgcgccgt gcagttcttc ctgccgggtg tgccgcaggt gtactacgtc 1140
ggcgcgctcg ccggcagcaa cgacatggag ttgctcaagc gcaccaatgt cggccgcgac 1200
atcaaccgcc actactacac gaccgcggag atcgacgcga acctcgagcg gcccgtcgta 1260
cgcgcgctca acgcgctcgc gaagttccgc aacgagctgc ccgcgttcga tggcggcttc 1320
aactacgccg tcgacggcga gacgatgagt ttcacgtgga acgatggtgc gacttccgcc 1380
accctgcgct tcacaccttc gcggggcatg ggcgcggaca acgcccaacc cgtggccgtg 1440
ctcacgtggg cagacgccgc cggcgagcac acgagcgacg acctgattgc gaatccgcct 1500
gtggtgcaca tggactga 1518
<210> 6
<211> 58
<212> DNA
<213> Artificial Sequence
<220>
<223> Foward primer
<400> 6
gcggtaccta gaactaaact taaggagact tattatgaag aacaaagtgc agctcatc 58
<210> 7
<211> 28
<212> DNA
<213> Artificial Sequence
<220>
<223> reverse primer
<400> 7
gtctagatta gtccatgtgc accacagg 28
<210> 8
<211> 1503
<212> DNA
<213> Unknown
<220>
<223> Alloscardovia criceti
<400> 8
atgaagaaca aagttcaatt aattacctat gcagatcgcc ttggtgatgg gacattgcag 60
tctatgaccg agaccatccg caagcatttt gatggcgtgt atgagggcgt gcatattctc 120
ccattcttca caccgttcga cggagctgat gcaggcttcg acccagtgga tcacacgcaa 180
gtggatccac gtttgggctc ttgggatgac gtggcagagc tttccaagac gcacgacatt 240
atggtcgata ccattgtgaa ccacatgtcg tgggaatcca agcagttcca ggacgtgatg 300
gctaagggtg aggaatctga gtattatcca atgttcctga ccatgtcttc gattttccca 360
gatggcgtca ccgaagagga tttgaccgcc atttatcgtc cacgtccagg tctgccattt 420
acgcattaca cctggggtgg caagacgcgt ctggtctgga caacctttac gcctcagcag 480
gtggatattg ataccgactc agaaatgggt tggaattatc tgctcaccat tttggatcag 540
ctgtctcagt cgcatgtatc ccagatccgt ttggatgcgg tgggctacgg tgcgaaggaa 600
aagaattcgt cctgcttcat gacgccgaag accttcaagc tcatcgagcg cattaaggct 660
gagggcgaga agcgtggctt ggaaaccttg attgaggtgc attcctacta caagaagcag 720
atcgaaattg cttccaaggt ggatcgcgtg tatgacttcg ccatcccggg tctgcttttg 780
catgctttgg aattcggcaa gaccgattcg ttggccaagt ggattgaagt acgtccgcac 840
aatgcggtca acgtactgga tacgcacgat ggcattggcg ttatcgacat cggctctgac 900
cagatggatc gctccttgct gggtctcgta ccagatgagg aagtcgatgc tctggtggag 960
tccattcatc gcaattccaa cggcgaatcc caggaagcaa ccggtgcggc cgcatctaac 1020
cttgatttgt atcaggtcaa ctgcacgtac tactccgctt tgggtagcga tgaccagaag 1080
tacatcgctg cgcgtgccgt gcagttcttc atgccaggcg tgccacaggt atattatgtt 1140
ggcgctttgg cgggtaagaa tgatatggag ctgctcaaga acaccaatgt gggccgcgat 1200
attaatcgtc actactactc cgcagccgaa gtcgctcagg aagtggagcg cccagtggtg 1260
aaggctctca atgcattggg tcgtttccgc aatactctgt ccgccttcga tggtgaattt 1320
agctacaccg aagcagacgg cgtgcttacc atgacttggg cggatgacgc taccagcgcc 1380
aagctcacct tcgcccctca ggccggtgct cacgatgtat ccgtagcccg cttggagtgg 1440
aaggatagtg ctggcgagca tgctaccgat gatctcattg caaacccacc agtggtggca 1500
tag 1503
<210> 9
<211> 55
<212> DNA
<213> Artificial Sequence
<220>
<223> foward primer
<400> 9
gcggtacccg aagtaaggag gtttagatat gaagaacaaa gttcaattaa ttacc 55
<210> 10
<211> 25
<212> DNA
<213> Artificial Sequence
<220>
<223> reverse primer
<400> 10
gtctagatta tgccaccact ggtgg 25
<210> 11
<211> 1515
<212> DNA
<213> Unknown
<220>
<223> Thermanaerothrix daxensis
<400> 11
atgaaaaacc aagttcaact catcacctac gtagaccgcc tgggaagcgg taacatcaaa 60
acactccacc aattgctgcg tggccccctg gctggcttat tcggcggtgt ccaccttctc 120
cccttctatt accccattaa gggagccgat gccgggtttg atccgattga tcacacccgg 180
gttgacccct gtctgggcag ttgggaggat atcagggcat tggggcagga tgttgactta 240
atggcggact taatcgttaa ccatatttca tcgtcctcgc cccagttcct ggattatttg 300
gagaaggggg acgactcgat ctacaaagat ttgtttctta cgatgagcag tgttttcccg 360
aacggtgcca ccgaagccga cttattgacc atttatcgcc ccagacccgg tttgcctttt 420
tcttatataa ccctgaagaa cggccaaaaa cgtttattgt ggaccacctt ctccaggcag 480
cagattgaca tcaatgtatt gcaccctatg gggagagagt acctgcactc ggtattgcgc 540
actctgcatg aaaacggcat tcgcatggtg cgtctggatg ctgttgggta tgccgtcaaa 600
aaggcgggaa ccacttgttt tatgatcccc gagacgtttg attttattga aaacctgacc 660
catcaagccc aggaattggg gatggaggtc ttggtcgaaa tccactcgca ctatcgcaag 720
caaattgaga ttgcccgtca ggtggatcgt gtctacgatt ttgctttgcc ccccctggtt 780
ctgcacgcca tattcaatcg cacggcatac tacctaaagc aatggctgag tatcagcccg 840
cgcaatgcga ttaccgttct ggatacgcat gatggcattg gggtgattga catcggcgcc 900
gacagcagtg atccacaaaa ctaccccggt ctcattcctc cggaagaatt agaggcttta 960
gtggagcaaa ttcatcttaa cagcaacggg cagagccgtc tggccagcgg tgccgccgcc 1020
tccaacttgg atttatatca ggtgaattgc actttttatg atgcgctcgg gcgcaacgac 1080
cgtgattatt tgttggcacg cgccattcag ttcttctcgc cgggcatccc tcaggtttac 1140
tacgtgggtt tgctggcggg cgaaaatgac atggatctgc tggcccgcac gggtgtcggg 1200
cgtgatatca accggcatta ctacaccctg gaggagattg cccaggccat ccagcgcccc 1260
gtggtgcaat cgctgttccg gctgattcgc tttcgcaacc agcaccccgc ttttaacggg 1320
gcgtttagca tgcccgaatc cccggattcc cggctcatct tgcgttggga taatggggca 1380
gcctgggcgg tattagaggt ggattttgct gccgggacct tttccatttc cggttcgccg 1440
ttagaggggg cggaacccat agaggcgtta ccaggtgccc acccagacaa ccgctacggg 1500
ggtatcgcca cttaa 1515
<210> 12
<211> 73
<212> DNA
<213> Artificial Sequence
<220>
<223> foward primer
<400> 12
gcggtacccg gcgctatcgg ctttcctttc acaggaggac atttattatg aaaaaccaag 60
ttcaactcat cac 73
<210> 13
<211> 23
<212> DNA
<213> Artificial Sequence
<220>
<223> reverse primer
<400> 13
gtctagatta agtggcgata ccc 23
<210> 14
<211> 1503
<212> DNA
<213> Artificial Sequence
<220>
<223> Alloscardovia criceti BamHI and NotI position substitution
<400> 14
atgaagaaca aagttcaatt aattacctat gcagatcgcc ttggtgatgg gacattgcag 60
tctatgaccg agaccatccg caagcatttt gatggcgtgt atgagggcgt gcatattctc 120
ccattcttca caccgttcga cggagctgat gcaggcttcg acccagtgga tcacacgcaa 180
gtcgatccac gtttgggctc ttgggatgac gtggcagagc tttccaagac gcacgacatt 240
atggtcgata ccattgtgaa ccacatgtcg tgggaatcca agcagttcca ggacgtgatg 300
gctaagggtg aggaatctga gtattatcca atgttcctga ccatgtcttc gattttccca 360
gatggcgtca ccgaagagga tttgaccgcc atttatcgtc cacgtccagg tctgccattt 420
acgcattaca cctggggtgg caagacgcgt ctggtctgga caacctttac gcctcagcag 480
gtggatattg ataccgactc agaaatgggt tggaattatc tgctcaccat tttggatcag 540
ctgtctcagt cgcatgtatc ccagatccgt ttggatgcgg tgggctacgg tgcgaaggaa 600
aagaattcgt cctgcttcat gacgccgaag accttcaagc tcatcgagcg cattaaggct 660
gagggcgaga agcgtggctt ggaaaccttg attgaggtgc attcctacta caagaagcag 720
atcgaaattg cttccaaggt ggatcgcgtg tatgacttcg ccatcccggg tctgcttttg 780
catgctttgg aattcggcaa gaccgattcg ttggccaagt ggattgaagt acgtccgcac 840
aatgcggtca acgtactgga tacgcacgat ggcattggcg ttatcgacat cggctctgac 900
cagatggatc gctccttgct gggtctcgta ccagatgagg aagtcgatgc tctggtggag 960
tccattcatc gcaattccaa cggcgaatcc caggaagcaa ccggtgctgc cgcatctaac 1020
cttgatttgt atcaggtcaa ctgcacgtac tactccgctt tgggtagcga tgaccagaag 1080
tacatcgctg cgcgtgccgt gcagttcttc atgccaggcg tgccacaggt atattatgtt 1140
ggcgctttgg cgggtaagaa tgatatggag ctgctcaaga acaccaatgt gggccgcgat 1200
attaatcgtc actactactc cgcagccgaa gtcgctcagg aagtggagcg cccagtggtg 1260
aaggctctca atgcattggg tcgtttccgc aatactctgt ccgccttcga tggtgaattt 1320
agctacaccg aagcagacgg cgtgcttacc atgacttggg cggatgacgc taccagcgcc 1380
aagctcacct tcgcccctca ggccggtgct cacgatgtat ccgtagcccg cttggagtgg 1440
aaggatagtg ctggcgagca tgctaccgat gatctcattg caaacccacc agtggtggca 1500
tag 1503
<210> 15
<211> 36
<212> DNA
<213> Artificial Sequence
<220>
<223> foward primer
<400> 15
gctggatcca tgaagaacaa agttcaatta attacc 36
<210> 16
<211> 28
<212> DNA
<213> Artificial Sequence
<220>
<223> reverse primer
<400> 16
ctgcggccgc ttatgccacc actggtgg 28
<210> 17
<211> 33
<212> DNA
<213> Artificial Sequence
<220>
<223> foward primer
<400> 17
gctggatcca tgaagaacaa agtgcagctc atc 33
<210> 18
<211> 31
<212> DNA
<213> Artificial Sequence
<220>
<223> reverse primer
<400> 18
ctgcggccgc ttagtccatg tgcaccacag g 31
<210> 19
<211> 35
<212> DNA
<213> Artificial Sequence
<220>
<223> foward primer
<400> 19
gctggatcca tgaaaaacca agttcaactc atcac 35
<210> 20
<211> 26
<212> DNA
<213> Artificial Sequence
<220>
<223> reverse primer
<400> 20
ctgcggccgc ttaagtggcg ataccc 26
<210> 21
<211> 289
<212> PRT
<213> Unknown
<220>
<223> Clostridium hylemonae
<400> 21
Met Lys His Gly Ile Tyr Tyr Ala Tyr Trp Glu Gln Glu Trp Ala Ala
1 5 10 15
Asp Tyr Lys Arg Tyr Val Glu Lys Val Ala Lys Leu Gly Phe Asp Ile
20 25 30
Leu Glu Ile Gly Ala Gly Pro Leu Pro Glu Tyr Ala Glu Gln Asp Val
35 40 45
Lys Glu Leu Lys Lys Cys Ala Gln Asp Asn Gly Ile Thr Leu Thr Ala
50 55 60
Gly Tyr Gly Pro Thr Phe Asn His Asn Ile Gly Ser Ser Asp Ala Gly
65 70 75 80
Val Arg Glu Glu Ala Leu Glu Trp Tyr Lys Arg Leu Phe Glu Val Leu
85 90 95
Ala Glu Leu Asp Ile His Leu Ile Gly Gly Ala Leu Tyr Ser Tyr Trp
100 105 110
Pro Val Asp Phe Ala Asn Ala Asp Lys Thr Glu Asp Trp Lys Trp Ser
115 120 125
Val Glu Gly Met Gln Arg Leu Ala Pro Ala Ala Ala Lys Tyr Asp Ile
130 135 140
Asn Leu Gly Met Glu Val Leu Asn Arg Phe Glu Ser His Ile Leu Asn
145 150 155 160
Thr Ala Glu Glu Gly Val Lys Phe Val Glu Glu Val Gly Met Asp Asn
165 170 175
Val Lys Val Met Leu Asp Thr Phe His Met Asn Ile Glu Glu Gln Ser
180 185 190
Ile Gly Gly Ala Ile Arg Arg Ala Gly Lys Leu Leu Gly His Phe His
195 200 205
Thr Gly Glu Cys Asn Arg Met Val Pro Gly Lys Gly Arg Ile Pro Trp
210 215 220
Arg Glu Ile Gly Asp Ala Leu Arg Asp Ile Gly Tyr Asp Gly Thr Ala
225 230 235 240
Val Met Glu Pro Phe Val Arg Met Gly Gly Gln Val Gly Ala Asp Ile
245 250 255
Lys Val Trp Arg Asp Ile Ser Arg Gly Ala Asp Glu Ala Gln Leu Asp
260 265 270
Asp Asp Ala Arg Arg Ala Leu Glu Phe Gln Arg Tyr Met Leu Glu Trp
275 280 285
Lys
<210> 22
<211> 336
<212> PRT
<213> Lactobacillus reuteri
<400> 22
Met Lys Ala Leu Val Leu Thr Gly Lys Lys Gln Leu Glu Ile Glu Asp
1 5 10 15
Ile Lys Glu Pro Glu Ile Lys Pro Asp Glu Val Leu Ile His Thr Ala
20 25 30
Tyr Ala Gly Ile Cys Gly Thr Asp Lys Ala Leu Tyr Ala Gly Leu Pro
35 40 45
Gly Ser Ala Ser Ala Val Pro Pro Ile Val Leu Gly His Glu Asn Ser
50 55 60
Gly Val Val Thr Lys Val Gly Ser Glu Val Thr Asn Val Lys Pro Gly
65 70 75 80
Asp Arg Val Thr Val Asp Pro Asn Ile Tyr Cys Gly Gln Cys Lys Tyr
85 90 95
Cys Arg Thr Gln Arg Pro Glu Leu Cys Glu His Leu Asp Ala Val Gly
100 105 110
Val Thr Arg Asn Gly Gly Phe Glu Glu Tyr Phe Thr Ala Pro Ala Lys
115 120 125
Val Val Tyr Pro Ile Pro Asp Asp Val Ser Leu Lys Ala Ala Ala Val
130 135 140
Val Glu Pro Ile Ser Cys Ala Met His Gly Val Asp Leu Leu Glu Thr
145 150 155 160
His Pro Tyr Gln Lys Ala Leu Val Leu Gly Asp Gly Phe Glu Gly Gln
165 170 175
Leu Phe Ala Gln Ile Leu Lys Ala Arg Gly Ile His Glu Val Thr Leu
180 185 190
Ala Gly Arg Ser Asp Glu Lys Leu Glu Asn Asn Arg Lys His Phe Gly
195 200 205
Val Lys Thr Ile Asn Thr Thr Lys Glu Glu Ile Pro Ala Asp Ala Tyr
210 215 220
Asp Ile Val Val Glu Ala Val Gly Leu Pro Ala Thr Gln Glu Gln Ala
225 230 235 240
Leu Ala Ala Ala Ala Arg Gly Ala Gln Val Leu Met Phe Gly Val Gly
245 250 255
Asn Pro Asp Asp Lys Phe Ser Val Asn Thr Tyr Asp Val Phe Gln Lys
260 265 270
Gln Leu Thr Ile Gln Gly Ala Phe Ile Asn Pro Tyr Thr Phe Glu Asp
275 280 285
Ser Ile Ala Leu Leu Ser Ser Gly Val Val Asp Pro Leu Pro Leu Phe
290 295 300
Ser His Glu Leu Asp Leu Asp Gly Val Glu Gly Phe Val Ser Gly Lys
305 310 315 320
Leu Gly Lys Val Ser Lys Ala Val Val Lys Val Gly Gly Glu Glu Ala
325 330 335
<210> 23
<211> 401
<212> PRT
<213> Mycobacterium vaccae
<400> 23
Met Ala Lys Val Leu Cys Val Leu Tyr Asp Asp Pro Val Asp Gly Tyr
1 5 10 15
Pro Lys Thr Tyr Ala Arg Asp Asp Leu Pro Lys Ile Asp His Tyr Pro
20 25 30
Gly Gly Gln Ile Leu Pro Thr Pro Lys Ala Ile Asp Phe Thr Pro Gly
35 40 45
Gln Leu Leu Gly Ser Val Ser Gly Glu Leu Gly Leu Arg Glu Tyr Leu
50 55 60
Glu Ser Asn Gly His Thr Leu Val Val Thr Ser Asp Lys Asp Gly Pro
65 70 75 80
Asp Ser Val Phe Glu Arg Glu Leu Val Asp Ala Asp Val Val Ile Ser
85 90 95
Gln Pro Phe Trp Pro Ala Tyr Leu Thr Pro Glu Arg Ile Ala Lys Ala
100 105 110
Lys Asn Leu Lys Leu Ala Leu Thr Ala Gly Ile Gly Ser Asp His Val
115 120 125
Asp Leu Gln Ser Ala Ile Asp Arg Asn Val Thr Val Ala Glu Val Thr
130 135 140
Tyr Cys Asn Ser Ile Ser Val Ala Glu His Val Val Met Met Ile Leu
145 150 155 160
Ser Leu Val Arg Asn Tyr Leu Pro Ser His Glu Trp Ala Arg Lys Gly
165 170 175
Gly Trp Asn Ile Ala Asp Cys Val Ser His Ala Tyr Asp Leu Glu Ala
180 185 190
Met His Val Gly Thr Val Ala Ala Gly Arg Ile Gly Leu Ala Val Leu
195 200 205
Arg Arg Leu Ala Pro Phe Asp Val His Leu His Tyr Thr Asp Arg His
210 215 220
Arg Leu Pro Glu Ser Val Glu Lys Glu Leu Asn Leu Thr Trp His Ala
225 230 235 240
Thr Arg Glu Asp Met Tyr Pro Val Cys Asp Val Val Thr Leu Asn Cys
245 250 255
Pro Leu His Pro Glu Thr Glu His Met Ile Asn Asp Glu Thr Leu Lys
260 265 270
Leu Phe Lys Arg Gly Ala Tyr Ile Val Asn Thr Ala Arg Gly Lys Leu
275 280 285
Cys Asp Arg Asp Ala Val Ala Arg Ala Leu Glu Ser Gly Arg Leu Ala
290 295 300
Gly Tyr Ala Gly Asp Val Trp Phe Pro Gln Pro Ala Pro Lys Asp His
305 310 315 320
Pro Trp Arg Thr Met Pro Tyr Asn Gly Met Thr Pro His Ile Ser Gly
325 330 335
Thr Thr Leu Thr Ala Gln Ala Arg Tyr Ala Ala Gly Thr Arg Glu Ile
340 345 350
Leu Glu Cys Phe Phe Glu Gly Arg Pro Ile Arg Asp Glu Tyr Leu Ile
355 360 365
Val Gln Gly Gly Ala Leu Ala Gly Thr Gly Ala His Ser Tyr Ser Lys
370 375 380
Gly Asn Ala Thr Gly Gly Ser Glu Glu Ala Ala Lys Phe Lys Lys Ala
385 390 395 400
Val
Claims (15)
- 자당 인산화 효소 또는 이를 발현하는 미생물; 또는 상기 미생물의 배양물 또는 분쇄물;을 포함하는 과당 제조용 조성물.
- 청구항 1에 있어서, 상기 자당 인산화 효소는 서열번호 1 내지 4 중 어느 하나의 서열로 이루어지거나, 이와 서열 상동성이 80% 이상인 서열로 이루어진 것인 과당 제조용 조성물.
- 청구항 1에 있어서, 상기 미생물은 내재적 또는 외인적으로 상기 효소를 발현하는 것인 과당 제조용 조성물.
- 청구항 1에 있어서, 상기 미생물은 에셰리키아 속 또는 코리네박테리움 속 미생물인 과당 제조용 조성물.
- 청구항 1에 있어서, 상기 미생물은 휴면 세포를 갖도록 유도된 것인 과당 제조용 조성물.
- 청구항 1의 조성물; 및
과당을 기질로 사용하는 당류 생산 경로의 효소, 이를 발현하는 미생물, 상기 미생물의 배양물 또는 분쇄물을 더 포함하는 당류 제조용 조성물.
- 청구항 6에 있어서, 상기 과당을 기질로 사용하는 당류 생산 경로는 사이코스 생산 경로, 만니톨 생산 경로, 타가토스 생산 경로, 소르비톨 생산 경로인 당류 제조용 조성물.
- 청구항 6에 있어서, 자당 인산화 효소를 발현하는 미생물이 과당을 기질로 사용하는 당류 생산 경로의 효소도 발현하는 것인 당류 제조용 조성물.
- 자당 및 글리세롤을 청구항 1 내지 5 중 어느 한 항의 조성물과 반응시키는 단계를 포함하는 과당의 제조 방법.
- 청구항 9에 있어서, 반응액에서 과당을 분리하는 단계를 더 포함하는 과당의 제조 방법.
- 청구항 9에 있어서, 상기 조성물은 상기 미생물을 포함하는 것이고, 상기 각 반응은 상기 미생물 내에서 수행되는 것인 과당의 제조 방법.
- 청구항 11에 있어서, 상기 자당과 자당 인산화 효소의 반응 전에 상기 미생물을 생육배지에서 배양하여 휴면 세포를 갖도록 유도하는 단계를 더 포함하는 과당의 제조 방법.
- 청구항 9에 있어서, 상기 반응은 버퍼를 포함하지 않는 반응액에서 수행되는 것인 과당의 제조 방법.
- 자당 및 글리세롤을 청구항 6 내지 8 중 어느 한 항의 조성물과 반응시키는 단계를 포함하는 당류의 제조 방법.
- 청구항 14에 있어서, 상기 당류는 사이코스, 만니톨, 타가토스, 소르비톨이고, 상기 조성물은 상기 당류 합성 경로의 효소, 이를 발현하는 미생물, 상기 미생물의 배양물 또는 분쇄물을 포함하는 것인 당류의 제조 방법.
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US18/277,380 US20240124909A1 (en) | 2021-03-30 | 2022-02-28 | Composition and method for production of fructose |
CN202280011682.9A CN116745413A (zh) | 2021-03-30 | 2022-02-28 | 用于制备果糖的组合物及制备方法 |
PCT/KR2022/002861 WO2022211288A1 (ko) | 2021-03-30 | 2022-02-28 | 과당 제조용 조성물 및 제조 방법 |
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WO2022211288A1 (ko) | 2022-10-06 |
CN116745413A (zh) | 2023-09-12 |
US20240124909A1 (en) | 2024-04-18 |
KR20230152646A (ko) | 2023-11-03 |
KR20240007710A (ko) | 2024-01-16 |
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