KR20230012047A - 알룰로스의 효소적 생산 - Google Patents
알룰로스의 효소적 생산 Download PDFInfo
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- KR20230012047A KR20230012047A KR1020227044366A KR20227044366A KR20230012047A KR 20230012047 A KR20230012047 A KR 20230012047A KR 1020227044366 A KR1020227044366 A KR 1020227044366A KR 20227044366 A KR20227044366 A KR 20227044366A KR 20230012047 A KR20230012047 A KR 20230012047A
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- KR
- South Korea
- Prior art keywords
- leu
- ala
- glu
- gly
- allulose
- Prior art date
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Abstract
본 발명은 다른 알룰로스 생산 방법의 효소에 비해, 개선된 발현, 개선된 안정성, 및 낮은 알룰로스에서 과당으로의 전환 활성을 갖는 것으로 특징지어지는 효소를 사용하는 알룰로스의 개선된 효소적 생산 공정에 관한 것이다. 개선된 공정은 알룰로스 6-인산염 에피머화효소를 사용하여 과당-6-인산염을 알룰로스 6-인산염(A6P)으로 전환시키는 단계, 및 알룰로스-6-인산염 인산가수분해효소를 사용하여 A6P를 알룰로스로 전환시키는 단계를 포함한다.
Description
본원에 제출된 서열 목록은 EFS-웹을 통한 ASCII 텍스트 파일(2021-05-18_Sequence_Listing_ST25, 2021년 5월 18일에 생성, 48,103 바이트)이며 본원에 참조로 혼입된다.
관련 출원에 대한 상호 참조
본 출원은 2020년 5월 18일에 출원된, 미국 출원 번호 63/026,294에 대한 우선권을 주장하고, 이의 전체 내용은 본원에 참조로 혼입된다.
본 발명은 D-알룰로스를 생성하기 위한 개선된 효소적 공정에 관한 것이다.
D-사이코스, 또는 간단히, 알룰로스라고도 하는 D-알룰로스는 자당의 단맛의 70%이지만, 이의 칼로리의 10%에 불과한 저칼로리의 천연 감미료이다. 이는 자연적으로 발생하는 단당류 6탄당이며, 밀과 기타 식물에 소량으로 존재한다. 알룰로스는 2012년 미국 식품의약국(FDA)에 의해 식품 첨가물로 승인되어, 일반적으로 안전하다고 인정되는 물질(GRAS)로 지정되었다. 그러나, 알룰로스의 높은 가격은 이의 감미료로서의 사용에 한계가 있다. 그럼에도 불구하고, 알룰로스는 자당의 칼로리의 10%를 함유하고 있을 뿐만 아니라, 1의 낮은 혈당 지수; 대사되지 않고 소장에서 완전히 흡수되어 소변과 대변으로 제거됨; 및 혈당 조절에 도움이 되는 알파-아밀라제, 수크라아제 및 말타아제의 억제를 비롯한 수많은 건강상의 이점을 자랑하는 한편, 이 모든 것이 식품 및 음료에서의 자당과 유사한 기능성을 가진다. 이와 같이, 알룰로스는 식품 및 음료 산업에서 다양한 응용 분야를 가지고 있다.
알룰로스는 주로, 과당의 효소적 이성질화를 수반하는 방법에 의해 생산된다. 예를 들어, PCT 출원 공개 번호 WO 2014/049373을 참조하라. 전반적으로, 이러한 방법은 과당으로부터 알룰로스를 분리하는데 비용이 많이 들고, 이와 연관된 상대적으로 낮은 생성물 수율이 더 높은 공급원료 비용을 초래하기 때문에 상업적으로 실행가능하지 않다.
에피머화효소를 사용하여 과당 6-인산염을 알룰로스 6-인산염으로 촉매화시킨 후, 탈인산화 단계를 사용하여 알룰로스를 생산하는 대안적인 공정은 PCT 출원 공개 번호 WO 2018/112139, WO 2018/004308, 및 WO 2018/129275에 기재되어 있으나, 이들 및 다른 대안적인 알룰로스 생산 방법은, 더 적은 양의 효소를 사용하여 더 높은 수율을 제공하는 알룰로스를 생산하는 공정에 대한 오랜 요구를 만족시키지 못한다. 이러한 개선을 염두에 두고, 하기 개시내용은 현재 사용되는 알룰로스 생산 방법에 비해, 더 큰 발현, 안정성을 갖고, 낮은 바람직하지 않은 알룰로스 전환 활성과 연관된 알룰로스의 생산에 사용하기 위한 효소를 설명한다. 전술한 개선 사항은 알룰로스 생산의 비용을 감소시키는 것에 대한 강한 산업적 및 상업적 관심을 충족시킨다.
본 발명은 당류, 예컨대, 예를 들어, 다당류, 올리고당류, 이당류, 자당, D-글루코오스 및 D-과당을 알룰로스로 효소적으로 전환시키는 개선된 알룰로스 제조 방법을 제공한다. 하나의 양태에서, 당류로부터 알룰로스를 생산하기 위한 본 발명의 개선된 공정은 알룰로스 6-인산염 에피머화효소(A6PE)를 사용하여 과당-6-인산염(F6P)을 알룰로스 6-인산염(A6P)으로 전환시키는 단계를 포함하고, 여기서 A6PE는 서열 번호: 1에 대해 적어도 90% 서열 동일성을 갖는 아미노산 서열을 포함한다. 또 다른 양태에서, 당류로부터 알룰로스를 생산하기 위한 본 발명에 따른 개선된 공정은 알룰로스-6-인산염 인산가수분해효소(A6PP)를 사용하여 A6P를 알룰로스로 전환시키는 단계를 포함하며, A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함한다. 본 발명의 실시양태에서, 개선된 공정은 알룰로스 6-인산염 에피머화효소(A6PE)를 사용하여 과당-6-인산염(F6P)을 알룰로스 6-인산염(A6P)으로 전환시키는 단계(A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함함), 및 알룰로스-6-인산염 인산가수분해효소(A6PP)를 사용하여 A6P를 알룰로스로 전환시키는 단계(A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함함)를 포함한다.
알룰로스를 제조하기 위한 본 발명의 공정은 또한 인산포도당이성질화효소(PGI)에 의해 촉매되는 단계에서, 포도당 6-인산염(G6P)을 F6P로 전환시키는 단계를 수반할 수 있다. 본 발명에 따른 다른 공정은 인산포도당자리옮김효소(Phosphoglucomutase, PGM)에 의해 촉매되는 반응에 의해 포도당 1-인산염(G1P)을 G6P로 전환시키는 단계를 추가로 포함할 수 있는 한편, 또 다른 공정은 적어도 하나의 다른 효소에 의해 촉매되는 반응에 의해 당류를 G1P로 전환시키는 단계를 추가로 포함할 수 있다.
본원에 설명된 임의의 공정에 사용되는 당류는 전분 또는 이의 유도체, 셀룰로스 또는 이의 유도체, 및 자당으로 이루어진 군으로부터 선택될 수 있다. 이와 관련하여, 전분 또는 이의 유도체는, 예를 들어, 아밀로스, 아밀로펙틴, 가용성 전분, 아밀로덱스트린, 말토덱스트린, 엿당, 말토트리오스, 또는 포도당일 수 있다. 본 발명의 일부 개선된 공정에서, 전분은 효소적 가수분해 또는 전분의 산 가수분해에 의해 전분 유도체로 전환된다. 전분 유도체를 수득하기 위한 전분의 효소적 가수분해의 예는, 비제한적으로, 이소아밀라제, 풀루라나제, 알파-아밀라제, 또는 이들 효소 중 둘 이상의 조합에 의해 촉매되는 반응을 포함한다. 본 발명의 일부 ㄱ공정은 4-글루칸 전이효소(4GT)의 첨가를 추가로 수반할 수 있다.
알룰로스를 제조하기 위한 본 발명의 다른 공정은 적어도 하나의 효소에 의해 촉매되는, 과당을 F6P로 전환시키는 단계를 추가로 포함한다. 본 발명의 다른 ㄱ공정은 적어도 하나의 효소에 의해 촉매되는 반응에서, 자당을 과당으로 전환시키는 단계를 추가로 포함한다. 알룰로스 제조 공정에 사용되는 G6P는 또한 적어도 하나의 효소에 의해 촉매되는 반응에서, 포도당을 G6P로 전환시켜 생성될 수 있다. 포도당은, 차례로, 적어도 하나의 효소에 의해 촉매되는 자당을 포도당으로 전환시켜 생성될 수 있다.
본 발명의 공정은 약 37℃ 내지 약 85℃ 범위의 온도, 약 4 내지 약 9 범위의 pH, 및/또는 약 0.5시간 내지 약 48시간 동안, 또는 연속 반응을 비롯한 다양한 반응 조건 하에 수행될 수 있다. 일부 실시양태에서, 알룰로스를 제조하는 공정의 단계는 단일 반응기에서 임의의 하나 이상의 전술한 반응 조건 하에 수행된다. 한편, 다른 실시양태에서, 반응 단계는 직렬로 배열될 수 있는 복수의 생물반응기를 사용하여 전술한 반응 조건 하에 수행된다.
본 발명의 일부 공정에서, 알룰로스를 제조하는 단계는 아데노신 3인산염(ATP) 또는 NAD(H)를 함유하지 않는, 즉 ATP-무함유 또는 NAD(H)-무함유 조건하에, 약 0.1mM 내지 약 150mM의 인산염 농도에서 수행되며, 인산염은 재사용되고/되거나, A6P를 알룰로스로 전환시키는 단계는 에너지적으로 유리한 화학 반응을 수반한다.
도 1은 전분 또는 이의 유도된 생성물을 알룰로스로 전환시키는 효소적 경로를 나타내는 개략도이다. 다음 약어가 사용된다: αGP, 알파-글루칸 인산화효소 또는 전분 인산화효소; PGM, 인산포도당자리옮김효소; PGI, 인산포도당이성질화효소; A6PE, 알룰로스 6-인산염 에피머화효소; A6PP, 알룰로스 6-인산염 인산가수분해효소; IA, 이소아밀라제; PA, 풀루라나제; MP, 엿당 인산화효소; PPGK, 폴리인산염 포도당인산화효소. 본 발명의 공정에서, A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함한다.
도 2는 셀룰로스 또는 이의 유도된 생성물을 알룰로스로 전환시키는 효소적 경로를 나타낸다. CDP, 셀로덱스트린 인산화효소; CBP, 셀로비오스 인산화효소; PPGK, 폴리인산염 포도당인산화효소; PGM, 인산포도당자리옮김효소; PGI, 인산포도당이성질화효소; A6PE, 알룰로스 6-인산염 에피머화효소; A6PP, 알룰로스 6-인산염 인산가수분해효소. 본 발명의 공정에서, A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함한다.
도 3은 과당을 알룰로스로 전환시키는 효소적 경로를 예시하는 개략도이다. PPFK, 폴리인산염 프럭토키나제; A6PE, 알룰로스 6-인산염 에피머화효소; A6PP, 알룰로스 6-인산염 인산가수분해효소. 본 발명의 공정에서, A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함한다.
도 4는 포도당을 알룰로스로 전환시키는 효소적 경로를 나타내는 개략도이다. PPGK, 폴리인산염 포도당인산화효소; PGI, 인산포도당이성질화효소; A6PE, 알룰로스 6-인산염 에피머화효소; A6PP, 알룰로스 6-인산염 인산가수분해효소. 본 발명의 공정에서, A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함한다.
도 5는 자당 또는 그 유도된 생성물을 알룰로스로 전환시키는 효소적 경로를 나타낸다. SP, 자당 인산화효소; PPFK, 폴리인산염 프럭토키나제; PGM, 인산포도당자리옮김효소; PGI, 인산포도당이성질화효소; A6PE, 알룰로스 6-인산염 에피머화효소; A6PP, 알룰로스 6-인산염 인산가수분해효소. 본 발명의 공정에서, A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함한다.
도 6은 HPLC에 의해 측정된 말토덱스트린의 알룰로스로의 전환을 나타낸다. 하기의 효소가 사용되었다: αGP(유니프로트 ID G8NCC0), PGM(유니프로트 ID A0A150LLZ1), PGI(유니프로트 ID Q5SLL6), A6PP(유니프로트 ID A0A0E3NCH4) 및 4GT(유니프로트 ID E8MXP8). A6PE(유니프로트 ID A0A090IXZ8) 및 (유니파크 ID UPI000411882A)를 본 발명의 개선된 공정에서 사용된 A6PE(A0A223HZI7)와 비교하였다.
도 7은 HPLC에 의해 측정된 G1P의 알룰로스로의 전환을 나타낸다. 다음 효소가 사용되었다: PGM(유니프로트 ID A0A150LLZ1), PGI(유니프로트 ID Q5SLL6) 및 A6PE(유니프로트 ID D9TQJ4). A6PP(유니프로트 ID A3DC21)를 본 발명의 개선된 공정에 사용된 A6PP(유니프로트 ID A0A0E3NCH4)와 비교하였다.
도 2는 셀룰로스 또는 이의 유도된 생성물을 알룰로스로 전환시키는 효소적 경로를 나타낸다. CDP, 셀로덱스트린 인산화효소; CBP, 셀로비오스 인산화효소; PPGK, 폴리인산염 포도당인산화효소; PGM, 인산포도당자리옮김효소; PGI, 인산포도당이성질화효소; A6PE, 알룰로스 6-인산염 에피머화효소; A6PP, 알룰로스 6-인산염 인산가수분해효소. 본 발명의 공정에서, A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함한다.
도 3은 과당을 알룰로스로 전환시키는 효소적 경로를 예시하는 개략도이다. PPFK, 폴리인산염 프럭토키나제; A6PE, 알룰로스 6-인산염 에피머화효소; A6PP, 알룰로스 6-인산염 인산가수분해효소. 본 발명의 공정에서, A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함한다.
도 4는 포도당을 알룰로스로 전환시키는 효소적 경로를 나타내는 개략도이다. PPGK, 폴리인산염 포도당인산화효소; PGI, 인산포도당이성질화효소; A6PE, 알룰로스 6-인산염 에피머화효소; A6PP, 알룰로스 6-인산염 인산가수분해효소. 본 발명의 공정에서, A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함한다.
도 5는 자당 또는 그 유도된 생성물을 알룰로스로 전환시키는 효소적 경로를 나타낸다. SP, 자당 인산화효소; PPFK, 폴리인산염 프럭토키나제; PGM, 인산포도당자리옮김효소; PGI, 인산포도당이성질화효소; A6PE, 알룰로스 6-인산염 에피머화효소; A6PP, 알룰로스 6-인산염 인산가수분해효소. 본 발명의 공정에서, A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함한다.
도 6은 HPLC에 의해 측정된 말토덱스트린의 알룰로스로의 전환을 나타낸다. 하기의 효소가 사용되었다: αGP(유니프로트 ID G8NCC0), PGM(유니프로트 ID A0A150LLZ1), PGI(유니프로트 ID Q5SLL6), A6PP(유니프로트 ID A0A0E3NCH4) 및 4GT(유니프로트 ID E8MXP8). A6PE(유니프로트 ID A0A090IXZ8) 및 (유니파크 ID UPI000411882A)를 본 발명의 개선된 공정에서 사용된 A6PE(A0A223HZI7)와 비교하였다.
도 7은 HPLC에 의해 측정된 G1P의 알룰로스로의 전환을 나타낸다. 다음 효소가 사용되었다: PGM(유니프로트 ID A0A150LLZ1), PGI(유니프로트 ID Q5SLL6) 및 A6PE(유니프로트 ID D9TQJ4). A6PP(유니프로트 ID A3DC21)를 본 발명의 개선된 공정에 사용된 A6PP(유니프로트 ID A0A0E3NCH4)와 비교하였다.
본원에 기술된 발명은 당류를 알룰로스로 전환시키는 개선된 효소적 공정에 관한 것이다. 보다 구체적으로, 본 발명은 당류를 알룰로스로 전환시키기 위한 개선된 무세포, 효소적 공정에 관한 것이다. 본 발명의 공정에 의해 알룰로스로 전환될 수 있는 당류의 예는, 비제한적으로, 전분, 셀룰로스, 자당, 포도당, 과당, 및 임의의 전술한 당류로부터 유도된 생성물을 포함한다. 본 발명에 따른 공정에 사용된 효소는 단일 무세포 효소 칵테일로 조합될 수 있다. 실제로, 알룰로스를 생산하기 위한 세포 기반 제조 방법과 비교하여, 이에 따른 공정은 공정에 사용된 기질, 생성물, 또는 둘 모두의 세포 내로 및 밖으로 수송을 늦출 수 있는, 세포막의 부재로 인해, 적어도 부분적으로 더 높은 반응 속도를 제공한다. 본 발명의 공정은 또한 발효 배지 및 세포 기반 공정에 사용된 세포와 연관된 영양이 풍부한 대사산물이 없는 최종 알룰로스 생성물을 생성한다.
알룰로스를 생성하기 위한 본 발명의 일부 공정은 본 발명 이전의 알룰로스 생산 방법에 사용된 A6PE 효소 중 어느 하나에 비해 하나 이상의 개선된 특성을 갖는 알룰로스 6-인산염 에피머화효소(A6PE)에 의해 촉매된 반응에 의해, 과당-6-인산염(F6P)을 알룰로스 6-인산염(A6P)으로 전환시키는 단계를 개선한다. 본 발명의 다른 공정은 본 발명 이전의 알룰로스 생산 방법에 사용된 A6PP 효소 중 어느 하나에 비해 하나 이상의 개선된 특성을 갖는 알룰로스-6-인산염 인산가수분해효소(A6PP)에 의해 촉매된 반응에 의해, A6P를 알룰로스로 전환시키는 단계를 개선한다. 본 발명의 일부 공정에서, 알룰로스의 제조 공정은 각각 (F6P에서 A6P로) 및 (A6P에서 알룰로스로) 전환 단계를 위해, 개선된 A6PE 및 개선된 A6PP가 사용되는 (F6P에서 A6P로) 및 (A6P에서 알룰로스로) 전환 단계를 포함할 수 있다. 알룰로스를 생산하기 위한 본 발명의 다른 공정은 A6P에서 알룰로스로의 전환 단계를 위해 개선되지 않은 A6PP를 사용하는 한편, F6P에서 A6P로의 전환 단계를 위해 개선된 A6PE를 사용할 수 있다. 반대로, F6P에서 A6P로의 전환 단계를 위해 개선되지 않은 A6PE를 사용하고, A6P에서 알룰로스로의 전환 단계를 위해 개선된 A6PP를 사용하는 본 발명의 공정도 있다. 전체가 본원에 참조에 의해 혼입되는 PCT 공개 WO2018/112139를 참조하라: 예를 들어 A6PE 및 A6PP, 예컨대 써모아나에로박테리움 써모사카롤리티쿰(유니프로트 ID D9TQJ4)로부터의 A6PP, 바실러스 써모아밀로보란스(유니프로트 ID A0A090IXZ8)로부터의 A6PE, 및 A6PP로부터의 클로스트리디움 써모셀룸(유니프로트 ID A3DC21)로부터의 A6PP.
알룰로스를 제조하는 공정에서, 활성이 더 높고 더 좋은 특성, 예컨대 안정성이 개선된 효소를 사용하는 것은 효소의 양을 더 적게 사용할 수 있어 전반적인 공정의 비용을 절감할 수 있다. 상기 논의된 바와 같이, 본 발명의 개선된 공정에서 F6P의 A6P로의 전환은 하기 개선된 특성 중 하나 이상을 비롯한 알룰로스 생산 공정의 개선에 기여하는 개선된 특성을 갖는 A6PE에 의해 촉진된다: 써모아나에로박테리움 써모사카롤리티쿰(유니프로트 ID D9TQJ4)으로부터의 호열성 A6PE와 비교하여, 더 높은 발현 수율, 열안정성, 및 과당 복귀라고도 하는 바람직하지 않은 낮은 알룰로스의 과당 에피머화 활성.
본 발명의 일부 공정에서, 개선된 공정에서 A6PE의 발현 수율은 적어도 10%, 적어도 20%, 적어도 30%, 적어도 40%, 적어도 50%, 적어도 60%, 적어도 70%, 적어도 80%, 적어도 90%, 적어도 100%, 적어도 200%, 적어도 300% 또는 적어도 400%인 개선되지 않은 공정, 예컨대, 비제한적으로, 유니프로트 ID D9TQJ4(써모아나에로박테리움 써모사카롤리티쿰)의 아미노산 서열을 갖는 A6PE와 같은 A6PE의 발현 수율보다 더 높은 발현 수율을 갖는다. 예를 들어, 알룰로스를 생산하기 위한 본 발명의 공정에서, F6P를 A6P로 전환시키는 단계는 유니프로트 ID A0A223HZI7(클로스트리디움 써모사카롤리티쿰)의 아미노산 서열을 갖는 A6PE를 사용하며, 이는 유니프로트 ID D9TQJ4의 아미노산 서열을 갖는 A6PE보다 대략 300%, 310%, 320%, 330%, 340%, 350%, 360%, 370%, 380%, 390% 또는 400% 더 높은 발현 수율을 갖는다.
본 발명의 일부 공정에서, 개선된 공정의 A6PE는 개선되지 않은 공정의 A6PE보다 더 안정하다. 보다 구체적으로, 본 발명의 개선된 공정에서 A6PE는 개선되지 않은 공정에서 A6PE보다 더 열안정적일 수 있다. 실제로, 본 발명의 일부 공정에서 A6PE는 50℃ 내지 60℃에서 30분 후, 50% 내지 60% 가용성, 60% 내지 70% 가용성, 70% 내지 80% 가용성, 80% 내지 90% 가용성, 90% 내지 100% 가용성, 또는 100% 가용성으로 유지될 수 있다. 유니프로트 ID A0A223HZI7의 아미노산 서열을 갖는 개선된 공정에서 F6P의 A6P로의 전환이 A6PE를 사용하는 본 발명의 공정에서, A6PE는 약 60℃ 에서 30분 후 약 80% 가용성으로 유지될 수 있고; 따라서, 개선된 공정에서 A6PE는 54℃, 55℃, 56℃, 57℃, 58℃, 59℃, 60℃, 61℃, 62℃, 63℃, 64℃, 65℃ 또는 66℃에서 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 또는 35분 후에, 적어도 75%, 76%, 77%, 78%, 79%, 80%, 81%, 82%, 83%, 84% 또는 85% 가용성일 수 있다.
알룰로스 생성 공정에서 A6PE에 의한 알룰로스의 과당으로의 전환은 바람직하지 않다. 본 발명의 일부 개선된 공정에서, A6PE-의존성 알룰로스에서 과당으로의 전환 활성은 알룰로스를 생성하기 위한 개선되지 않은 공정에서 보다 더 낮다. 본 발명의 개선된 공정에서, 예를 들어, 1% 이하, 0.9% 이하, 0.8% 이하, 0.7% 이하, 0.6% 이하, 0.5% 이하, 0.4% 이하, 0.3% 이하, 0.2% 이하, 0.1% 이하, 또는 0%의 본 발명의 공정에 의해 생성된 알룰로스가 과당으로 전환된다.
본 발명의 개선된 공정에 사용된 A6PE 효소는 F6P/A6P에 특이적이며, A6PE에 의해 촉매된 에피머화는 가역적이다. 본원에서 사용된 용어, "특이적"은, 본 발명의 개선된 공정에서 A6PE의 F6/A6P 에피머화 활성이 반응에 존재하는 다른 인산화된 단당류에 대한 것보다 더 높다는 것을 의미한다. 예를 들어, 본 발명의 개선된 공정에서 A6PE의 F6P/A6P 에피머화 활성은 G6P에 대한 이의 에피머화 활성보다 더 높다.
본 발명의 개선된 공정에서 F6P에서 A6P로의 전환은 2가 금속 A6PE 보조인자, 예컨대 마그네슘, 망간, 코발트, 또는 아연을 이용할 수 있다. 본 발명의 일부 공정에서, 예를 들어, 코발트는 F6P에서 A6P로의 전환 반응 단계에서 A6PE의 보조인자이다.
상기 논의된 바와 같이, 본 발명의 개선된 공정에서 A6PE 효소의 특성의 예는, 비제한적으로, 증가된 발현 수율, 증가된 안정성, 및 알룰로스의 과당으로의 감소된 전환을 포함한다. 본 발명의 일부 개선된 공정에서, A6PE의 아미노산 서열은 호열성이다. 보다 구체적으로, 본 발명의 특정한 개선된 공정에서 A6PE는 클로스트리디움 써모사카롤리티쿰으로부터의 A6PE와 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 99% 또는 100% 서열 동일성을 공유하는 아미노산 서열을 갖는다. 따라서, 본 발명의 일부 개선된 공정에서, A6PE의 아미노산 서열은 유니프로트 ID A0A223HZI7의 서열을 갖는 C. 써모사카롤리티쿰 호열성 에피머화효소의 아미노산 서열과 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 99% 또는 100% 서열 동일성을 공유한다.
본 발명의 일부 개선된 공정에서 A6PE의 또 다른 구조적 특징은 촉매작용을 위한 (α/β)8-배럴 도메인이다. 본 발명의 개선된 공정 중 일부에서, (α/β)8-배럴 도메인은 배럴의 7번째 β 가닥의 끝에 Ser, 8번째 β-가닥의 끝에 Ser, 활성 부위 루프에 Gly를 갖는 인산염 결합 도메인을 함유한다. 본 발명의 다른 개선된 공정에서, A6PE는 배럴의 2번째 및 3번째 β-가닥에 His를 갖는 금속 결합 도메인을 함유한다. 본 발명의 다른 개선된 공정에서, A6PE는 1,1 양성자 전달을 위한 산/염기 촉매로서 작용하는 배럴의 2번째 및 7번째 β-가닥에 Asp를 함유한다. 본 발명의 다른 개선된 공정에서, A6PE는 His가 금속 결합에 사용되고 Asp가 산/염기 촉매작용에 사용되는 배럴의 두 번째 β-가닥에 His 소수성 잔기-Asp 서명을 함유한다. 본 발명의 다른 개선된 공정에서, A6PE는 리불로스-인산염 3 에피머화효소 패밀리(Pfam PF00834)의 구성원이다. 본 발명의 또 다른 개선된 공정에서, A6PE는 상기 설명된 임의의 (α/β)8-배럴 도메인 구조적 특징 중 2개 이상을 함유한다. 따라서, 본 발명의 일부 개선된 공정에서, A6PE는 촉매작용을 위한 (α/β)8-배럴 도메인, 배럴의 7번째 β-가닥 끝에 Ser, 배럴의 8번째 β-가닥 끝에 Ser, 활성 부위 루프에 Gly, 배럴의 2번째 및 3번째 β-가닥에 His, 배럴의 2번째 및 7번째 β-가닥에 Asp, 배럴의 2번째 β-가닥에 His-소수성 잔기-Asp 시그니처를 함유하고, 리불로스-인산염 3 에피머화효소 패밀리(Pfam PF00834)의 구성원이다. (α/β)8-배럴 도메인의 이러한 특징은 당업계에 공지되어 있고, 예를 들어, Chan 등 Structural Basis for Substrate Specificity in Phosphate Binding (beta/alpha)8-Barrels: D-Allulose 6-Phosphate 3-Epimerase from Escherichia coli K-12. Biochemistry 2008; 47(36):9608-9617에서 참조된다.
본 발명의 개선된 공정에서, 알룰로스-6-인산염 인산가수분해효소(A6PP)는 A6P를 알룰로스로 특이적으로 전환시키는 인산가수분해효소이다. 따라서, 본 발명의 개선된 공정에서 A6PP는 A6P에 대해 특이적이다. 본원에 사용된 "특이적"이라는 용어는, A6PP의 A6P 탈인산화 활성이 공정에서 다른 인산화된 단당류에 대한 것보다 더 높다는 것을 의미한다. 예를 들어, 본 발명의 개선된 공정의 A6PP는 G1P, G6P 및 F6P에서보다 A6P에서 더 높은 탈인산화 활성을 갖는다. 본 발명의 개선된 공정에서 A6PP는 또한, 2가 금속 보조인자, 예컨대 아연, 망간, 코발트 또는 마그네슘, 바람직하게는 마그네슘을 이용할 수 있다.
본 발명의 개선된 공정에서 A6P의 알룰로스로의 전환은 본 발명 이전의 알룰로스 제조 공정에 사용된 임의의 A6PP 효소에 비해 증가된 활성을 갖는 A6PP를 사용할 수 있다. 본 발명의 일부 개선된 공정에서, 예를 들어, A6PP는 클로스트리디움 써모셀룸(유니프로트 ID A3DC21)으로부터의 A6PP보다 더 높은 활성을 갖는 A6P를 알룰로스로 전환시킨다. 국제 특허 출원 공개 WO 2018/112139 및 WO 2018/129275를 참조하고, 이의 전체가 본원에 혼입된다. 보다 구체적으로, 본 발명의 개선된 공정에서, A6PP는 A6P에서 알룰로스로의 활성을 갖는 메타노사르시나 써모필라 CHTI-55로부터의 A6PP의 아미노산 서열을 가지며, 이는 유니프로트 ID A3DC21의 아미노산 서열을 갖는 클로스트리디움 써모셀룸으로부터의 A6PP의 활성에 비해, 적어도 10%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 110%, 120%, 130%, 140%, 150%, 160%, 170%, 180%, 190%, 200%, 210%, 220%, 230%, 240%, 250%, 260%, 270%, 280%, 290% 또는 300% 개선된다. 더욱 보다 구체적으로, 본 발명의 일부 개선된 공정에서, A6PP는 A6P에서 알룰로스로의 활성을 갖는 유니프로트 ID A0A0E3NCH4(서열 번호 2)의 아미노산 서열을 가지며, 이는 유니프로트 ID A3DC21의 아미노산 서열을 갖는 클로스트리디움 써모셀룸으로부터의 A6PP의 활성에 비해, 적어도 10%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 110%, 120%, 130%, 140%, 150%, 160%, 170%, 180%, 190%, 200%, 210%, 220%, 230%, 240%, 250%, 260%, 270%, 280%, 290% 또는 300% 개선된다.
본 발명의 일부 개선된 공정에서, A6PP는 메타노사르시나 써모필라 CHTI-55로부터의 A6PP와 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 99% 또는 100% 서열 동일성을 공유하는 아미노산 서열을 갖는다. 따라서, 본 발명의 일부 개선된 공정에서, A6PP의 아미노산 서열은 유니프로트 ID A0A0E3NCH4(서열번호 2) 의 서열을 갖는 메타노사르시나 써모필라 CHTI-55 인산가수분해효소의 아미노산 서열과 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 99% 또는 100% 서열 동일성을 공유한다.
본 발명의 일부 개선된 공정에서 A6PE의 또 다른 구조적 특징은 촉매작용을 위한 로스마노이드(Rossmanoid) 접힘 도메인이다. 본 발명의 이러한 개선된 공정 중 일부에서, A6PP는 하기 특징 중 하나 이상을 함유한다: 기질 특이성을 위한 C1 캡핑 도메인; 마그네슘을 배위하기 위한 로스마노이드 접힘의 첫 번째 β-가닥에서의 DxD 서명(여기서 두 번째 Asp는 일반적인 산/염기 촉매임); 반응 중간체의 안정성을 돕는 로스마노이드 접힘의 두 번째 β-가닥 끝에 Thr 또는 Ser; 반응 중간체의 안정성을 돕는 로스마노이드 접힘의 세번째 β-가닥에 대한 α-나선 C-말단의 N-말단에 Lys; 및 마그네슘과 같은 2가 금속 양이온을 배위하기 위한 로스마노이드 접힘의 4 번째 β-가닥 끝에 E(D/N) 서명이 있다. 예를 들어, Burroughs 등, Evolutionary Genomics of the HAD Superfamily: Understanding the Structural Adaptations and Catalytic Diversity in a Superfamily of Phosphoesterases and Allied Enzymes. J. Mol. Biol. 2006; 361; 1003-1034를 참조하라. 본원에 확립된 바와 같이, 본 발명의 개선된 공정은 A6PE를 사용하여 F6P를 A6P로 전환시키는 단계, 및 A6PP를 사용하여 A6P를 알룰로스로 전환시키는 단계를 포함한다. 본 발명의 개선된 공정은 또한 추가적인 상류 단계를 포함할 수 있다. 예를 들어, 본 발명의 일부 공정은 포도당 6-인산염(G6P)을 F6P로 전환시키기 위해 인산포도당이성질화효소(PGI)를 사용하여 당류로부터 알룰로스를 생성한다. 사용될 수 있는 예시적인 PGI는 국제 특허 출원 공개 WO2017/059278에 개시된 것들을 포함한다: 클로스트리디움 써모셀룸의 PGI(유니프로트 ID A3DBX9) 및 써머스 써모필러스의 PGI(유니프로트 ID Q5SLL6).
본 발명의 일부 개선된 공정은 또한 인산포도당자리옮김효소(PGM)를 사용하여 포도당 1-인산염(G1P)을 G6P로 전환시키는 단계를 포함한다. PGM의 예는 국제 특허 출원 공개 WO2017/059278에 개시된 써모코쿠스 코다카렌시스(유니프로트 ID Q68BJ6)의 PGM; 또는 PCT 출원 공개 2020/092315에 개시된 칼디바실러스 데비리스(유니프로트 A0A150LLZ1)로부터의 PGM이다.
본 발명의 일부 개선된 공정은 또한 적어도 하나의 효소를 사용하여 당류를 G1P로 전환시키는 단계를 포함한다. 예를 들어, 개선된 공정은, 도 1에 설명된 바와 같이 전분 또는 이의 유도체, 도 2에 설명된 바와 같이 셀룰로스 또는 이의 유도체, 도 3에 설명된 바와 같이 과당, 도 4에 설명된 바와 같이 포도당, 도 5에 설명된 바와 같이 자당으로부터 선택된 당류를 전환시킬 수 있다. 본 발명의 이러한 개선된 공정에서 당류를 G1P로 전환시키는 단계에서 사용되는 효소 또는 효소들은, 예를 들어, 알파-글루칸 인산화효소(αGP), 엿당 인산화효소, 자당 인산화효소, 셀로덱스트린 인산화효소, 셀로비오스 인산화효소, 및/또는 셀룰로스 인산화효소, 및 이들의 혼합물일 수 있다. F6P에 도달하기 위한 효소 또는 효소 조합의 선택은 공정에 사용된 당류에 따라 다르다.
셀룰로스는 가장 풍부한 생물 자원이며 식물 세포 벽의 주요 구성 요소이다. 비식품 목질섬유소의 바이오매스에는 셀룰로스, 헤미셀룰로스, 목질소 뿐만 아니라 기타 미량 성분이 포함되어 있다. 아비셀(미정질 셀룰로스), 재생 비정질 셀룰로스, 세균성 셀룰로스, 여과지 등을 포함한 순수 셀룰로스를 일련의 처리를 통해 제조할 수 있다. 부분적으로 가수분해된 셀룰로스 기질은 중합도가 7 초과인 수불용성 셀로덱스트린, 중합도가 3 내지 6인 수용성 셀로덱스트린, 셀로비오스, 포도당 및 과당을 포함한다.
본 발명의 일부 개선된 공정에서, 셀룰로스 및 이의 유도된 생성물은 하기를 비롯한 일련의 효소적 단계에 의해 알룰로스로 전환될 수 있다: 예컨대 각각, 셀로덱스트린 인산화효소(CDP) 및 셀로비오스 인산화효소(CBP)에 의해 촉매되는 셀로덱스트린 및 셀로비오스 및 무 인산염으로부터 G1P를 생성하는 단계; PGM에 의해 촉매되는 G1P를 G6P로 전환시키는 단계; PGI에 의해 촉매되는 G6P를 F6P로 전환시키는 단계; 상기 설명된 바와 같이 F6P를 알룰로스로 전환시키는 단계이며, 인산염 이온은 셀로덱스트린 및 셀로비오스를 G1P로 전환시킴으로써 재활용될 수 있다.
고체 셀룰로스를 수용성 셀로덱스트린 및 셀로비오스로 가수분해하기 위해 여러 효소가 사용될 수 있다. 이러한 효소에는 엔도글루카나제 및 셀로바이오하이드롤라제가 포함되지만, 베타-글루코시다제(셀로비아제)는 포함되지 않는다. 셀룰로스 가수분해 및 G1P 생성 전에, 셀룰로스 및 바이오매스를 전처리하여 반응성을 증가시키고, 셀룰로스 사슬의 중합도를 감소시킬 수 있다. 셀룰로스 및 바이오매스 전처리 방법은 묽은 산 전처리, 셀룰로스 용매-기반 목질섬유소 분류, 암모니아 섬유 팽창, 암모니아 수용액 침지, 이온성 액체 처리, 및 염산, 황산, 인산 및 이들의 조합을 비롯한 농축된 산을 사용한 부분 가수분해가 포함된다.
당류가 셀로비오스를 포함하고, 효소가 셀로비오스 인산화효소를 함유하는 경우, G1P는 셀로비오스 인산화효소에 의해 셀로비오스 및 인산염으로부터 생성된다. 당류가 셀로덱스트린을 함유하고 효소가 셀로덱스트린 인산화효소를 포함하는 경우, 셀로덱스트린 인산화효소에 의해 셀로덱스트린 및 인산염으로부터 G1P가 생성된다. 당류가 셀룰로스를 포함하고, 효소가 셀룰로스 인산화효소를 함유하는 경우, G1P는 셀룰로스 인산화효소에 의해 셀룰로스 및 인산염으로부터 생성된다.
당류가 엿당을 포함하고 효소가 엿당 인산화효소를 포함할 때, G1P는 엿당 인산화효소에 의해 엿당 및 인산염으로부터 생성된다. 당류가 자당을 포함하고, 효소가 자당 인산화효소를 함유하는 경우, G1P는 자당 인산화효소에 의해 자당과 인산염으로부터 생성된다.
당류가 전분 또는 전분 유도체인 경우, 이 유도체는 아밀로오스, 아밀로펙틴, 가용성 전분, 아밀로덱스트린, 말토덱스트린, 엿당, 말토트리오스 및 포도당 및 이들의 혼합물로 이루어진 군으로부터 선택될 수 있다. 본 발명의 특정 공정에서, 당류를 G1P로 전환시키는데 사용되는 효소는 αGP를 함유한다. 이 단계에서, 당류가 전분을 함유하는 경우, G1P는 αGP에 의해 전분 및 인산염으로부터 생성되고; 당류가 가용성 전분, 아밀로덱스트린, 또는 말토덱스트린을 함유하는 경우, G1P는 가용성 전분 및 인산염, 아밀로덱스트린 및 인산염, 또는 말토덱스트린 및 인산염으로부터 αGP에 의해 생성된다. αGP의 예는 국제 특허 출원 공개 WO2017/059278에 개시된 써모토가 마리티마(유니프로트 ID G4FEH8)로부터의 αGP; 또는 국제 특허 출원 공개 2020/092315에 개시된 써머스 속균 CCB_US3_UF1(유니프로트 G8NCC0)으로부터의 αGP이다.
본 발명에 따른 일부 공정은 전분을 전분 유도체로 전환시키는 단계를 추가로 포함할 수 있으며, 여기서 전분 유도체는 전분의 효소적 가수분해 또는 전분의 산 가수분해에 의해 제조된다. 본 발명의 특정 공정에서, 엿당 인산화효소(MP)는 분해 생성물 엿당을 G1P 및 포도당으로 인산분해적으로 절단함으로써 알룰로스 수율을 증가시키기 위해 사용될 수 있다. 달리, 4-글루칸 전이효소(4GT)를 사용하여 분해 생성물인 포도당, 엿당 및 말토트리오스를 더 긴 말토올리고당으로 재활용함으로써 알룰로스 수율을 증가시킬 수 있고, 이는 αGP에 의해 인산분해적으로 절단되어 G1P를 생성할 수 있다. 4GT의 예는 국제 특허 출원 공개 WO2017/059278에 개시된 써모코쿠스 리토랄리스(유니프로트 ID O32462)로부터의 4GT; 또는 국제 특허 출원 공개 2020/092315에 개시된 혐기성 써모필라 균주 DSM 14523(유니프로트 E8MXP8)으로부터의 4GT이다. 본 발명의 일부 공정에서, 폴리인산염 및 인산염 포도당인산화효소(PPGK)가 공정에 첨가될 수 있고, 따라서 분해 생성물 포도당을 G6P로 인산화함으로써 알룰로스의 수율을 증가시킬 수 있다.
전분은 자연에서 가장 널리 사용되는 에너지 저장 화합물이며 대부분 식물 종자에 저장된다. 천연 전분은 선형 아밀로오스와 분지형 아밀로펙틴을 함유한다. 전분 유도체의 예는 아밀로스, 아밀로펙틴, 가용성 전분, 아밀로덱스트린, 말토덱스트린, 엿당, 과당 및 포도당을 포함한다. 셀룰로스 유도체의 예는 전처리된 바이오매스, 재생된 무정형 셀룰로스, 셀로덱스트린, 셀로비오스, 과당, 및 포도당을 포함한다. 자당 유도체는 과당과 포도당을 포함한다.
공정에서 전분 유도체를 사용하는 경우, 전분 유도체는 이소아밀라제, 풀루라나제, α-아밀라제, 또는 이들의 조합에 의해 촉매되는 전분의 효소적 가수분해에 의해 제조될 수 있다. 옥수수 전분에는 αGP 작용을 방해하는 많은 가지가 함유되어 있다. 이소아밀라제와 풀루라나제는 전분을 탈분지하여, 선형 아밀로덱스트린을 생성하는 데 사용할 수 있다. 이소아밀라제-전처리 및 풀루라나제-전처리된 전분은 최종 제품에서 더 높은 F6P 농도를 초래할 수 있다. 이소아밀라제와 풀루라나제는 알파-1,6-글리코시드 결합을 절단하여, 알파-글루칸 인산화효소에 의한 전분의 보다 완전한 분해를 허용한다. 알파-아밀라제는 알파-1,4-글리코시드 결합을 절단하므로, 알파-아밀라제는 전분을 단편으로 분해하여 알룰로스로 더 빠르게 전환시키는 데 사용된다.
알룰로스는 또한 과당으로부터 생성될 수 있다. 도 3을 참조하라. 본 발명에 따른 공정은 또한 과당을 F6P로 전환시키는 단계를 포함할 수 있으며, 여기서 이 단계는 적어도 하나의 효소에 의해 촉매되고, 선택적으로, 자당을 과당으로 전환시키는 단계는 적어도 하나의 효소에 의해 촉매된다. 예를 들어, 이 공정은 폴리인산염 프럭토키나제(PPFK)에 의해 촉매되는 폴리인산염 및 과당으로부터 F6P를 생성하는 단계를 수반한다. F6P에서 알룰로스로의 전환은 상기 설명되어 있다. 과당은, 예를 들어, 자당의 효소적 전환에 의해 생성될 수 있다. A6P가 알룰로스로 전환될 때 생성된 인산염 이온은 이후 자당을 G1P로 전환시키는 단계에서 재활용될 수 있다.
알룰로스는 또한 포도당으로부터 생성될 수 있다. 도 4를 참조하라. 본 발명에 따른 공정은 또한 적어도 하나의 효소에 의해 촉매되는 포도당을 G6P로 전환시키는 단계, 및 선택적으로, 자당을 과당으로 전환시키는 단계를 포함할 수 있으며, 여기서 이 단계는 적어도 하나의 효소에 의해 촉매된다. 예를 들어, 이 공정은 폴리인산염 포도당인산화효소(PPGK)에 의해 촉매되는 폴리인산염 및 포도당으로부터 G6P를 생성하는 단계를 수반한다. 포도당은, 예를 들어, 말토트리오스를 장쇄 말토덱스트린으로 재순환시키는 4-글루칸 전이효소에 의해 생성될 수 있다.
본 발명의 일부 방법에서, A6P가 알룰로스로 전환될 때 생성된 인산염 이온은, 특히 공정이 단일 반응 용기에서 수행되는 경우, 전분 유도체를 G1P로 전환시키는 단계(예를 들어, 도 1 참조), 셀룰로스 유도체를 G1P로 전환시키는 단계(예를 들어, 도 2 참조), 또는 자당을 G1P로 전환시키는 단계(도 5 참조)로 재순환된다. 추가로, PPFK 및 폴리인산염은 SP에 의한 자당의 인산분해 절단에 의해 생성된 과당으로부터 F6P를 생성함으로써 알룰로스 수율을 증가시키는 데 사용될 수 있다.
예를 들어, 당류로부터 알룰로스를 제조하는 공정은 하기 단계를 포함한다: (i) 하나 이상의 효소를 사용하여 당류를 포도당 1-인산염(G1P)으로 전환시키는 단계; (ii) 인산포도당자리옮김효소(PGM, EC 5.4.2.2)를 사용하여 G1P를 G6P로 전환시키는 단계; (iii) 인산포도당이성질화효소(PGI, EC 5.3.1.9)를 사용하여 G6P를 F6P로 전환시키는 단계; (iv) 알룰로스 6-인산염 에피머화효소(A6PE)를 통해 F6P를 A6P로 전환시키는 단계, 및 (v) 알룰로스 6-인산염 인산가수분해효소(A6PP)를 통해 A6P를 알룰로스로 전환시키는 단계. 본 발명의 개선된 공정에서, A6PE는 서열 번호: 1에 대해 적어도 90% 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP는 서열 번호: 2에 대해 적어도 90% 서열 동일성을 갖는 아미노산 서열을 포함한다. 이러한 공정에서, 예를 들어, 단계 (i)의 효소는 αGP이다. 일반적으로, 공정에 사용된 효소 단위의 비율은 1:1:1:1:1(αGP:PGM:PGI:A6PE:A6PP)이다. 효소 단위는 1 umol의 기질을 1 분 동안 생성물로 전환시키는 데 필요한 효소의 양이다. 따라서, 더 높은 활성을 갖는 효소는 동일한 반응을 촉매하는 더 낮은 활성을 갖는 효소와 비교하여, 하나의 효소 단위 당 효소 mg의 관점에서 더 적은 양의 효소를 가질 것이다. 제품 수율을 최적화하기 위해, 이러한 비율을 임의의 수의 조합으로 조정할 수 있다. 예를 들어, 특정 효소는 다른 효소의 양에 비해, 약 2배, 3배, 4배, 5배 등의 양으로 존재할 수 있다.
본 발명에 따른 알룰로스의 제조 공정은 다음의 추가 단계를 포함할 수 있다: 효소적 가수분해 또는 산 가수분해에 의해 다당류 및 올리고당류로부터 포도당을 생성하는 단계, 적어도 하나의 효소에 의해 촉매되는 포도당을 G6P로 전환시키는 단계, 효소적 가수분해 또는 산 가수분해에 의해 다당류 및 올리고당류로부터 과당을 생성하는 단계, 및 적어도 하나의 효소에 의해 촉매되는 과당을 G6P로 전환시키는 단계. 다당류 및 올리고당류의 예는 위에 열거되어 있다.
본 발명에 따른 알룰로스의 제조 공정은 단일 생물반응기 또는 반응 용기에서 수행될 수 있다. 달리, 단계는 또한 직렬로 배열된, 복수의 생물반응기 또는 반응 용기에서 수행될 수 있다. 바람직한 공정에서, 알룰로스의 효소적 생성은 단일 반응 용기에서 수행된다.
본 발명에 사용된 효소는 가용성인, 고정화된, 조립된, 또는 응집된 단백질의 형태를 취할 수 있다. 이들 효소는 당업계에 공지된 바와 같이, 기능성을 개선하기 위해 일반적으로 사용되는 불용성 유기 또는 무기 지지체에 흡착될 수 있다. 이들은 고분자 지지체, 예컨대 아가로스, 메타크릴레이트, 폴리스티렌, 페놀-포름알데히드, 또는 덱스트란 뿐만 아니라, 무기 지지체, 예컨대 유리, 금속 또는 탄소 기반 재료를 포함한다. 이러한 물질은 종종 고정된 효소의 부착 및 활성을 촉진하는 큰 표면 대 부피 비율 및 특수 표면으로 생성된다. 효소는 공유, 이온성, 또는 소수성 상호작용을 통해 이러한 고체 지지체에 부착될 수 있다. 효소는 또한 고형 지지체, 가장 흔히 폴리-히스티딘 서열에 대한 친화성을 갖는 또 다른 단백질 또는 펩티드 서열에 대한 공유 융합과 같은 유전적으로 조작된 상호작용을 통해 부착될 수 있다. 효소는 표면 또는 표면 코팅에 직접 부착되거나, 표면 또는 표면 코팅에 이미 존재하는 다른 단백질에 부착될 수 있다. 효소는 하나의 담체 상에, 개별 담체 상에, 또는 둘의 조합에 모두 고정될 수 있다(예를 들어, 담체 당 2개의 효소가 그 담체를 혼합함). 이러한 변형은 연속 반응기에서 회전율을 최적화하기 위해 균일하게 또는 정의된 층에서 혼합될 수 있다. 예를 들어, 반응기의 시작은 높은 초기 G1P 증가를 보장하기 위해 aGP의 층을 가질 수 있다. 효소는 하나의 운반체 상에, 개별 운반체 상에, 또는 그룹으로 모두 고정될 수 있다. 이러한 효소는 회전율을 최적화하기 위해 균일하게 또는 정해진 층 또는 구역에서 혼합될 수 있다.
HEPES, PBS, BIS-TRIS, MOPS, DIPSO, Trizma, 인산염 완충액 등과 같은 당업계에 공지된 임의의 적합한 생물학적 완충액이 본 발명의 개선된 공정에 사용될 수 있다. 모든 실시양태에 대한 반응 완충액은 4.0 내지 9.0 범위의 pH를 가질 수 있다. 보다 바람직하게는, 반응 완충액 pH는 약 6.0 내지 약 7.8의 범위일 수 있다. 예를 들어, 반응 완충액 pH는 6.0, 6.2, 6.4, 6.6, 6.8, 7.0, 7.2, 7.3, 7.4, 7.5, 7.6, 7.7 또는 7.8일 수 있다.
본 발명의 일부 개선된 공정에서 반응 완충액은 2가 금속 양이온을 함유한다. 예는 Mn2+, Co2+, Mg2+ 및 Zn2+ 등을 포함하고, 바람직하게는 Co2+ 및 Mg2+ 이다. 2가 금속 양이온의 농도는 약 0 mM 내지 약 150 mM, 약 0 mM 내지 약 100 mM, 약 1 mM 내지 약 50 mM, 바람직하게는 약 5 mM 내지 약 50 mM, 또는 바람직하게는 약 5 mM 내지 약 50 mM의 범위, 또는 보다 바람직하게는 10 mM 내지 약 50 mM의 범위일 수 있다. 예를 들어, 2가 금속 양이온 농도는 약 0.1 mM, 약 0.5 mM, 약 1 mM, 약 1.5 mM, 약 2 mM, 약 2.5 mM, 약 5 mM, 약 6 mM, 약 7 mM, 약 8 mM, 약 9 mM, 약 10 mM, 약 15 mM, 약 20 mM, 약 25 mM, 약 30 mM, 약 35 mM, 약 40 mM, 약 45 mM, 약 50 mM, 또는 약 55 mM일 수 있다.
개선된 공정 단계가 수행되는 반응 온도는 37 내지 85 ℃ 범위일 수 있다. 보다 바람직하게는, 단계는 약 37 ℃ 내지 약 85 ℃ 범위의 온도에서 수행된다. 온도는, 예를 들어, 약 40 ℃, 약 45 ℃, 약 50℃, 약 55 ℃ 또는 약 60 ℃일 수 있다. 바람직하게는, 반응 온도는 약 50 ℃이다. 본 발명의 일부 개선된 공정에서, 반응 온도는 일정하고, 공정 동안 변하지 않는다.
개시된 공정의 반응 시간은 필요에 따라 조정될 수 있고, 약 0.5시간 내지 약 48시간의 범위일 수 있다. 예를 들어, 반응 시간은 약 16시간, 약 18시간, 약 20시간, 약 22시간, 약 24시간, 약 26시간, 약 28시간, 약 30시간, 약 32시간, 약 34시간, 약 36시간, 약 38시간, 약 40시간, 약 42시간, 약 44시간, 약 46시간, 또는 약 48시간일 수 있다. 보다 바람직하게는 반응 시간은 약 24시간이다.
본 발명의 개선된 공정의 단계는 충전층 반응기 또는 유사한 장치를 사용하여 회분식으로 또는 연속식으로 실행할 수 있다. 연속 공정에서, 용액 말토덱스트린은 용액이 다운스트림 처리를 위해 컬럼을 떠날 때 알룰로스로의 전환이 완료되는 속도로 고정된 효소의 층을 통해 펌핑될 것이다. 예를 들어, 말토덱스트린이 컬럼을 떠날 때 최대 알룰로스 수율이 달성되도록, 200g/L의 말토덱스트린을 고정된 효소로 채워진 컬럼(예를 들어, 50℃로 유지됨)을 통해 펌핑할 수 있다. 이 공정론은 배치 방법보다 체적 생산성이 더 높다. 이는 당사 제품이 컬럼 및 반응 조건과 접촉하는 시간을 제한하여, 제품 분해의 가능성(예를 들어, 잠재적인 하이드록시메틸푸르푸랄 형성)을 줄인다. 배치 방식이든 연속 방식이든 본 발명의 다양한 단계는 다른 단계와 동일한 반응 조건을 사용하여 수행될 수 있다. 예를 들어, 단일 생물반응기 또는 반응 용기를 사용하는 본 발명의 특정 공정에서, 반응 조건, 예컨대 pH 및 온도, 및 반응 완충액은 공정의 모든 단계에 대해 일정하게 유지된다.
A6P의 A6PP 탈인산화에 의해 생성된 인산염 이온은, 특히 모든 공정 단계가 단일 생물반응기 또는 반응 용기에서 수행되는 경우, 당류를 G1P로 전환시키는 공정 단계에서 재활용될 수 있다. 개시된 공정에서 인산염을 재순환시키는 능력은 비화학량론적 양의 인산염이 사용되도록 하여, 반응 인산염 농도를 낮게 유지한다. 이는 전반적인 경로 및 공정의 전반적인 속도에 영향을 미치지만, 개별 효소의 활성을 제한하지 않고 알룰로스 제조 공정의 전반적인 효율성을 허용한다.
예를 들어, 반응 인산염 농도는 약 0.1 mM 내지 약 300 mM, 약 0.1 mM 내지 약 150 mM, 약 1 mM 내지 약 50 mM, 바람직하게는 약 5 mM 내지 약 50 mM, 또는 바람직하게는 약 0.1 mM 내지 약 50 mM, 보다 바람직하게는 약 10 mM 내지 약 50 mM의 범위일 수 있다. 예를 들어, 반응 인산염 농도는 약 0.1 mM, 약 0.5 mM, 약 1 mM, 약 1.5 mM, 약 2 mM, 약 2.5 mM, 약 5 mM, 약 6 mM, 약 7 mM, 약 8 mM, 약 9 mM, 약 10 mM, 약 15 mM, 약 20 mM, 약 25 mM, 약 30 mM, 약 35 mM, 약 40 mM, 약 45 mM, 약 50 mM, 또는 약 55 mM일 수 있다.
따라서, 낮은 인산염 농도는 낮은 총 인산염으로 인해 생산 비용을 줄이고, 따라서 인산염 제거 비용을 낮춘다. 또한 고농도의 무 인산염에 의한 A6PP의 억제를 방지하고 인산염 오염에 대한 가능성을 줄인다.
또한, 본원에 개시된 공정은 인산염의 공급원으로서 ATP를 첨가하지 않고, 즉 ATP-무함유로 수행될 수 있다. NAD(H)를 추가하지 않고도, 즉 NAD(H) 없이 공정을 수행할 수도 있다. 다른 이점은 또한 개시된 알룰로스 제조 공정의 적어도 하나의 단계가 에너지적으로 유리한 화학 반응을 수반한다는 사실을 포함한다. 활성이 더 높은 효소를 사용하면 전체 에너지에 영향을 미치지 않지만, 개선된 공정에서 더 적은 양의 효소를 사용하는 능력이 유리하다. 장점은 제품의 총 생산 비용에서 효소의 전반적인 비용이 절감된다는 것이다.
본 발명에 따른 공정은 전반적인 반응에 대해 매우 유리한 평형 상수로 인해 높은 수율을 달성할 수 있다. 이론적으로, 출발 물질이 중간체로 완전히 전환되면 최대 99%의 수율을 얻을 수 있다. 또한, 본 발명에 따른 A6P를 알룰로스로 전환시키는 단계는 공급원료에 관계없이, 비가역적 인산가수분해효소 반응이다. 따라서, 알룰로스가 매우 높은 수율로 생성된다.
본 발명의 공정은 저비용 출발 물질을 사용하고 공급원료 및 생성물 분리와 연관된 비용을 감소시킴으로써 생산 비용을 감소시킨다. 전분 및 그 유도체, 셀룰로스 및 그 유도체, 및 자당은, 예를 들어, 결정질 과당보다 저렴한 공급원료이다. 알룰로스가 과당으로부터 생성될 때, 수율은 단지 약 28%에 불과하다(WO 2016/160573). 이후 과당과 알룰로스는 크로마토그래피를 통해 분리되며, 이는 함께 개시된 방법보다 더 높은 생산 비용을 초래한다.
본 발명에 따른 공정은 알룰로스의 용이한 회수를 허용하고, 분리 비용은 최소화된다. 바람직하게는, 본 발명의 공정에서, 알룰로스의 회수는 크로마토그래피 분리를 통하지 않는다. 연속 반응에서 알룰로스를 생산한 후, 생성물은 대신 한외여과, 이온 교환(양이온 다음 음이온, 혼합층 아님), 농축, 결정화, 결정 분리, 및 건조를 거친다. 알룰로스의 높은 수율로 인해, 알룰로스를 정제하는데 필요한 모든 것은 결정화 단계이다. 결정화 전에 알룰로스를 추가로 정제하기 위해, 한외여과를 사용하여 결정화 과정에 존재하는 효소의 위험을 제거하거나 나노여과를 사용하여 알룰로스와 공결정화되거나 모액(말토덱스트린, 말토테트라오스, 말토트리오스, 말토오스 등)의 재활용 가능성을 제한할 수 있는 전환되지 않은 덱스트린을 제거할 수 있다.
본 발명에 따른 개선된 알룰로스 제조 공정은, 다음 단계를 포함한다: (i) 하나 이상의 효소를 사용하여 당류를 포도당 1-인산염(G1P)으로 전환시키는 단계; (ii) 인산포도당자리옮김효소(PGM, EC 5.4.2.2)를 사용하여 G1P를 G6P로 전환시키는 단계; (iii) 인산포도당이성질화효소(PGI, EC 5.3.1.9)를 사용하여 G6P를 F6P로 전환시키는 단계; (iv) 알룰로스 6-인산염 에피머화효소(A6PE)를 통해 F6P를 A6P로 전환시키는 단계, 및 (v) 알룰로스 6-인산염 인산가수분해효소(A6PP)를 통해 A6P를 알룰로스로 전환시키는 단계(여기서 A6PE가 서열 번호:1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP가 서열 번호:2에 대해 적어도 90% 서열 동일성을 갖는 아미노산 서열을 포함함). 이 공정은 바람직하게는 단일 생물반응기 또는 반응 용기에서 수행된다.
바람직하게는, 본 발명에 따른 개선된 알룰로스 제조 공정은 하기 단계를 포함한다: (i) αGP를 사용하여 당류를 포도당 1-인산염(G1P)으로 전환시키는 단계(여기서 당류는 전분, 또는 하나 이상의 전분 유도체, 또는 이들의 조합으로 이루어진 군으로부터 선택됨); (ii) 인산포도당자리옮김효소(PGM, EC 5.4.2.2)를 사용하여 G1P를 G6P로 전환시키는 단계; (iii) 인산포도당이성질화효소(PGI, EC 5.3.1.9)를 사용하여 G6P를 F6P로 전환시키는 단계; (iv) 알룰로스 6-인산염 에피머화효소(A6PE)를 통해 F6P를 A6P로 전환시키는 단계, 및 (v) 알룰로스 6-인산염 인산가수분해효소(A6PP)를 통해 A6P를 알룰로스로 전환시키는 단계(A6PE가 서열 번호:1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하고/하거나, A6PP가 서열 번호:2에 대해 적어도 90% 서열 동일성을 갖는 아미노산 서열을 포함함). 공정은 바람직하게는 단일 반응기 용기에서 수행되고 위에서 논의된 하나 이상의 다양한 공정 조건을 혼입할 수 있다.
실시예
재료 및 방법 포도당 1-인산염, 염화 마그네슘, 인산 나트륨(일염기성 및 이염기성)을 포함한 모든 화학물질은, 달리 명시되지 않는 한, 시약 등급 이상이며 Sigma-Aldrich(St. Louis, MO, USA) 또는 Fisher Scientific(Pittsburgh, PA, USA)에서 구입된다. 대장균 BL21(DE3)(Sigma-Aldrich, St. Louis, MO, USA)을 재조합 단백질 발현을 위한 숙주 세포로 사용하였다. 50 mg L-1 카나마이신을 함유하는 ZYM-5052 배지를 대장균 세포 성장 및 재조합 단백질 발현에 사용하였다.
재조합 효소의 생산 및 정제 단백질 발현 플라스미드(pET28a)를 함유하는 대장균 BL21(DE3) 균주를 50 mg L-1 카나마이신을 함유하는 ZYM-5052 배지 100 mL와 함께 1 L 삼각 플라스크에서 인큐베이션하였다. 세포를 16 내지 24 시간 동안 220 rpm에서 회전식 진탕시키면서 37 ℃에서 성장시켰다. 세포를 12 ℃에서 원심분리하여 수확하고 열 침전을 위해, 50 mM NaCl 및 5 mM MgCl2를 함유하는 20 mM HEPES(pH 7.5); 또는 Ni 정제를 위해 300 mM NaCl 및 5mM 이미다졸을 함유하는 20 mM HEPES(pH 7.5)로 1회 세척하였다. 세포 펠렛을 동일한 완충액에 재현탁하고, 초음파 처리하여 용해시켰다. 원심분리 후, 상층액의 표적 단백질을 50 내지 80 ℃에서 30 분 동안 열 안정성에 대해 시험하였다. His 태그가 붙은 단백질은 Profinity IMAC Ni-Charged Resin(Bio-Rad, Hercules, CA, USA)으로 정제되었다. 정제된 단백질의 양은 280 nm에서의 흡광도에 의해 정량화되었고 표 1의 상대 발현 수율 계산에 사용되었다.
열 안정성 단백질 발현 플라스미드(pET28a)를 품은 대장균 BL21(DE3) 균주를 50 mg L-1 카나마이신을 함유하는 ZYM-5052 배지 100 mL와 함께 1-L 삼각 플라스크에서 인큐베이션 하였다. 세포를 16 내지 24 시간 동안 220 rpm에서 회전식 진탕시키면서 37 ℃에서 성장시켰다. 세포를 12 ℃에서 원심분리하여 수확하고, 50 mM NaCl 및 5 mM MgCl2를 함유하는 20 mM HEPES(pH 7.5)로 1회 세척하였다. 세포 펠렛을 동일한 완충액에 재현탁하고, 초음파 처리하여 용해시켰다. 원심분리 후, 상층액의 표적 단백질을 50 내지 80 ℃에서 30분 동안 열 안정성에 대해 시험하였다. 재조합 단백질의 안정성은 나트륨 도데실 황산염 폴리아크릴아미드 겔 전기영동(SDS-PAGE)에 의해 조사되었고, 표 1에 기술된 바와 같이 육안 검사에 의해 기록되었다.
실시예 1. 개선된 공정에서 알룰로스로의 G1P의 알룰로스 6-인산염 에피머화효소(A6PE)-의존성 전환에 대한 상대적 활성 평가. 유니프로트 ID A0A223HZI7("A0A223HZI7 A6PE")의 아미노산 서열을 갖는 A6PE를 포함하는 효소적 공정에 의한 G1P의 알룰로스로의 전환은 각 공정에서 사용된 A6PE에 대해서만 다른 G1P에서 알룰로스로의 전환 공정과 비교되었다. 보다 구체적으로, G1P에서 알룰로스로의 전환은 하기를 포함하는 공정을 사용하여 비교되었다: 유니프로트 ID A0A150LLZ1의 아미노산 서열을 갖는 PGM; 유니프로트 ID Q5SLL6의 아미노산 서열을 갖는 PGI; 유니프로트 ID D9TQJ4, 유니프로트 ID A0A090IXZ8, 유니프로트 ID A8UV28, 유니프로트 ID G7M2I3, 유니프로트 ID A0A094WLM1, 유니파크 ID UPI000411882A, 또는 유니프로트 P32719(P32719 효소는 50℃에서 불안정함)의 아미노산 서열을 갖는 A0A223HZI7 A6PE 또는 A6PE; 및 유니프로트 ID A0A0E3NCH4의 아미노산 서열을 갖는 A6PP. 각 공정은 38.5 mM G1P, 50 mM HEPES pH 7.2, 15 mM MgCl2, 0.5 mM CoCl2, 0.05 g/L PGM, 0.05 g/L PGI, 0.025 g/L A6PE, 0.025 g/L A6PE, 0.15 g/L A6PP를 함유하는 0.20 mL 반응 혼합물에서 수행되었다. 반응물을 50 ℃에서 3시간 동안 인큐베이션 하였다. A6PE는 G1P를 알룰로스로 전환시키는 속도 제한 효소였다. Vivaspin® 2 농축기(10,000 MWCO)를 사용하여 효소 여과를 통해 반응을 중단하고, Agilent Hi-Plex H 컬럼과 굴절률 검출기를 사용하여 HPLC(Agilent 1100 시리즈)로 분석했다. 샘플 실행은 65 ℃에서 15.5 분 동안 0.6 mL/min의 5 mM H2SO4에서 수행되었다.
결과는 유니프로트 A8UV28 아미노산 서열을 갖는 A6PE가 시험된 조건 하에서 활성이 아니라는 점을 제외하고는, 활성에서 유의미한 A6PE-의존성 차이를 나타내지 않았다.
실시예 2. 낮은 알룰로스 6-인산염 에피머화효소(A6PE)-의존성 알룰로스에서 과당으로의 전환 활성 평가. A0A223HZI7 A6PE를 포함하는 효소적 공정에 의한 알룰로스의 과당으로의 전환을 각 공정에서 사용된 A6PE에 대해서만 다른 알룰로스에서 과당으로의 전환 공정과 비교하였다. 보다 구체적으로, 알룰로스에서 과당으로의 전환은 하기의 아미노산 서열을 갖는 A0A223HZI7 A6PE 또는 A6PE를 포함하는 공정을 사용하여 비교되었다: 유니프로트 ID D9TQJ4, 유니프로트 ID A0A090IXZ8, 유니프로트 ID G7M2I3, 유니프로트 ID A0A093WLM1, 유니프로트 ID A0A093WLM1, 유니파크 ID UPI000411882A(유니프로트 ID P32719 및 유니프로트 ID A8UV28의 아미노산 서열을 갖는 A6PE는 경로와의 비호환성으로 인해 생략됨). 각 공정은 200 g/L 알룰로스, 10 mM HEPES pH 7.2, 5 mM MgCl2, 0.5 mM CoCl2 및 0.025 g/L 또는 0.25 g/L A6PE를 함유하는 0.20 mL 반응 혼합물에서 수행되었다. 반응물을 50 ℃에서 6시간 동안 인큐베이션 하였다. Vivaspin 2 농축기(10,000 MWCO)를 사용한 효소의 여과를 통해 반응을 중단하고, SupelCogel Pb-칼럼 및 굴절률 검출기를 사용하여 HPLC(Agilent 1100 시리즈)를 통해 분석하였다. 샘플 실행은 80 ℃에서 40 분 동안 0.6 mL/분의 초순수에서 수행되었다
표 2에 요약된 결과는 시험된 A6PE가 유니프로트 ID A0A090IXZ8 및 유니파크 ID UPI000411882A의 아미노산 서열을 갖는 효소를 제외하고는 알룰로스로부터 비교적 적은 과당을 생성함을 나타냈다. 뚜렷하게, 0.025 g/L의 효소 조성에서 A0A223HZI7 A6PE에 대해 알룰로스의 과당으로의 전환이 관찰되지 않았다.
실시예 3. 말토덱스트린의 알룰로스로의 전환 특성이 개선된 알룰로스 6-인산염 에피머화효소(A6PE)의 상대적 활성 평가. A0A223HZI7 A6PE(알룰로스로부터 과당 활성을 나타내지 않음)를 포함하는 효소적 공정에 의한 말토덱스트린의 알룰로스로의 전체 캐스케이드 전환은, 알룰로스로부터의 과당 활성이 다른 F6PE가 알룰로스 수율에 어떻게 영향을 미치는지 확인하기 위해, 각 공정에서 사용된 A6PE에 대해서만 다른 말토덱스트린에서 알룰로스로의 전환 공정과 비교되었다. 보다 구체적으로, 말토덱스트린에서 알룰로스로의 전환은 하기를 포함하는 공정을 사용하여 비교되었다: 유니프로트 ID G8NCC0의 아미노산 서열을 갖는 αGP; 유니프로트 ID A0A150LLZ1의 아미노산 서열을 갖는 PGM; 유니프로트 ID Q5SLL6의 아미노산 서열을 갖는 PGI; 유니프로트 ID A0A090IXZ8(높은 알룰로스로부터의 과당 활성을 입증함) 또는 유니파크 ID UPI000411882A(보통의 알룰로스로부터의 과당 활성을 입증함)의 아미노산 서열을 갖는 A0A223HZI7 A6PE 또는 A6PE; 유니프로트 ID A0A0E3NCH4의 아미노산 서열을 갖는 A6PP; 및 유니프로트 ID E8MXP8의 아미노산 서열을 갖는 4GT. 각 공정은 100 g/L 탈분지된 Sigma Aldrich 말토덱스트린 DE 4-7, 25 mM 인산 나트륨 pH 7.2, 15 mM MgCl2, 0.5 mM CoCl2, 0.3 g/L αGP, 0.075 g/L PGM, 0.075 g/L PGI, 0.1 g/L A6PE, 0.1 g/L A6PP 및 0.04 g/L 4GT를 함유하는 0.20 mL 반응 혼합물 에서 수행되었다. 반응은 분석 당시 반응이 완전히 완료되지 않도록 50 ℃에서 18시간 동안 인큐베이션 하였다. Vivaspin® 2 농축기(10,000 MWCO)를 사용한 효소 여과를 통해 반응을 중단하고 SupelCogel® Pb-칼럼 및 굴절률 검출기를 사용하여 HPLC(Agilent® 1100 시리즈)를 통해 분석하였다. 샘플 실행은 80 ℃에서 40분 동안 0.6mL/분의 초순수에서 수행되었다.
결과는, 도 6에 도시된 바와 같이, 유니파크 ID UPI000411882A의 아미노산 서열을 갖는 A6PE를 수반하는 공정이 A0A223HZI7 A6PE를 수반하는 공정보다 실질적으로 더 많은 과당을 생성함을 보여주었다. 예상한 대로, 유니프로트 ID A0A090IXZ8의 아미노산 서열을 갖는 A6PE를 수반하는 공정은 중간 양의 과당을 생성하였다. A0A223HZI7 A6PE를 수반하는 공정은 18시간 동안 가장 많은 알룰로스를 생성하였다. 이는 가장 높은 알룰로스 수율 경로, 및 A6PE를 사용하여 알룰로스를 생성하기 위해 이전에 개시된 것보다 더 효율적인 하나의 경로를 초래하였다. 주어진 A6PE 효소에 대한 F6P/A6P 대 알룰로스에 대한 상대적 친화도는 알룰로스로부터의 과당 활성 대 말트로덱스트린으로부터의 알룰로스 캐스케이드 간의 관찰된 차이에 의해 입증된다. 예를 들어, 유니프로트 ID A0A090IXZ8의 아미노산 서열을 갖는 A6PE는 유니파크 ID UPI000411882A의 아미노산 서열을 갖는 A6PE와 비교하여 알룰로스 단독으로부터의 경우 훨씬 더 많은 양의 과당을 생성하지만, 완전한 캐스케이드 반응에서 유니프로트 ID A0A090IXZ8의 아미노산 서열을 갖는 A6PE가 F6P/A6P가 유니파크 ID UPI000411882A의 아미노산 서열을 갖는 A6PE보다 이 효소에 대해 더 효율적으로 알룰로스와 경쟁할 수 있기 때문에 더 잘 수행된다.
실시예 4. G1P에서 알룰로스로의 전환 특성이 개선된 알룰로스 6-인산염 인산가수분해효소(A6PP)의 상대적 활성 평가. 유니프로트 ID A0A0E3NCH4의 아미노산 서열을 갖는 A6PP("A0A0E3NCH4 A6PP")를 사용하는 효소적 공정에 의한 G1P의 알룰로스로의 전환을 각 공정에서 사용된 A6PP에 대해서만 다른 알룰로스 전환 공정으로의 G1P와 비교하였다. 보다 구체적으로, G1P에서 알룰로스로의 전환은 하기를 포함하는 공정을 사용하여 비교되었다: 유니프로트 ID A0A150LLZ1의 아미노산 서열을 갖는 PGM, 유니프로트 ID Q5SLL6의 아미노산 서열을 갖는 PGI, 유니프로트 ID D9TQJ4의 아미노산 서열을 갖는 A6PE, 유니프로트 ID A3DC21의 아미노산 서열을 갖는 A0A0E3NCH4 A6PP 또는 A6PP. 이전에 개시된 유니프로트 ID Q5LGR4 또는 유니프로트 ID Q89ZR1의 아미노산 서열을 갖는 A6PP는 이들 효소가 50 ℃에서 불안정하기 때문에 비교에 포함될 수 없다. 각 공정은 38.5 mM G1P, 50 mM HEPES pH 7.2, 0.5 mM CoCl2, 0.05 g/L PGM, 0.05 g/L PGI, 0.025 g/L A6PE 및 0.05 g/L A6PP을 포함하는 0.20 mL 반응 혼합물에서 수행되었다. 반응물을 50 ℃에서 3 시간 동안 인큐베이션 하였다. A6PP는 G1P를 알룰로스로 전환시키는 속도 제한 효소였다. Vivaspin® 2 농축기(10,000 MWCO)를 사용한 효소 여과를 통해 반응을 중단하고, Agilent Hi-Plex® H 컬럼 및 굴절률 검출기를 사용하여 HPLC(Agilent 1100 시리즈)를 통해 분석하였다. 샘플 실행은 65 ℃에서 15.5 분 동안 0.6 mL/min으로 5 mM H2SO4에서 수행되었다. 표 3에 요약된 결과는 유니프로트 ID A3DC21의 아미노산 서열을 갖는 이전에 개시된 A6PP를 사용하는 공정과 비교하여 알룰로스 생성에서 2.2배 개선을 나타내었다.
서열 목록
서열 번호: 1; A6PE; 유니프로트 ID A0A223HZI7; 써모아나에로박테리움 써모사카롤리티쿰
MKPMFAPSLMCANFLDLKNQIEILNERADIYHIDIMDGHYVKNFALSPYLMEQLKTIAKIPMDAHLMVENPADFLECIAKSGATYISPHAETINKDAFRIMRTIKALGCKTGIVLNPATPVEYIKYYIGMLDKITILTVDAGFAGQTFINEMLDKIAEIKSLRDQNGYSYLIEVDGSCNEKTFKQLAEAGTDVFVVGSSGLFNLDTDLKVAWDKMMDTFTRCTSN
서열 번호: 2; A6PP; 유니프로트 ID A0A0E3NCH4; 메타노사르시나 써모필라
MLKALIFDMDGVLVDSMPFHAAAWKKAFFEMGMEIQDSDIFAIEGSNPRNGLPLLIRKARKEPEAFDFEAITSIYRQEFKRVFEPKAFEGMKECLEVLKKRFLLSVVSGSDHVIVHSIINRLFPGIFDIVVTGDDIINSKPHPDPFLKAVELLNVRREECVVIENAILGVEAAKNARIYCIGVPTYVEPSHLDKADLVVEDHRQLMQHLLSLEPANGFRQ
서열 번호: 3; A6PE; 유니프로트 ID D9TQJ4; 써모아나에로박테리움 써모사카롤리티쿰
MKYLFSPSLMCMNLIKLNEQISVLNSKADFLHVDIMDGHFVKNITLSPFFIEQIKSYVNIPIDAHLMVENPGDYIEICEKSGASFITIHAETINREAFRIIDRIKSHGLMVGIALNPATPISEIKHYINKIDKITIMTVDPGFAGQPFIPEVLEKIRDLKRLKDDNNYNYLIEADGSCNKNTFQVLKDAGCKVFVLGSSGLFNLSDDLGKAWEIMIGNFNG
서열 번호: 4; A6PE; 유니프로트 ID A0A090IXZ8; 바실러스 써모아밀로보란스
MSNKIEFSPSLMTMDLDKFKEQITFLNNHVGSYHIDIMDGHYVPNITLSPWFVQEVRKISDVPMSAHLMVTNPSFWVQQLIDIKCEWICMHVETLDGLAFRLIDQIHDAGLKAGVVLNPETSVDAIRPYIDLVDKVTIMTVDPGFAGQRFIDSTLEKIVELRKLREEHGYKYVIEMDGSSNRKSFKKIYEAGPDIYIIGRSGLFGLHEDIEKAWEIMCKDFEEMTGEKVL
서열 번호: 5; A6PE; 유니프로트 ID P32719; 대장균
MKISPSLMCMDLLKFKEQIEFIDSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPLDCHLMVTRPQDYIAQLARAGADFITLHPETINGQAFRLIDEIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAWREREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGTSGLFNHAENIDEAWRIMTAQILAAKSEVQPHAKTA
서열 번호: 6; A6PE; 유니프로트 ID A8UV28; 하이드로게니비르가 속균 128-5-R1-1
MEKLLAPSILAGDWWNIGEQIEATLRGGADIIHFDVMDGHFVPNITVGPEILTSISRRVNVPVDAHLMIENPDRYIPSFVEAGAKWISVHIENVPHIHRTLTLIRELGAKAGVVLNPGTPLSAVEEAIHYADYVLLMSVNPGFSGQRFIERSLERLSLLRDMRDRLNPDCLIEVDGGVKEDNVVEVVRAGADVVVVGSGIFSAKDVEAQTRKLKDLISSAVAV
서열 번호: 7; A6PE; 유니파크 ID UPI000411882A; 브레비바실러스 써모러버
MGFKFSPSLMCMNLLDIQHQIEVMNRRADLVHIDIMDGHYVKNLTLSPFFIEQLKESLHVPMDVHLMVENPTDFIERVKEAGASIISPHAETINTDAFRIIDKVKSLGCQMGIVLNPATPIAYIQHYIHLVDKITIMTVDPGYAGQKFIPEMLEKIRQAKRLKEERGYRYLIEVDGSCNVGTFKRLAEAGAEVFIVGSSGLFNLHPDLEVAWDMMMDNFQREVGETTA
서열 번호: 8; A6PE; 유니프로트 ID G7M2I3; 클로스트리디움 속균 DL-VIII
MKPMFAPSLMCANFLDLKNQIEILNERADIFHVDIMDGHYVKNFSLSPAMMEQLKTITKIPMDAHLMVENPADFLEGIAKAGATYISPHAETINKDAFRIMRTIKALGCKTGVVLNPATPVEYIKHYLGMLDKITILTVDAGFAGQTFIEEMLDKIEEVKRLREENGYSYLIEVDGSCNEKTFKKLAEAGTEVFIVGSSGLFNLDADLKVSWDKMMNMFNKCINN
서열 번호: 9; A6PE; 유니프로트 ID A0A094WLM1; 호알칼리성 바실러스균
MYKFSPSLMCMDLSRFKEQVEVLNDKADFYHVDIMDGHFVKNITLSPFFIQELKKITDVPIDAHLMVTNPADFVEMTIDAGADYISLHAETINGNAFRLINQIKEKGKKFGVVLNPATPLESIRHYIQHVDKLTIMTVDPGFAGQKFVEEMIGKIKEAKELKERNGYKYLITIDGSCNKNTFKKLVEAGAEVLIVGSSGLFGLDEDVNIAWDKMMDTFHLEVKDISQV
서열 번호: 10; A6PP; 유니프로트 ID A3DC21; 헝가테클로스트리디움 써모셀룸
MIKYKAVFFDFDYTLADSSKAVIECINYALQKMGYPESSPESICRTIGLTLAEAFKILSGDTSDSNADLFRQYFKERADLVMCDRTVMYSTVECVLKKLKKADVKTGIVSTKYRYRIEDILKRDKLLQYFDVIVGGEDVAAHKPDPEGLLKAISMVGCQKEEVLFVGDSTVDARTAKNAGVDFVAVLTGTTGANEFSEYNPGAVIEDLSGLLDMFML
서열 번호: 11; A6PP; 유니프로트 ID Q5LGR4; 박테로이데스 프라길리스
MKYTVYLFDFDYTLADSSRGIVTCFRSVLERHGYTGITDDMIKRTIGKTLEESFSILTGITDADQLESFRQEYSKEADIYMNANTILFPDTLPTLTHLKKQGIRIGIISTKYRFRILSFLRNHMPDDWFDIIIGGEDVTHHKPDPEGLLLAIDRLKACPEEVLYIGDSTVDAGTAAAAGVSFTGVTSGMTTAQEFQAYPYDRIISTLGQLISVPEDKSGCPL
서열 번호: 12; A6PP; 유니프로트 ID Q89ZR1; 박테로이드 테타이오타오미크론
MNYKTYLFDFDYTLADSSRGIVTCFRNVLNRHQYTNVTDEAIKRTIGKTLEESFSILTGVTDWEQLTAFRQEYRLEADVHMNVNTRLFPDTLSTLKELKERGARIGIISTKYRFRILSFLDEYLPENFLDIVVGGEDVQAAKPSPEGIKFALEHLGRTPQETLYIGDSTVDAETAQNAGVDFAGVLNGMTTADELRAYPHRFIMENLSGLLYI
서열 번호: 13; PGM; 유니프로트 ID A0A150LLZ1; 칼디바실러스 데비리스
MEWKQRAERWLRFENLDPELKKQLEEMAKDEKKLEDLFYKYLEFGTGGMRGEIGPGTNRINIYTVRKASEGLARFLLASGGEEKAKQGVVIAYDSRRKSREFALETAKTVGKHGIKAYVFESLRPTPELSFAVRYLHAAAGVVITASHNPPEYNGYKVYGEDGGQLTPKAADELIRYVYEVEDELSLTVPGEQELIDRGLLQYIGENIDLAYIEKLKTIQLNRDVILNGGKDLKIVFTPLHGTAGQLVQTGLREFGFQNVYVVKEQEQPDPDFSTVKSPNPEEHEAFEIAIRYGKKYDADLIMGTDPDSDRLGIVVKNGQGDYVVLTGNQTGAILLYYLLSQKKEKGMLVRNSAVLKTIVTSELGRAIASDFGVETIDTLTGFKFIGEKIKEFKETGSHVFQFGYEESYGYLIGDFVRDKDAIQAALFAAEAAAYYKAQGKSLYDVLMEIYKKYGFYKESLRSITLKGKDGAEKIRAIMDAFRQNPPEEVSGIPVAITEDYLTQKRVDKAAGQTTPIHLPKSNVLKYYLADESWFCIRPSGTEPKCKFYFAVRGDSEAQSEARLRQLETNVMAMVEKILQK
서열 번호: 14; PGI; 유니프로트 ID Q5SLL6; 써머스 써모필러스
MLRLDTRFLPGFPEALSRHGPLLEEARRRLLAKRGEPGSMLGWMDLPEDTETLREVRRYREANPWVEDFVLIGIGGSALGPKALEAAFNESGVRFHYLDHVEPEPILRLLRTLDPRKTLVNAVSKSGSTAETLAGLAVFLKWLKAHLGEDWRRHLVVTTDPKEGPLRAFAEREGLKAFAIPKEVGGRFSALSPVGLLPLAFAGADLDALLMGARKANETALAPLEESLPLKTALLLHLHRHLPVHVFMVYSERLSHLPSWFVQLHDESLGKVDRQGQRVGTTAVPALGPKDQHAQVQLFREGPLDKLLALVIPEAPLEDVEIPEVEGLEAASYLFGKTLFQLLKAEAEATYEALAEAGQRVYALFLPEVSPYAVGWLMQHLMWQTAFLGELWEVNAFDQPGVELGKVLTRKRLAG
서열 번호: 15; 4GT; 유니프로트 ID E8MXP8; 혐기성 써모필라
MSLFKRASGILLHPTSLPGPDGIGDLGPEAYRWVNFLAESGCSLWQILPLGPTGFGDSPYQCFSAFAGNPYLVSPALLLDEGLLTSEDLADRPEFPASRVDYGPVIQWKLTLLDRAYVRFKRSTSQKRKAAFEAFKEEQRAWLLDFSLFMAIKEAHGGASWDYWPEPLRKRDPEALNAFHRAHEVDVERHSFRQFLFFRQWQALRQYAHEKGVQIIGDVPIFVAYDSADVWSHPDLFYLDETGKPTVVAGVPPDYFSATGQLWGNPLYRWDYHRETGFAWWLERLKATFAMVDIVRLDHFRGFAGYWEVPYGMPTAEKGRWVPGPGIALFEAIRNALGGLPIIAEDLGEITPDVIELREQLGLPGMKIFQFAFASDADDPFLPHNYVQNCVAYTGTHDNDTAIGWYNSAPEKERDFVRRYLARSGEDIAWDMIRAVWSSVAMFAIAPLQDFLKLGPEARMNYPGRPAGNWGWRYEAFMLDDGLKNRIKEINYLYGRLPEHMKPPKVVKKWT
서열 번호: 16; αGP; 유니프로트 ID G8NCC0; 써모스 속균 CCB_US3_UF1
MPLLPEPLSGLKELAYNLWWSWNPEAAELFQEIDPSLWKRFRGNPVKLLLEADPGRLEGLAATSYPARVGAVVEALRAYLREREEKQGPLVAYFSAEYGFHSSLPIYSGGLGVLAGDHVKAASDLGLNLVGVGIFYHEGYFHQRLSPEGVQVEVYETLHPEELPLYPVQDREGRPLRVGVEFPGRTLWLSAYRVQVGAVPVYLLTANLPENTPEDRAITARLYAPGLEMRIQQELVLGLGGVRLLRALGLAPEVFHMNEGHSAFLGLERVRELVAEGHPFPVALELARAGALFTTHTPVPAGHDAFPLELVERYLGGFWERMGTDRETFLSLGLEEKPWGKVFSMSNLALRTSAQANGVSRLHGEVSREMFHHLWPGFLREEVPIGHVTNGVHTWTFLHPRLRRHYAEVFGPEWRKRPEDPETWKVEALGEEFWQIHKDLRAELVREVRTRLYEQRRRNGESPSRLREAEKVLDPEALTIGFARRFATYKRAVLLFKDPERLRRLLHGHYPIQFVFAGKAHPKDEPGKAYLQELFAKIREYGLEDRMVVLEDYDMYLARVLVHGSDVWLNTPRRPMEASGTSGMKAALNGALNLSVLDGWWAEAYNGKNGFAIGDERVYESEEAQDMADAQALYDVLEFEVLPLFYAKGPEGYSSGWLSMVHESLRTVGPRYSAARMVGDYLEIYRRGGAWAEAARAGQEALAAFHQALPALQGVTLRAQVPGDLTLNGVPMRVRAFLEGEVPEALRPFLEVQLVVRRSSGHLEVVPMRPGPDGYEVAYRPSRPGSYAYGVRLALRHPITGHVAWVRWA
SEQUENCE LISTING
<110> BONUMOSE, INC.
<120> ENZYMATIC PRODUCTION OF ALLULOSE
<130> 146.0014-WO00
<150> 63/026,294
<151> 2020-05-18
<160> 16
<170> PatentIn version 3.5
<210> 1
<211> 225
<212> PRT
<213> Thermoanaerobacterium thermosaccharolyticum
<400> 1
Met Lys Pro Met Phe Ala Pro Ser Leu Met Cys Ala Asn Phe Leu Asp
1 5 10 15
Leu Lys Asn Gln Ile Glu Ile Leu Asn Glu Arg Ala Asp Ile Tyr His
20 25 30
Ile Asp Ile Met Asp Gly His Tyr Val Lys Asn Phe Ala Leu Ser Pro
35 40 45
Tyr Leu Met Glu Gln Leu Lys Thr Ile Ala Lys Ile Pro Met Asp Ala
50 55 60
His Leu Met Val Glu Asn Pro Ala Asp Phe Leu Glu Cys Ile Ala Lys
65 70 75 80
Ser Gly Ala Thr Tyr Ile Ser Pro His Ala Glu Thr Ile Asn Lys Asp
85 90 95
Ala Phe Arg Ile Met Arg Thr Ile Lys Ala Leu Gly Cys Lys Thr Gly
100 105 110
Ile Val Leu Asn Pro Ala Thr Pro Val Glu Tyr Ile Lys Tyr Tyr Ile
115 120 125
Gly Met Leu Asp Lys Ile Thr Ile Leu Thr Val Asp Ala Gly Phe Ala
130 135 140
Gly Gln Thr Phe Ile Asn Glu Met Leu Asp Lys Ile Ala Glu Ile Lys
145 150 155 160
Ser Leu Arg Asp Gln Asn Gly Tyr Ser Tyr Leu Ile Glu Val Asp Gly
165 170 175
Ser Cys Asn Glu Lys Thr Phe Lys Gln Leu Ala Glu Ala Gly Thr Asp
180 185 190
Val Phe Val Val Gly Ser Ser Gly Leu Phe Asn Leu Asp Thr Asp Leu
195 200 205
Lys Val Ala Trp Asp Lys Met Met Asp Thr Phe Thr Arg Cys Thr Ser
210 215 220
Asn
225
<210> 2
<211> 220
<212> PRT
<213> Methanosarcina thermophila
<400> 2
Met Leu Lys Ala Leu Ile Phe Asp Met Asp Gly Val Leu Val Asp Ser
1 5 10 15
Met Pro Phe His Ala Ala Ala Trp Lys Lys Ala Phe Phe Glu Met Gly
20 25 30
Met Glu Ile Gln Asp Ser Asp Ile Phe Ala Ile Glu Gly Ser Asn Pro
35 40 45
Arg Asn Gly Leu Pro Leu Leu Ile Arg Lys Ala Arg Lys Glu Pro Glu
50 55 60
Ala Phe Asp Phe Glu Ala Ile Thr Ser Ile Tyr Arg Gln Glu Phe Lys
65 70 75 80
Arg Val Phe Glu Pro Lys Ala Phe Glu Gly Met Lys Glu Cys Leu Glu
85 90 95
Val Leu Lys Lys Arg Phe Leu Leu Ser Val Val Ser Gly Ser Asp His
100 105 110
Val Ile Val His Ser Ile Ile Asn Arg Leu Phe Pro Gly Ile Phe Asp
115 120 125
Ile Val Val Thr Gly Asp Asp Ile Ile Asn Ser Lys Pro His Pro Asp
130 135 140
Pro Phe Leu Lys Ala Val Glu Leu Leu Asn Val Arg Arg Glu Glu Cys
145 150 155 160
Val Val Ile Glu Asn Ala Ile Leu Gly Val Glu Ala Ala Lys Asn Ala
165 170 175
Arg Ile Tyr Cys Ile Gly Val Pro Thr Tyr Val Glu Pro Ser His Leu
180 185 190
Asp Lys Ala Asp Leu Val Val Glu Asp His Arg Gln Leu Met Gln His
195 200 205
Leu Leu Ser Leu Glu Pro Ala Asn Gly Phe Arg Gln
210 215 220
<210> 3
<211> 221
<212> PRT
<213> Thermoanaerobacterium thermosaccharolyticum
<400> 3
Met Lys Tyr Leu Phe Ser Pro Ser Leu Met Cys Met Asn Leu Ile Lys
1 5 10 15
Leu Asn Glu Gln Ile Ser Val Leu Asn Ser Lys Ala Asp Phe Leu His
20 25 30
Val Asp Ile Met Asp Gly His Phe Val Lys Asn Ile Thr Leu Ser Pro
35 40 45
Phe Phe Ile Glu Gln Ile Lys Ser Tyr Val Asn Ile Pro Ile Asp Ala
50 55 60
His Leu Met Val Glu Asn Pro Gly Asp Tyr Ile Glu Ile Cys Glu Lys
65 70 75 80
Ser Gly Ala Ser Phe Ile Thr Ile His Ala Glu Thr Ile Asn Arg Glu
85 90 95
Ala Phe Arg Ile Ile Asp Arg Ile Lys Ser His Gly Leu Met Val Gly
100 105 110
Ile Ala Leu Asn Pro Ala Thr Pro Ile Ser Glu Ile Lys His Tyr Ile
115 120 125
Asn Lys Ile Asp Lys Ile Thr Ile Met Thr Val Asp Pro Gly Phe Ala
130 135 140
Gly Gln Pro Phe Ile Pro Glu Val Leu Glu Lys Ile Arg Asp Leu Lys
145 150 155 160
Arg Leu Lys Asp Asp Asn Asn Tyr Asn Tyr Leu Ile Glu Ala Asp Gly
165 170 175
Ser Cys Asn Lys Asn Thr Phe Gln Val Leu Lys Asp Ala Gly Cys Lys
180 185 190
Val Phe Val Leu Gly Ser Ser Gly Leu Phe Asn Leu Ser Asp Asp Leu
195 200 205
Gly Lys Ala Trp Glu Ile Met Ile Gly Asn Phe Asn Gly
210 215 220
<210> 4
<211> 230
<212> PRT
<213> Bacillus thermoamylovorans
<400> 4
Met Ser Asn Lys Ile Glu Phe Ser Pro Ser Leu Met Thr Met Asp Leu
1 5 10 15
Asp Lys Phe Lys Glu Gln Ile Thr Phe Leu Asn Asn His Val Gly Ser
20 25 30
Tyr His Ile Asp Ile Met Asp Gly His Tyr Val Pro Asn Ile Thr Leu
35 40 45
Ser Pro Trp Phe Val Gln Glu Val Arg Lys Ile Ser Asp Val Pro Met
50 55 60
Ser Ala His Leu Met Val Thr Asn Pro Ser Phe Trp Val Gln Gln Leu
65 70 75 80
Ile Asp Ile Lys Cys Glu Trp Ile Cys Met His Val Glu Thr Leu Asp
85 90 95
Gly Leu Ala Phe Arg Leu Ile Asp Gln Ile His Asp Ala Gly Leu Lys
100 105 110
Ala Gly Val Val Leu Asn Pro Glu Thr Ser Val Asp Ala Ile Arg Pro
115 120 125
Tyr Ile Asp Leu Val Asp Lys Val Thr Ile Met Thr Val Asp Pro Gly
130 135 140
Phe Ala Gly Gln Arg Phe Ile Asp Ser Thr Leu Glu Lys Ile Val Glu
145 150 155 160
Leu Arg Lys Leu Arg Glu Glu His Gly Tyr Lys Tyr Val Ile Glu Met
165 170 175
Asp Gly Ser Ser Asn Arg Lys Ser Phe Lys Lys Ile Tyr Glu Ala Gly
180 185 190
Pro Asp Ile Tyr Ile Ile Gly Arg Ser Gly Leu Phe Gly Leu His Glu
195 200 205
Asp Ile Glu Lys Ala Trp Glu Ile Met Cys Lys Asp Phe Glu Glu Met
210 215 220
Thr Gly Glu Lys Val Leu
225 230
<210> 5
<211> 231
<212> PRT
<213> Escherichia coli
<400> 5
Met Lys Ile Ser Pro Ser Leu Met Cys Met Asp Leu Leu Lys Phe Lys
1 5 10 15
Glu Gln Ile Glu Phe Ile Asp Ser His Ala Asp Tyr Phe His Ile Asp
20 25 30
Ile Met Asp Gly His Phe Val Pro Asn Leu Thr Leu Ser Pro Phe Phe
35 40 45
Val Ser Gln Val Lys Lys Leu Ala Thr Lys Pro Leu Asp Cys His Leu
50 55 60
Met Val Thr Arg Pro Gln Asp Tyr Ile Ala Gln Leu Ala Arg Ala Gly
65 70 75 80
Ala Asp Phe Ile Thr Leu His Pro Glu Thr Ile Asn Gly Gln Ala Phe
85 90 95
Arg Leu Ile Asp Glu Ile Arg Arg His Asp Met Lys Val Gly Leu Ile
100 105 110
Leu Asn Pro Glu Thr Pro Val Glu Ala Met Lys Tyr Tyr Ile His Lys
115 120 125
Ala Asp Lys Ile Thr Val Met Thr Val Asp Pro Gly Phe Ala Gly Gln
130 135 140
Pro Phe Ile Pro Glu Met Leu Asp Lys Leu Ala Glu Leu Lys Ala Trp
145 150 155 160
Arg Glu Arg Glu Gly Leu Glu Tyr Glu Ile Glu Val Asp Gly Ser Cys
165 170 175
Asn Gln Ala Thr Tyr Glu Lys Leu Met Ala Ala Gly Ala Asp Val Phe
180 185 190
Ile Val Gly Thr Ser Gly Leu Phe Asn His Ala Glu Asn Ile Asp Glu
195 200 205
Ala Trp Arg Ile Met Thr Ala Gln Ile Leu Ala Ala Lys Ser Glu Val
210 215 220
Gln Pro His Ala Lys Thr Ala
225 230
<210> 6
<211> 223
<212> PRT
<213> Hydrogenivirga sp. 128-5-R1-1
<400> 6
Met Glu Lys Leu Leu Ala Pro Ser Ile Leu Ala Gly Asp Trp Trp Asn
1 5 10 15
Ile Gly Glu Gln Ile Glu Ala Thr Leu Arg Gly Gly Ala Asp Ile Ile
20 25 30
His Phe Asp Val Met Asp Gly His Phe Val Pro Asn Ile Thr Val Gly
35 40 45
Pro Glu Ile Leu Thr Ser Ile Ser Arg Arg Val Asn Val Pro Val Asp
50 55 60
Ala His Leu Met Ile Glu Asn Pro Asp Arg Tyr Ile Pro Ser Phe Val
65 70 75 80
Glu Ala Gly Ala Lys Trp Ile Ser Val His Ile Glu Asn Val Pro His
85 90 95
Ile His Arg Thr Leu Thr Leu Ile Arg Glu Leu Gly Ala Lys Ala Gly
100 105 110
Val Val Leu Asn Pro Gly Thr Pro Leu Ser Ala Val Glu Glu Ala Ile
115 120 125
His Tyr Ala Asp Tyr Val Leu Leu Met Ser Val Asn Pro Gly Phe Ser
130 135 140
Gly Gln Arg Phe Ile Glu Arg Ser Leu Glu Arg Leu Ser Leu Leu Arg
145 150 155 160
Asp Met Arg Asp Arg Leu Asn Pro Asp Cys Leu Ile Glu Val Asp Gly
165 170 175
Gly Val Lys Glu Asp Asn Val Val Glu Val Val Arg Ala Gly Ala Asp
180 185 190
Val Val Val Val Gly Ser Gly Ile Phe Ser Ala Lys Asp Val Glu Ala
195 200 205
Gln Thr Arg Lys Leu Lys Asp Leu Ile Ser Ser Ala Val Ala Val
210 215 220
<210> 7
<211> 228
<212> PRT
<213> Brevibacillus thermoruber
<400> 7
Met Gly Phe Lys Phe Ser Pro Ser Leu Met Cys Met Asn Leu Leu Asp
1 5 10 15
Ile Gln His Gln Ile Glu Val Met Asn Arg Arg Ala Asp Leu Val His
20 25 30
Ile Asp Ile Met Asp Gly His Tyr Val Lys Asn Leu Thr Leu Ser Pro
35 40 45
Phe Phe Ile Glu Gln Leu Lys Glu Ser Leu His Val Pro Met Asp Val
50 55 60
His Leu Met Val Glu Asn Pro Thr Asp Phe Ile Glu Arg Val Lys Glu
65 70 75 80
Ala Gly Ala Ser Ile Ile Ser Pro His Ala Glu Thr Ile Asn Thr Asp
85 90 95
Ala Phe Arg Ile Ile Asp Lys Val Lys Ser Leu Gly Cys Gln Met Gly
100 105 110
Ile Val Leu Asn Pro Ala Thr Pro Ile Ala Tyr Ile Gln His Tyr Ile
115 120 125
His Leu Val Asp Lys Ile Thr Ile Met Thr Val Asp Pro Gly Tyr Ala
130 135 140
Gly Gln Lys Phe Ile Pro Glu Met Leu Glu Lys Ile Arg Gln Ala Lys
145 150 155 160
Arg Leu Lys Glu Glu Arg Gly Tyr Arg Tyr Leu Ile Glu Val Asp Gly
165 170 175
Ser Cys Asn Val Gly Thr Phe Lys Arg Leu Ala Glu Ala Gly Ala Glu
180 185 190
Val Phe Ile Val Gly Ser Ser Gly Leu Phe Asn Leu His Pro Asp Leu
195 200 205
Glu Val Ala Trp Asp Met Met Met Asp Asn Phe Gln Arg Glu Val Gly
210 215 220
Glu Thr Thr Ala
225
<210> 8
<211> 225
<212> PRT
<213> Clostridium sp. DL-VIII
<400> 8
Met Lys Pro Met Phe Ala Pro Ser Leu Met Cys Ala Asn Phe Leu Asp
1 5 10 15
Leu Lys Asn Gln Ile Glu Ile Leu Asn Glu Arg Ala Asp Ile Phe His
20 25 30
Val Asp Ile Met Asp Gly His Tyr Val Lys Asn Phe Ser Leu Ser Pro
35 40 45
Ala Met Met Glu Gln Leu Lys Thr Ile Thr Lys Ile Pro Met Asp Ala
50 55 60
His Leu Met Val Glu Asn Pro Ala Asp Phe Leu Glu Gly Ile Ala Lys
65 70 75 80
Ala Gly Ala Thr Tyr Ile Ser Pro His Ala Glu Thr Ile Asn Lys Asp
85 90 95
Ala Phe Arg Ile Met Arg Thr Ile Lys Ala Leu Gly Cys Lys Thr Gly
100 105 110
Val Val Leu Asn Pro Ala Thr Pro Val Glu Tyr Ile Lys His Tyr Leu
115 120 125
Gly Met Leu Asp Lys Ile Thr Ile Leu Thr Val Asp Ala Gly Phe Ala
130 135 140
Gly Gln Thr Phe Ile Glu Glu Met Leu Asp Lys Ile Glu Glu Val Lys
145 150 155 160
Arg Leu Arg Glu Glu Asn Gly Tyr Ser Tyr Leu Ile Glu Val Asp Gly
165 170 175
Ser Cys Asn Glu Lys Thr Phe Lys Lys Leu Ala Glu Ala Gly Thr Glu
180 185 190
Val Phe Ile Val Gly Ser Ser Gly Leu Phe Asn Leu Asp Ala Asp Leu
195 200 205
Lys Val Ser Trp Asp Lys Met Met Asn Met Phe Asn Lys Cys Ile Asn
210 215 220
Asn
225
<210> 9
<211> 228
<212> PRT
<213> Bacillus alcalophilus
<400> 9
Met Tyr Lys Phe Ser Pro Ser Leu Met Cys Met Asp Leu Ser Arg Phe
1 5 10 15
Lys Glu Gln Val Glu Val Leu Asn Asp Lys Ala Asp Phe Tyr His Val
20 25 30
Asp Ile Met Asp Gly His Phe Val Lys Asn Ile Thr Leu Ser Pro Phe
35 40 45
Phe Ile Gln Glu Leu Lys Lys Ile Thr Asp Val Pro Ile Asp Ala His
50 55 60
Leu Met Val Thr Asn Pro Ala Asp Phe Val Glu Met Thr Ile Asp Ala
65 70 75 80
Gly Ala Asp Tyr Ile Ser Leu His Ala Glu Thr Ile Asn Gly Asn Ala
85 90 95
Phe Arg Leu Ile Asn Gln Ile Lys Glu Lys Gly Lys Lys Phe Gly Val
100 105 110
Val Leu Asn Pro Ala Thr Pro Leu Glu Ser Ile Arg His Tyr Ile Gln
115 120 125
His Val Asp Lys Leu Thr Ile Met Thr Val Asp Pro Gly Phe Ala Gly
130 135 140
Gln Lys Phe Val Glu Glu Met Ile Gly Lys Ile Lys Glu Ala Lys Glu
145 150 155 160
Leu Lys Glu Arg Asn Gly Tyr Lys Tyr Leu Ile Thr Ile Asp Gly Ser
165 170 175
Cys Asn Lys Asn Thr Phe Lys Lys Leu Val Glu Ala Gly Ala Glu Val
180 185 190
Leu Ile Val Gly Ser Ser Gly Leu Phe Gly Leu Asp Glu Asp Val Asn
195 200 205
Ile Ala Trp Asp Lys Met Met Asp Thr Phe His Leu Glu Val Lys Asp
210 215 220
Ile Ser Gln Val
225
<210> 10
<211> 217
<212> PRT
<213> Hungateiclostridium thermocellum
<400> 10
Met Ile Lys Tyr Lys Ala Val Phe Phe Asp Phe Asp Tyr Thr Leu Ala
1 5 10 15
Asp Ser Ser Lys Ala Val Ile Glu Cys Ile Asn Tyr Ala Leu Gln Lys
20 25 30
Met Gly Tyr Pro Glu Ser Ser Pro Glu Ser Ile Cys Arg Thr Ile Gly
35 40 45
Leu Thr Leu Ala Glu Ala Phe Lys Ile Leu Ser Gly Asp Thr Ser Asp
50 55 60
Ser Asn Ala Asp Leu Phe Arg Gln Tyr Phe Lys Glu Arg Ala Asp Leu
65 70 75 80
Val Met Cys Asp Arg Thr Val Met Tyr Ser Thr Val Glu Cys Val Leu
85 90 95
Lys Lys Leu Lys Lys Ala Asp Val Lys Thr Gly Ile Val Ser Thr Lys
100 105 110
Tyr Arg Tyr Arg Ile Glu Asp Ile Leu Lys Arg Asp Lys Leu Leu Gln
115 120 125
Tyr Phe Asp Val Ile Val Gly Gly Glu Asp Val Ala Ala His Lys Pro
130 135 140
Asp Pro Glu Gly Leu Leu Lys Ala Ile Ser Met Val Gly Cys Gln Lys
145 150 155 160
Glu Glu Val Leu Phe Val Gly Asp Ser Thr Val Asp Ala Arg Thr Ala
165 170 175
Lys Asn Ala Gly Val Asp Phe Val Ala Val Leu Thr Gly Thr Thr Gly
180 185 190
Ala Asn Glu Phe Ser Glu Tyr Asn Pro Gly Ala Val Ile Glu Asp Leu
195 200 205
Ser Gly Leu Leu Asp Met Phe Met Leu
210 215
<210> 11
<211> 222
<212> PRT
<213> Bacteroides fragilis
<400> 11
Met Lys Tyr Thr Val Tyr Leu Phe Asp Phe Asp Tyr Thr Leu Ala Asp
1 5 10 15
Ser Ser Arg Gly Ile Val Thr Cys Phe Arg Ser Val Leu Glu Arg His
20 25 30
Gly Tyr Thr Gly Ile Thr Asp Asp Met Ile Lys Arg Thr Ile Gly Lys
35 40 45
Thr Leu Glu Glu Ser Phe Ser Ile Leu Thr Gly Ile Thr Asp Ala Asp
50 55 60
Gln Leu Glu Ser Phe Arg Gln Glu Tyr Ser Lys Glu Ala Asp Ile Tyr
65 70 75 80
Met Asn Ala Asn Thr Ile Leu Phe Pro Asp Thr Leu Pro Thr Leu Thr
85 90 95
His Leu Lys Lys Gln Gly Ile Arg Ile Gly Ile Ile Ser Thr Lys Tyr
100 105 110
Arg Phe Arg Ile Leu Ser Phe Leu Arg Asn His Met Pro Asp Asp Trp
115 120 125
Phe Asp Ile Ile Ile Gly Gly Glu Asp Val Thr His His Lys Pro Asp
130 135 140
Pro Glu Gly Leu Leu Leu Ala Ile Asp Arg Leu Lys Ala Cys Pro Glu
145 150 155 160
Glu Val Leu Tyr Ile Gly Asp Ser Thr Val Asp Ala Gly Thr Ala Ala
165 170 175
Ala Ala Gly Val Ser Phe Thr Gly Val Thr Ser Gly Met Thr Thr Ala
180 185 190
Gln Glu Phe Gln Ala Tyr Pro Tyr Asp Arg Ile Ile Ser Thr Leu Gly
195 200 205
Gln Leu Ile Ser Val Pro Glu Asp Lys Ser Gly Cys Pro Leu
210 215 220
<210> 12
<211> 213
<212> PRT
<213> Bacteroides thetaiotaomicron
<400> 12
Met Asn Tyr Lys Thr Tyr Leu Phe Asp Phe Asp Tyr Thr Leu Ala Asp
1 5 10 15
Ser Ser Arg Gly Ile Val Thr Cys Phe Arg Asn Val Leu Asn Arg His
20 25 30
Gln Tyr Thr Asn Val Thr Asp Glu Ala Ile Lys Arg Thr Ile Gly Lys
35 40 45
Thr Leu Glu Glu Ser Phe Ser Ile Leu Thr Gly Val Thr Asp Trp Glu
50 55 60
Gln Leu Thr Ala Phe Arg Gln Glu Tyr Arg Leu Glu Ala Asp Val His
65 70 75 80
Met Asn Val Asn Thr Arg Leu Phe Pro Asp Thr Leu Ser Thr Leu Lys
85 90 95
Glu Leu Lys Glu Arg Gly Ala Arg Ile Gly Ile Ile Ser Thr Lys Tyr
100 105 110
Arg Phe Arg Ile Leu Ser Phe Leu Asp Glu Tyr Leu Pro Glu Asn Phe
115 120 125
Leu Asp Ile Val Val Gly Gly Glu Asp Val Gln Ala Ala Lys Pro Ser
130 135 140
Pro Glu Gly Ile Lys Phe Ala Leu Glu His Leu Gly Arg Thr Pro Gln
145 150 155 160
Glu Thr Leu Tyr Ile Gly Asp Ser Thr Val Asp Ala Glu Thr Ala Gln
165 170 175
Asn Ala Gly Val Asp Phe Ala Gly Val Leu Asn Gly Met Thr Thr Ala
180 185 190
Asp Glu Leu Arg Ala Tyr Pro His Arg Phe Ile Met Glu Asn Leu Ser
195 200 205
Gly Leu Leu Tyr Ile
210
<210> 13
<211> 581
<212> PRT
<213> Caldibacillus debilis
<400> 13
Met Glu Trp Lys Gln Arg Ala Glu Arg Trp Leu Arg Phe Glu Asn Leu
1 5 10 15
Asp Pro Glu Leu Lys Lys Gln Leu Glu Glu Met Ala Lys Asp Glu Lys
20 25 30
Lys Leu Glu Asp Leu Phe Tyr Lys Tyr Leu Glu Phe Gly Thr Gly Gly
35 40 45
Met Arg Gly Glu Ile Gly Pro Gly Thr Asn Arg Ile Asn Ile Tyr Thr
50 55 60
Val Arg Lys Ala Ser Glu Gly Leu Ala Arg Phe Leu Leu Ala Ser Gly
65 70 75 80
Gly Glu Glu Lys Ala Lys Gln Gly Val Val Ile Ala Tyr Asp Ser Arg
85 90 95
Arg Lys Ser Arg Glu Phe Ala Leu Glu Thr Ala Lys Thr Val Gly Lys
100 105 110
His Gly Ile Lys Ala Tyr Val Phe Glu Ser Leu Arg Pro Thr Pro Glu
115 120 125
Leu Ser Phe Ala Val Arg Tyr Leu His Ala Ala Ala Gly Val Val Ile
130 135 140
Thr Ala Ser His Asn Pro Pro Glu Tyr Asn Gly Tyr Lys Val Tyr Gly
145 150 155 160
Glu Asp Gly Gly Gln Leu Thr Pro Lys Ala Ala Asp Glu Leu Ile Arg
165 170 175
Tyr Val Tyr Glu Val Glu Asp Glu Leu Ser Leu Thr Val Pro Gly Glu
180 185 190
Gln Glu Leu Ile Asp Arg Gly Leu Leu Gln Tyr Ile Gly Glu Asn Ile
195 200 205
Asp Leu Ala Tyr Ile Glu Lys Leu Lys Thr Ile Gln Leu Asn Arg Asp
210 215 220
Val Ile Leu Asn Gly Gly Lys Asp Leu Lys Ile Val Phe Thr Pro Leu
225 230 235 240
His Gly Thr Ala Gly Gln Leu Val Gln Thr Gly Leu Arg Glu Phe Gly
245 250 255
Phe Gln Asn Val Tyr Val Val Lys Glu Gln Glu Gln Pro Asp Pro Asp
260 265 270
Phe Ser Thr Val Lys Ser Pro Asn Pro Glu Glu His Glu Ala Phe Glu
275 280 285
Ile Ala Ile Arg Tyr Gly Lys Lys Tyr Asp Ala Asp Leu Ile Met Gly
290 295 300
Thr Asp Pro Asp Ser Asp Arg Leu Gly Ile Val Val Lys Asn Gly Gln
305 310 315 320
Gly Asp Tyr Val Val Leu Thr Gly Asn Gln Thr Gly Ala Ile Leu Leu
325 330 335
Tyr Tyr Leu Leu Ser Gln Lys Lys Glu Lys Gly Met Leu Val Arg Asn
340 345 350
Ser Ala Val Leu Lys Thr Ile Val Thr Ser Glu Leu Gly Arg Ala Ile
355 360 365
Ala Ser Asp Phe Gly Val Glu Thr Ile Asp Thr Leu Thr Gly Phe Lys
370 375 380
Phe Ile Gly Glu Lys Ile Lys Glu Phe Lys Glu Thr Gly Ser His Val
385 390 395 400
Phe Gln Phe Gly Tyr Glu Glu Ser Tyr Gly Tyr Leu Ile Gly Asp Phe
405 410 415
Val Arg Asp Lys Asp Ala Ile Gln Ala Ala Leu Phe Ala Ala Glu Ala
420 425 430
Ala Ala Tyr Tyr Lys Ala Gln Gly Lys Ser Leu Tyr Asp Val Leu Met
435 440 445
Glu Ile Tyr Lys Lys Tyr Gly Phe Tyr Lys Glu Ser Leu Arg Ser Ile
450 455 460
Thr Leu Lys Gly Lys Asp Gly Ala Glu Lys Ile Arg Ala Ile Met Asp
465 470 475 480
Ala Phe Arg Gln Asn Pro Pro Glu Glu Val Ser Gly Ile Pro Val Ala
485 490 495
Ile Thr Glu Asp Tyr Leu Thr Gln Lys Arg Val Asp Lys Ala Ala Gly
500 505 510
Gln Thr Thr Pro Ile His Leu Pro Lys Ser Asn Val Leu Lys Tyr Tyr
515 520 525
Leu Ala Asp Glu Ser Trp Phe Cys Ile Arg Pro Ser Gly Thr Glu Pro
530 535 540
Lys Cys Lys Phe Tyr Phe Ala Val Arg Gly Asp Ser Glu Ala Gln Ser
545 550 555 560
Glu Ala Arg Leu Arg Gln Leu Glu Thr Asn Val Met Ala Met Val Glu
565 570 575
Lys Ile Leu Gln Lys
580
<210> 14
<211> 415
<212> PRT
<213> Thermus thermophilus
<400> 14
Met Leu Arg Leu Asp Thr Arg Phe Leu Pro Gly Phe Pro Glu Ala Leu
1 5 10 15
Ser Arg His Gly Pro Leu Leu Glu Glu Ala Arg Arg Arg Leu Leu Ala
20 25 30
Lys Arg Gly Glu Pro Gly Ser Met Leu Gly Trp Met Asp Leu Pro Glu
35 40 45
Asp Thr Glu Thr Leu Arg Glu Val Arg Arg Tyr Arg Glu Ala Asn Pro
50 55 60
Trp Val Glu Asp Phe Val Leu Ile Gly Ile Gly Gly Ser Ala Leu Gly
65 70 75 80
Pro Lys Ala Leu Glu Ala Ala Phe Asn Glu Ser Gly Val Arg Phe His
85 90 95
Tyr Leu Asp His Val Glu Pro Glu Pro Ile Leu Arg Leu Leu Arg Thr
100 105 110
Leu Asp Pro Arg Lys Thr Leu Val Asn Ala Val Ser Lys Ser Gly Ser
115 120 125
Thr Ala Glu Thr Leu Ala Gly Leu Ala Val Phe Leu Lys Trp Leu Lys
130 135 140
Ala His Leu Gly Glu Asp Trp Arg Arg His Leu Val Val Thr Thr Asp
145 150 155 160
Pro Lys Glu Gly Pro Leu Arg Ala Phe Ala Glu Arg Glu Gly Leu Lys
165 170 175
Ala Phe Ala Ile Pro Lys Glu Val Gly Gly Arg Phe Ser Ala Leu Ser
180 185 190
Pro Val Gly Leu Leu Pro Leu Ala Phe Ala Gly Ala Asp Leu Asp Ala
195 200 205
Leu Leu Met Gly Ala Arg Lys Ala Asn Glu Thr Ala Leu Ala Pro Leu
210 215 220
Glu Glu Ser Leu Pro Leu Lys Thr Ala Leu Leu Leu His Leu His Arg
225 230 235 240
His Leu Pro Val His Val Phe Met Val Tyr Ser Glu Arg Leu Ser His
245 250 255
Leu Pro Ser Trp Phe Val Gln Leu His Asp Glu Ser Leu Gly Lys Val
260 265 270
Asp Arg Gln Gly Gln Arg Val Gly Thr Thr Ala Val Pro Ala Leu Gly
275 280 285
Pro Lys Asp Gln His Ala Gln Val Gln Leu Phe Arg Glu Gly Pro Leu
290 295 300
Asp Lys Leu Leu Ala Leu Val Ile Pro Glu Ala Pro Leu Glu Asp Val
305 310 315 320
Glu Ile Pro Glu Val Glu Gly Leu Glu Ala Ala Ser Tyr Leu Phe Gly
325 330 335
Lys Thr Leu Phe Gln Leu Leu Lys Ala Glu Ala Glu Ala Thr Tyr Glu
340 345 350
Ala Leu Ala Glu Ala Gly Gln Arg Val Tyr Ala Leu Phe Leu Pro Glu
355 360 365
Val Ser Pro Tyr Ala Val Gly Trp Leu Met Gln His Leu Met Trp Gln
370 375 380
Thr Ala Phe Leu Gly Glu Leu Trp Glu Val Asn Ala Phe Asp Gln Pro
385 390 395 400
Gly Val Glu Leu Gly Lys Val Leu Thr Arg Lys Arg Leu Ala Gly
405 410 415
<210> 15
<211> 511
<212> PRT
<213> Anaerolinea thermophila
<400> 15
Met Ser Leu Phe Lys Arg Ala Ser Gly Ile Leu Leu His Pro Thr Ser
1 5 10 15
Leu Pro Gly Pro Asp Gly Ile Gly Asp Leu Gly Pro Glu Ala Tyr Arg
20 25 30
Trp Val Asn Phe Leu Ala Glu Ser Gly Cys Ser Leu Trp Gln Ile Leu
35 40 45
Pro Leu Gly Pro Thr Gly Phe Gly Asp Ser Pro Tyr Gln Cys Phe Ser
50 55 60
Ala Phe Ala Gly Asn Pro Tyr Leu Val Ser Pro Ala Leu Leu Leu Asp
65 70 75 80
Glu Gly Leu Leu Thr Ser Glu Asp Leu Ala Asp Arg Pro Glu Phe Pro
85 90 95
Ala Ser Arg Val Asp Tyr Gly Pro Val Ile Gln Trp Lys Leu Thr Leu
100 105 110
Leu Asp Arg Ala Tyr Val Arg Phe Lys Arg Ser Thr Ser Gln Lys Arg
115 120 125
Lys Ala Ala Phe Glu Ala Phe Lys Glu Glu Gln Arg Ala Trp Leu Leu
130 135 140
Asp Phe Ser Leu Phe Met Ala Ile Lys Glu Ala His Gly Gly Ala Ser
145 150 155 160
Trp Asp Tyr Trp Pro Glu Pro Leu Arg Lys Arg Asp Pro Glu Ala Leu
165 170 175
Asn Ala Phe His Arg Ala His Glu Val Asp Val Glu Arg His Ser Phe
180 185 190
Arg Gln Phe Leu Phe Phe Arg Gln Trp Gln Ala Leu Arg Gln Tyr Ala
195 200 205
His Glu Lys Gly Val Gln Ile Ile Gly Asp Val Pro Ile Phe Val Ala
210 215 220
Tyr Asp Ser Ala Asp Val Trp Ser His Pro Asp Leu Phe Tyr Leu Asp
225 230 235 240
Glu Thr Gly Lys Pro Thr Val Val Ala Gly Val Pro Pro Asp Tyr Phe
245 250 255
Ser Ala Thr Gly Gln Leu Trp Gly Asn Pro Leu Tyr Arg Trp Asp Tyr
260 265 270
His Arg Glu Thr Gly Phe Ala Trp Trp Leu Glu Arg Leu Lys Ala Thr
275 280 285
Phe Ala Met Val Asp Ile Val Arg Leu Asp His Phe Arg Gly Phe Ala
290 295 300
Gly Tyr Trp Glu Val Pro Tyr Gly Met Pro Thr Ala Glu Lys Gly Arg
305 310 315 320
Trp Val Pro Gly Pro Gly Ile Ala Leu Phe Glu Ala Ile Arg Asn Ala
325 330 335
Leu Gly Gly Leu Pro Ile Ile Ala Glu Asp Leu Gly Glu Ile Thr Pro
340 345 350
Asp Val Ile Glu Leu Arg Glu Gln Leu Gly Leu Pro Gly Met Lys Ile
355 360 365
Phe Gln Phe Ala Phe Ala Ser Asp Ala Asp Asp Pro Phe Leu Pro His
370 375 380
Asn Tyr Val Gln Asn Cys Val Ala Tyr Thr Gly Thr His Asp Asn Asp
385 390 395 400
Thr Ala Ile Gly Trp Tyr Asn Ser Ala Pro Glu Lys Glu Arg Asp Phe
405 410 415
Val Arg Arg Tyr Leu Ala Arg Ser Gly Glu Asp Ile Ala Trp Asp Met
420 425 430
Ile Arg Ala Val Trp Ser Ser Val Ala Met Phe Ala Ile Ala Pro Leu
435 440 445
Gln Asp Phe Leu Lys Leu Gly Pro Glu Ala Arg Met Asn Tyr Pro Gly
450 455 460
Arg Pro Ala Gly Asn Trp Gly Trp Arg Tyr Glu Ala Phe Met Leu Asp
465 470 475 480
Asp Gly Leu Lys Asn Arg Ile Lys Glu Ile Asn Tyr Leu Tyr Gly Arg
485 490 495
Leu Pro Glu His Met Lys Pro Pro Lys Val Val Lys Lys Trp Thr
500 505 510
<210> 16
<211> 809
<212> PRT
<213> Thermus sp. CCB_US3_UF1
<400> 16
Met Pro Leu Leu Pro Glu Pro Leu Ser Gly Leu Lys Glu Leu Ala Tyr
1 5 10 15
Asn Leu Trp Trp Ser Trp Asn Pro Glu Ala Ala Glu Leu Phe Gln Glu
20 25 30
Ile Asp Pro Ser Leu Trp Lys Arg Phe Arg Gly Asn Pro Val Lys Leu
35 40 45
Leu Leu Glu Ala Asp Pro Gly Arg Leu Glu Gly Leu Ala Ala Thr Ser
50 55 60
Tyr Pro Ala Arg Val Gly Ala Val Val Glu Ala Leu Arg Ala Tyr Leu
65 70 75 80
Arg Glu Arg Glu Glu Lys Gln Gly Pro Leu Val Ala Tyr Phe Ser Ala
85 90 95
Glu Tyr Gly Phe His Ser Ser Leu Pro Ile Tyr Ser Gly Gly Leu Gly
100 105 110
Val Leu Ala Gly Asp His Val Lys Ala Ala Ser Asp Leu Gly Leu Asn
115 120 125
Leu Val Gly Val Gly Ile Phe Tyr His Glu Gly Tyr Phe His Gln Arg
130 135 140
Leu Ser Pro Glu Gly Val Gln Val Glu Val Tyr Glu Thr Leu His Pro
145 150 155 160
Glu Glu Leu Pro Leu Tyr Pro Val Gln Asp Arg Glu Gly Arg Pro Leu
165 170 175
Arg Val Gly Val Glu Phe Pro Gly Arg Thr Leu Trp Leu Ser Ala Tyr
180 185 190
Arg Val Gln Val Gly Ala Val Pro Val Tyr Leu Leu Thr Ala Asn Leu
195 200 205
Pro Glu Asn Thr Pro Glu Asp Arg Ala Ile Thr Ala Arg Leu Tyr Ala
210 215 220
Pro Gly Leu Glu Met Arg Ile Gln Gln Glu Leu Val Leu Gly Leu Gly
225 230 235 240
Gly Val Arg Leu Leu Arg Ala Leu Gly Leu Ala Pro Glu Val Phe His
245 250 255
Met Asn Glu Gly His Ser Ala Phe Leu Gly Leu Glu Arg Val Arg Glu
260 265 270
Leu Val Ala Glu Gly His Pro Phe Pro Val Ala Leu Glu Leu Ala Arg
275 280 285
Ala Gly Ala Leu Phe Thr Thr His Thr Pro Val Pro Ala Gly His Asp
290 295 300
Ala Phe Pro Leu Glu Leu Val Glu Arg Tyr Leu Gly Gly Phe Trp Glu
305 310 315 320
Arg Met Gly Thr Asp Arg Glu Thr Phe Leu Ser Leu Gly Leu Glu Glu
325 330 335
Lys Pro Trp Gly Lys Val Phe Ser Met Ser Asn Leu Ala Leu Arg Thr
340 345 350
Ser Ala Gln Ala Asn Gly Val Ser Arg Leu His Gly Glu Val Ser Arg
355 360 365
Glu Met Phe His His Leu Trp Pro Gly Phe Leu Arg Glu Glu Val Pro
370 375 380
Ile Gly His Val Thr Asn Gly Val His Thr Trp Thr Phe Leu His Pro
385 390 395 400
Arg Leu Arg Arg His Tyr Ala Glu Val Phe Gly Pro Glu Trp Arg Lys
405 410 415
Arg Pro Glu Asp Pro Glu Thr Trp Lys Val Glu Ala Leu Gly Glu Glu
420 425 430
Phe Trp Gln Ile His Lys Asp Leu Arg Ala Glu Leu Val Arg Glu Val
435 440 445
Arg Thr Arg Leu Tyr Glu Gln Arg Arg Arg Asn Gly Glu Ser Pro Ser
450 455 460
Arg Leu Arg Glu Ala Glu Lys Val Leu Asp Pro Glu Ala Leu Thr Ile
465 470 475 480
Gly Phe Ala Arg Arg Phe Ala Thr Tyr Lys Arg Ala Val Leu Leu Phe
485 490 495
Lys Asp Pro Glu Arg Leu Arg Arg Leu Leu His Gly His Tyr Pro Ile
500 505 510
Gln Phe Val Phe Ala Gly Lys Ala His Pro Lys Asp Glu Pro Gly Lys
515 520 525
Ala Tyr Leu Gln Glu Leu Phe Ala Lys Ile Arg Glu Tyr Gly Leu Glu
530 535 540
Asp Arg Met Val Val Leu Glu Asp Tyr Asp Met Tyr Leu Ala Arg Val
545 550 555 560
Leu Val His Gly Ser Asp Val Trp Leu Asn Thr Pro Arg Arg Pro Met
565 570 575
Glu Ala Ser Gly Thr Ser Gly Met Lys Ala Ala Leu Asn Gly Ala Leu
580 585 590
Asn Leu Ser Val Leu Asp Gly Trp Trp Ala Glu Ala Tyr Asn Gly Lys
595 600 605
Asn Gly Phe Ala Ile Gly Asp Glu Arg Val Tyr Glu Ser Glu Glu Ala
610 615 620
Gln Asp Met Ala Asp Ala Gln Ala Leu Tyr Asp Val Leu Glu Phe Glu
625 630 635 640
Val Leu Pro Leu Phe Tyr Ala Lys Gly Pro Glu Gly Tyr Ser Ser Gly
645 650 655
Trp Leu Ser Met Val His Glu Ser Leu Arg Thr Val Gly Pro Arg Tyr
660 665 670
Ser Ala Ala Arg Met Val Gly Asp Tyr Leu Glu Ile Tyr Arg Arg Gly
675 680 685
Gly Ala Trp Ala Glu Ala Ala Arg Ala Gly Gln Glu Ala Leu Ala Ala
690 695 700
Phe His Gln Ala Leu Pro Ala Leu Gln Gly Val Thr Leu Arg Ala Gln
705 710 715 720
Val Pro Gly Asp Leu Thr Leu Asn Gly Val Pro Met Arg Val Arg Ala
725 730 735
Phe Leu Glu Gly Glu Val Pro Glu Ala Leu Arg Pro Phe Leu Glu Val
740 745 750
Gln Leu Val Val Arg Arg Ser Ser Gly His Leu Glu Val Val Pro Met
755 760 765
Arg Pro Gly Pro Asp Gly Tyr Glu Val Ala Tyr Arg Pro Ser Arg Pro
770 775 780
Gly Ser Tyr Ala Tyr Gly Val Arg Leu Ala Leu Arg His Pro Ile Thr
785 790 795 800
Gly His Val Ala Trp Val Arg Trp Ala
805
Claims (23)
- 당류로부터의 알룰로스의 개선된 생산 공정으로서, 상기 개선은 알룰로스 6-인산염 에피머화효소(A6PE)를 사용하여 과당-6-인산염(F6P)를 알룰로스 6-인산염(A6P)으로 전환시키는 단계를 포함하며, 상기 A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하는, 공정.
- 당류로부터 알룰로스의 개선된 생산 공정으로서, 상기 개선은 알룰로스-6-인산염 인산가수분해효소(A6PP)를 사용하여 A6P를 알룰로스로 전환시키는 단계를 포함하며, 상기 A6PP는 서열 번호: 2에 대해 적어도 90% 서열 동일성을 갖는 아미노산 서열을 포함하는, 공정.
- 제2항에 있어서, 알룰로스 6-인산염 에피머화효소(A6PE)를 사용하여 과당-6-인산염(F6P)을 알룰로스 6-인산염(A6P)으로 전환시키는 단계를 추가로 포함하며, 상기 A6PE는 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하는, 공정.
- 제1항 내지 제3항 중 어느 한 항에 있어서, 포도당 6-인산염(G6P)을 F6P로 전환시키는 단계를 추가로 포함하며, 상기 단계는 인산포도당 이성질화효소(PGI)에 의해 촉매되는, 공정.
- 제4항에 있어서, 포도당 1-인산염(G1P)을 G6P로 전환시키는 단계를 추가로 포함하며, 상기 단계는 인산포도당자리옮김효소(PGM)에 의해 촉매되는, 공정.
- 제5항에 있어서, 당류를 G1P로 전환시키는 단계를 추가로 포함하며, 상기 단계는 적어도 하나의 효소에 의해 촉매되고, 상기 당류는 전분 또는 이의 유도체, 셀룰로스 또는 이의 유도체 및 자당으로 이루어진 군으로부터 선택되는, 공정.
- 제6항에 있어서, 적어도 하나의 효소가 알파-글루칸 인산화효소(αGP), 엿당 인산화효소, 자당 인산화효소, 셀로덱스트린 인산화효소, 셀로비오스 인산화효소, 및 셀룰로스 인산화효소로 이루어진 군으로부터 선택되는 것인, 공정.
- 제6항에 있어서, 상기 당류가 아밀로스, 아밀로펙틴, 가용성 전분, 말토덱스트린, 엿당, 말토트리오스, 및 포도당으로 이루어진 군으로부터 선택된 전분 또는 이의 유도체인, 공정.
- 제8항에 있어서, 전분을 전분 유도체로 전환시키는 단계를 추가로 포함하며, 상기 전분 유도체는 전분의 효소적 가수분해 또는 전분의 산 가수분해에 의해 제조되는, 공정.
- 제9항에 있어서, 4-글루칸 전이효소(4GT)가 상기 공정에 첨가되는, 공정.
- 제9항에 있어서, 상기 전분 유도체가 이소아밀라제, 풀루라나제, 알파-아밀라제, 또는 이들의 조합에 의해 촉매되는 전분의 효소적 가수분해에 의해 제조되는, 공정.
- 제1항 내지 제3항 중 어느 한 항에 있어서,
적어도 하나의 효소에 의해 촉매되는 과당을 F6P로 전환시키는 단계; 및
선택적으로, 적어도 하나의 효소에 의해 촉매되는 자당을 과당으로 전환시키는 단계를 추가로 포함하는, 공정. - 제4항에 있어서,
적어도 하나의 효소에 의해 촉매되는 포도당을 G6P로 전환시키는 단계, 및
선택적으로, 적어도 하나의 효소에 의해 촉매되는 자당을 포도당으로 전환시키는 단계를 추가로 포함하는, 공정. - 제2항에 있어서, 상기 공정이 하기 단계를 포함하는 알룰로스를 생산하기 위한 효소적 공정이며, 하기 공정 단계 (i) 내지 (v)는 단일 반응 용기에서 수행되는, 공정:
(ⅰ) α-글루칸 인산화효소 또는 전분 인산화효소를 사용하여 당류를 포도당 1-인산염(G1P)으로 전환시키되, 상기 당류는 전분, 하나 이상의 전분의 유도체, 또는 이들의 조합으로 이루어진 군으로부터 선택되는, 단계;
(ⅱ) 인산포도당자리옮김효소(PGM)를 사용하여 G1P를 포도당 6-인산염(G6P)으로 전환시키는 단계;
(ⅲ) 인산포도당이성질화효소(PGI)를 사용하여 G6P를 과당 6-인산염(F6P)으로 전환시키는 단계;
(ⅳ) 알룰로스 6-인산염 에피머화효소(A6PE)를 사용하여 F6P를 알룰로스 6- 인산염(A6P)으로 전환시키는 단계, 및
(ⅴ) 알룰로스 6-인산염 인산가수분해효소(A6PP)를 사용하여 A6P를 알룰로스로 전환시키되, 상기 A6PP는 서열 번호: 2에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하는, 단계. - 제14항에 있어서, 상기 A6PE가 서열 번호: 1에 대해 적어도 90%의 서열 동일성을 갖는 아미노산 서열을 포함하는, 공정.
- 제14항 또는 제15항에 있어서, 상기 공정 단계가 하기 공정 조건 중 적어도 하나에서 수행되는, 공정:
(a) 약 37 ℃ 내지 약 85 ℃ 범위의 온도에서;
(b) 약 5.0 내지 약 9.0 범위의 pH에서; 또는
(c) 약 1 시간 내지 약 48 시간 동안. - 제14항 내지 제16항 중 어느 한 항에 있어서, 상기 공정 단계가 하기 공정 조건 중 적어도 하나에서 수행되는, 공정:
(a) 인산염의 공급원으로서 아데노신 삼인산염(ATP) 없이;
(b) 니코틴아미드 아데노신 디뉴클레오티드 없이;
(c) 약 0.1 mM 내지 약 150 mM의 인산염 농도에서;
(d) 약 0.1 mM 내지 50 mM의 Mg2+ 농도에서;
(e) 약 0.1 mM 내지 50 mM의 Co2+ 농도에서;
(f) 인산염이 재순환됨; 그리고
(g) 공정의 적어도 하나의 단계가 에너지적으로 유리한 화학 반응을 수반함. - 제17항에 있어서, 인산염이 재순환되고, A6P의 A6PP 탈인산화에 의해 생성된 인산염 이온이 당류를 G1P로 전환시키는 공정 단계에서 사용되는, 공정.
- 제17항에 있어서, A6P를 알룰로스로 전환시키는 단계가 에너지적으로 유리하고, 비가역적인 반응인, 공정.
- 제14항 내지 제19항 중 어느 한 항에 있어서, 생성된 알룰로스를 분리 회수하는 단계를 추가로 포함하고, 상기 분리 회수는 크로마토그래피 분리를 통하지 않는, 공정.
- 제14항 또는 제15항에 있어서, 상기 전분의 유도체가 아밀로스, 아밀로펙틴, 가용성 전분, 아밀로덱스트린, 말토덱스트린, 말토트리오스, 엿당, 및 포도당으로 이루어진 군으로부터 선택되는, 공정.
- 제1항 내지 제21항 중 어느 한 항의 공정으로부터 생성된 알룰로스.
- 제1항 내지 제21항 중 어느 한 항의 공정으로부터 생성된 알룰로스를 함유하는 소비재 제품.
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