
극한성 미생물Deinococcus geothermalis 유래 재조합 글루코아밀레이즈의 전분 분해 활성 특징
Characterization of the Starch Degradation Activity of recombinant glucoamylase from Extremophile Deinococcus geothermalis
- 장승원(Seung-Won Jang) 권덕호(Deok-Ho Kwon) 박재범(Jae-Bum Park) 정종현(Jong-Hyun Jung) 하석진(Suk-Jin Ha)
- 강원대학교 산업기술연구소
- 산업기술연구
- vol.39
- 2019.10
- 15 - 19 (5 pages)
This work focused on characterization of the starch degradation activity from extremophile strain Deinococcus geothermalis. Glucoamylase gene from D. geothermalis was cloned and overexpressed by pET-21a vector using E. coli BL21 (DE3). In order to characterize starch degrading activity of recombinant glucoamylase, enzyme was purified using HisPur Ni-NTA column. The recombinant glucoamylase from D. geothermalis exhibited the optimum temperature as 45°C for starch degradation activity. And highly acido-stable starch degrading activity was shown at pH 2. For further optimization of starch degrading activity with metal ion, various metal ions (AgCl 2 , HgCl 2 , MnSO 4⦁ 4H 2 O, CoCl 2⦁ 6H 2 O, MgSO 4 , ZnSO 4⦁ 7H 2 O, K 2 SO 4 , FeCl 2⦁ 4H 2 O, NaCl, or CuSO 4 ) were added for enzyme reaction. As results, it was found that FeCl 2⦁ 4H 2 O or MnSO 4⦁ 4H 2 O addition resulted in 17% and 9% improved starch degrading activity, respectively. The recombinant glucoamylase from D. geothermalis might be used for simultaneous saccharification and fermentation (SSF) process at high acidic conditions.
1. 서 론
2. 결과 및 고찰
3. 실험재료 및 방법
4. 결 론