Extracellular Expression and Catalytic Bioactivity of Optimized Human Aromatase (CYP19) in Pichia Pastoris
Yan-ying HU, Yong-hui ZHONG, Jing ZHEN, Hui-tu ZHANG, Shi-ru JIA, Fu-ping LU, Yu-jie DAI, Xiu-li ZHANG
Available Online May 2017.
- https://doi.org/10.2991/bbe-17.2017.3How to use a DOI?
- Recombinant aromatase, Pichia pastoris, Heterologous protein production.
- The fragment encoding aromatase (CYP19) with 45 N-terminal amino acids cut-off was cloned into pPIC9K vector and transformed to the yeast Pichia pastoris. The multi-copy recombinant strain was selected for the production of recombinant aromatase. The catalytic bioactivity of secreted enzyme was further verified by fluorescent substrate detection method. The results indicate that aromatase was successfully expressed in recombinant Pichia pastoris strain and secreted into the culture supernatant. The extracellular expression of the bioactive aromatase by P. pastoris provides us a better alternative for aromatase commercial production and promotes the research progress for the discovery of novel aromatase.
- Open Access
- This is an open access article distributed under the CC BY-NC license.
Cite this article
TY - CONF AU - Yan-ying HU AU - Yong-hui ZHONG AU - Jing ZHEN AU - Hui-tu ZHANG AU - Shi-ru JIA AU - Fu-ping LU AU - Yu-jie DAI AU - Xiu-li ZHANG PY - 2017/05 DA - 2017/05 TI - Extracellular Expression and Catalytic Bioactivity of Optimized Human Aromatase (CYP19) in Pichia Pastoris BT - Proceedings of the 2nd International Conference on Biomedical and Biological Engineering 2017 (BBE 2017) PB - Atlantis Press SP - 11 EP - 16 SN - 2468-5747 UR - https://doi.org/10.2991/bbe-17.2017.3 DO - https://doi.org/10.2991/bbe-17.2017.3 ID - HU2017/05 ER -