Extracellular Expression and Catalytic Bioactivity of Optimized Human Aromatase (CYP19) in Pichia Pastoris

DOI

10.2991/bbe-17.2017.3How to use a DOI?

Keywords

Recombinant aromatase, Pichia pastoris, Heterologous protein production.

Abstract

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.

Copyright

© 2017, the Authors. Published by Atlantis Press.

Open Access

This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).

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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  - 10.2991/bbe-17.2017.3
ID  - HU2017/05
ER  -