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Updated: Feb 8, 2026

Methanol Independent Expression by Pichia Pastoris Employing De-repression Technologies
Published on: January 23, 2019
Production of functional peptides with inhibition ability against angiotensin I-Converting enzyme using P. pastoris
Hsueh-Ming Tai1, Ching-Chin Li1, Chun-Yu Hung1
1Nugen Bioscience (Taiwan) Co., Ltd, 4F., No.35, Keya Rd., Daya Dist., Taichung City, 428, Taiwan.
Abstract:
To obtain the angiotension-I converting enzyme inhibitor (ACEI), a fusion ACEI polypeptide encoded with 8 DNA sequences of GPL, GPM, IKW, IVY, IRPVQ, IWHHT, IYPRY and IAPG, which were selected and designed and cloned into pGAPZαC and then transformed into Pichia pastoris SMD1168H. After 3 days induction, the fraction with highest ACEI activity was expressed and purified using a Ni Sepharose™ 6 Fast Flow. The IC50 of recombinant ACEI polypeptide was 88.2 μM. A 128-fold increase of ACEI activity (0.69 μM) was obtained after pepsin digestion, which was equivalent to 0.022 μM of captopril. Reverse phase HPLC indicated all the 8 peptides contained in ACEI-hydrolysate after pepsin digestion.
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