Production of functional peptides with inhibition ability against angiotensin I-Converting enzyme using P. pastoris expression system

Authors

H.-M. Tai
C.-C. Li
C.-Y. Hung
L.-J. Yin

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. © 2018

Abstract Image

ScienceDirect Link

10.1016/j.jfda.2018.02.001

Recommended Citation

Tai, H.-M.; Li, C.-C.; Hung, C.-Y.; and Yin, L.-J. (2018) "Production of functional peptides with inhibition ability against angiotensin I-Converting enzyme using P. pastoris expression system," Journal of Food and Drug Analysis: Vol. 26 : Iss. 3 , Article 7.
Available at: https://doi.org/10.1016/j.jfda.2018.02.001

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https://www.sciencedirect.com/science/article/pii/S1021949818300413/pdfft?md5=e66998ea54ed3d711cc534b3bebff230&pid=1-s2.0-S1021949818300413-main.pdf