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