Journal of Food and Drug Analysis 2018-02-21

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

Hsueh-Ming Tai, Ching-Chin Li, Chun-Yu Hung, Li-Jung Yin

Index: 10.1016/j.jfda.2018.02.001

Full Text: HTML

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 Pichiapastoris 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.

Latest Articles:

Organic solute carrier 22 (SLC22) family: Potential for interactions with food, herbal/dietary supplements, endogenous compounds, and drugs

2018-03-24

[10.1016/j.jfda.2018.03.002]

Effects of processing adjuvants on traditional Chinese herbs

2018-03-19

[10.1016/j.jfda.2018.02.004]

Kinetics of lactose fermentation in milk with kombucha starter

2018-03-14

[10.1016/j.jfda.2018.02.002]

Simultaneous analysis of 23 illegal adulterated aphrodisiac chemical ingredients in health foods and Chinese traditional patent medicines by ultrahigh performance liquid chromatography coupled with quadrupole time-of-flight mass spectrometry

2018-03-14

[10.1016/j.jfda.2018.02.003]

Volatile sulfur compounds in tropical fruits

2018-02-16

[10.1016/j.jfda.2018.01.014]

More Articles...