Angiotensin converting enzyme inhibitory activity of Proteolytic digests of peanut (Arachis hyopogaea L.) flour

CRSP:   |  Region:   |  Topic:   |  Database:

E.E. Quist; R.D. Phillips; F.K. Saalia

Type of Document:
Scholarly Article


LWT- Food Science and Technology

Date of Publication:

Place of Publication:
Not Available


Abstract: Defatted raw and roasted peanut flour were hydrolyzed with alcalase or sequentially with pepsin and pancreatin, and then the hydrolyzates were fractionated by RP-HPLC and tested for hypotensive potential. This research revealed that proteolytic peanut digests have an inhibitory effect on the activity of angiotensin converting enzyme (ACE). Three fractions from the hydrophobic end of the chromatogram of each hydrolyzate were the most potent for inhibiting ACE activity in comparison to seven other fractions. These potentially potent fractions were then assayed for IC50. Fractions from the alcalase digestion of raw peanut exhibited IC50 values of 8.7

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