Enzyme inhibitor

ACE inhibitor

Biology

Identification (biology)

Angiotensin-converting enzyme

Captopril

Spontaneously hypertensive rat

Ultrafiltration (renal)

Papain

Peptide

Endocrinology

Hydrolysate

Biochemistry

Botany

Food science

Blood pressure

Renin–angiotensin system

In vitro

Oral administration

Enzyme

Internal medicine

Hydrolysis

Pharmacology

Mung bean

IC50

Medicine

Chemistry

Journal of Functional Foods

Defatted mung bean meal was hydrolyzed with bromelain to obtain MPH, which was fractionated into different peptide fractions (<1 kDa, 1–5 kDa, 5–10 kDa, >10 kDa) using membrane ultrafiltration. The <1 kDa was the most active inhibitor of angiotensin converting enzyme (ACE) and renin. Five peptides (LPRL, YADLVE, LRLESF, HLNVVHEN, and PGSGCAGTDL) identified from the <1 kDa fraction were studied for antihypertensive effects in comparison to the MPH. Results showed that LRLESF was the most potent inhibitor of ACE (IC50 = 5.4 µM) while LPRL was the weakest (IC50 = 1912 µM). In contrast, YADLVE was the strongest renin inhibitor with 97% inhibition while LRLESF was the weakest (~30%). Oral administration to spontaneously hypertensive rats revealed strong blood pressure reductions with up to −36 mmHg when compared to −15 mmHg for MPH. However, YADLVE had the most persistent effect after 24 h while PGSGCAGTDL had the least.

Identification of antihypertensive peptides from mung bean protein hydrolysate and their effects in spontaneously hypertensive rats