Antihypertensive Properties of Enzymatic Hydrolysate of Rapeseed Protein and Its Ultrafiltered Fractions

doi:10.7506/spkx1002-6630-201315012

Abstract

Abstract:

In this study, rapeseed protein isolate was hydrolyzed by alcalase and then separated into four different peptide
fractions (＜ 1 kD, 1 to 3 kD, 3 to 5 kD, and 5 to 10 kD) by membrane ultrafiltration. Renin and angiotensin converting
enzyme-Ⅰ (ACE) inhibitory activity, and oxygen radical absorbance capacity (ORAC) of the rapeseed protein hydrolysate
(RPH) and its ultra-filtered fractions were evaluated. The results showed a negative correlation between the molecular
weights of the fractions and their ORAC values. The fraction less than 1 kD revealed the highest ACE inhibitory activity
(83.42 ± 0.35)% and ORAC value, while the hydrolysate had the highest renin inhibitory activity when compared with
other fractions. Therefore, RPH and the fraction less than 1 kD can be used to develop functional and healthcare foods
which can lower blood pressure.

Key words: rapeseed protein isolate, membrane ultrafiltration, angiotensin converting enzyme-Ⅰ, renin, oxygen radical absorbance capacity

CLC Number:

TS201.2

HE Rong1，JU Xing-rong1,2,*. Antihypertensive Properties of Enzymatic Hydrolysate of Rapeseed Protein and Its Ultrafiltered Fractions[J]. FOOD SCIENCE, doi: 10.7506/spkx1002-6630-201315012.

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Antihypertensive Properties of Enzymatic Hydrolysate of Rapeseed Protein and Its Ultrafiltered Fractions

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