Selective separation and concentration of antihypertensive peptides from rapeseed protein hydrolysate by electrodialysis with ultrafiltration membranes

Rong He; Abraham T Girgih; Elodie Rozoy; Laurent Bazinet; Xing-Rong Ju; Rotimi E Aluko

doi:10.1016/j.foodchem.2015.11.081

Selective separation and concentration of antihypertensive peptides from rapeseed protein hydrolysate by electrodialysis with ultrafiltration membranes

Food Chem. 2016 Apr 15;197(Pt A):1008-14. doi: 10.1016/j.foodchem.2015.11.081.

Authors

Rong He¹, Abraham T Girgih², Elodie Rozoy³, Laurent Bazinet³, Xing-Rong Ju⁴, Rotimi E Aluko⁵

Affiliations

¹ College of Food Science & Engineering, Nanjing University of Finance and Economics, Nanjing 210023, People's Republic of China; Department of Human Nutritional Sciences and the Richardson Centre for Functional Foods and Nutraceuticals, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada; College of Food Science, Jiangnan University, Wuxi 214122, People's Republic of China; College of Food Science and Engineering/Collaborative Innovation Center for Modern Grain Circulation and Safety/Key Laboratory of Grains and Oils Quality Control and Processing, Nanjing University of Finance and Economics, Nanjing 210023, China. Electronic address: rong.he@njue.edu.cn.
² Department of Human Nutritional Sciences and the Richardson Centre for Functional Foods and Nutraceuticals, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada.
³ Department of Food Sciences, Laval University, Quebec G1V 0A6, Canada.
⁴ College of Food Science & Engineering, Nanjing University of Finance and Economics, Nanjing 210023, People's Republic of China; College of Food Science, Jiangnan University, Wuxi 214122, People's Republic of China.
⁵ Department of Human Nutritional Sciences and the Richardson Centre for Functional Foods and Nutraceuticals, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada. Electronic address: rotimi.aluko@umanitoba.ca.

PMID: 26617047
DOI: 10.1016/j.foodchem.2015.11.081

Abstract

Rapeseed protein isolate was subjected to alcalase digestion to obtain a protein hydrolysate that was separated into peptide fractions using electrodialysis with ultrafiltration membrane (EDUF) technology. The EDUF process (6h duration) led to isolation of three peptide fractions: anionic (recovered in KCl-1 compartment), cationic (recovered in KCl-2 compartment), and those that remained in the feed compartment, which was labeled final rapeseed protein hydrolysate (FRPH). As expected the KCl-1 peptides were enriched in negatively-charged (43.57%) while KCl-2 contained high contents of positively-charged (28.35%) amino acids. All the samples inhibited angiotensin converting enzyme (ACE) and renin activities in dose-dependent manner with original rapeseed protein hydrolysate having the least ACE-inhibitory IC50 value of 0.0932±0.0037 mg/mL while FRPH and KCl-2 had least renin-inhibitory IC50 values of 0.47±0.05 and 0.55±0.06 mg/mL, respectively. Six hours after oral administration (100 mg/kg body weight) to spontaneously hypertensive rats, the FRPH produced the maximum systolic blood pressure reduction of -51 mmHg.

Keywords: ACE; Electrodialysis with ultrafiltration membrane; Protein hydrolysate; Rapeseed; Renin; Spontaneously hypertensive rats; Systolic blood pressure.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Angiotensin-Converting Enzyme Inhibitors / analysis
Angiotensin-Converting Enzyme Inhibitors / chemistry
Animals
Antihypertensive Agents / analysis*
Blood Pressure / drug effects
Brassica rapa / chemistry*
Dialysis
Male
Peptides / analysis*
Peptidyl-Dipeptidase A / pharmacology
Protein Hydrolysates / analysis*
Rats
Rats, Inbred SHR
Renin / antagonists & inhibitors
Ultrafiltration

Substances

Angiotensin-Converting Enzyme Inhibitors
Antihypertensive Agents
Peptides
Protein Hydrolysates
ACE protein, human
Peptidyl-Dipeptidase A
Renin