TY - JOUR
T1 - Blood pressure lowering effects of Australian canola protein hydrolysates in spontaneously hypertensive rats
AU - Alashi, Adeola
AU - Blanchard, Christopher
AU - Mailer, Rodney
AU - Agboola, Samson
AU - Mawson, Andrew
AU - Rong, He.
AU - Malomo, Sunday A.
AU - Girgih, Abraham T.
AU - Aluko, Rotimi E.
N1 - Includes bibliographical references.
PY - 2014/1
Y1 - 2014/1
N2 - The in vitro and in vivo antihypertensive activities of canola protein hydrolysates and ultrafiltration membrane fractions (<1, 1-3, 3-5, & 5-10 kDa) were examined in this study. The hydrolysates were obtained after 4 h enzyme hydrolysis of canola protein isolate (CPI) using each of Alcalase, chymotrypsin, pepsin, trypsin and pancreatin. The hydrolysates had significantly (p<0.05) reduced (35-70%) surface hydrophobicity when compared to the CPI. Alcalase hydrolysate contained the highest level of low molecular weight peptides and produced highest (p<0.05) in vitro inhibition of angiotensin converting enzyme (ACE) activity. However, pancreatin hydrolysate was the most effective (63.2%) in vitro renin inhibitor. Membrane fractionation of pancreatin hydrolysate led to a 15% reduction in renin inhibition by the 1-3 kDa peptide fraction. In contrast, ACE and renin inhibitions were significantly (p<0.05) increased by 10-20% after membrane ultrafiltration fractionation of the trypsin hydrolysate. Trypsin hydrolysate was ineffective at reducing hypertension in spontaneously hypertensive rats after oral administration (200 mg/kg body weight). However, Alcalase and pepsin hydrolysates showed appreciable antihypertensive effects, with Alcalase hydrolysate producing the greatest (-34 mmHg) and fastest (4 h) decrease in systolic blood pressure (SBP). CPI had the most prolonged (24 h) SBP-reducing effect, which is attributable to the extensive protein hydrolysis in the GIT. We conclude that the Alcalase and pepsin hydrolysates may serve as useful ingredients to formulate antihypertensive functional foods and nutraceuticals.
AB - The in vitro and in vivo antihypertensive activities of canola protein hydrolysates and ultrafiltration membrane fractions (<1, 1-3, 3-5, & 5-10 kDa) were examined in this study. The hydrolysates were obtained after 4 h enzyme hydrolysis of canola protein isolate (CPI) using each of Alcalase, chymotrypsin, pepsin, trypsin and pancreatin. The hydrolysates had significantly (p<0.05) reduced (35-70%) surface hydrophobicity when compared to the CPI. Alcalase hydrolysate contained the highest level of low molecular weight peptides and produced highest (p<0.05) in vitro inhibition of angiotensin converting enzyme (ACE) activity. However, pancreatin hydrolysate was the most effective (63.2%) in vitro renin inhibitor. Membrane fractionation of pancreatin hydrolysate led to a 15% reduction in renin inhibition by the 1-3 kDa peptide fraction. In contrast, ACE and renin inhibitions were significantly (p<0.05) increased by 10-20% after membrane ultrafiltration fractionation of the trypsin hydrolysate. Trypsin hydrolysate was ineffective at reducing hypertension in spontaneously hypertensive rats after oral administration (200 mg/kg body weight). However, Alcalase and pepsin hydrolysates showed appreciable antihypertensive effects, with Alcalase hydrolysate producing the greatest (-34 mmHg) and fastest (4 h) decrease in systolic blood pressure (SBP). CPI had the most prolonged (24 h) SBP-reducing effect, which is attributable to the extensive protein hydrolysis in the GIT. We conclude that the Alcalase and pepsin hydrolysates may serve as useful ingredients to formulate antihypertensive functional foods and nutraceuticals.
KW - Open access version available
KW - Antihypertensive properties, angiotensin converting enzyme
KW - Canola protein isolate
KW - Hydrophobicity
KW - Protein hydrolysates
KW - Renin
KW - Spontaneously hypertensive rats
KW - Angiotensin converting enzyme
U2 - 10.1016/j.foodres.2013.11.015
DO - 10.1016/j.foodres.2013.11.015
M3 - Article
SN - 0963-9969
VL - 55
SP - 281
EP - 287
JO - Food Research International
JF - Food Research International
ER -