Antihypertensive effect of rapeseed peptides and their potential in improving the effectiveness of captopril.

BACKGROUND: The main objective of this study was to evaluate the safety and antihypertensive activity of rapeseed peptides and to investigate their potential synergy with captopril. RESULTS: The peptides were nontoxic with the maximum tolerated dose exceeding 25 g kg-1 BW d-1 for mice and they had angiotensin converting enzyme (ACE) inhibitory activity with IC50 value of 1.27 mg mL-1 . Rapeseed peptides did not have a synergistic effect with captopril on inhibiting ACE activity in simulated digestion tests in vitro. But in vivo they could synergistically augment the amplitude range of lowering blood pressure with captopril by approximately 9% and prolong the antihypertensive effect duration time by over 20% in antihypertension tests of spontaneously hypertensive rats. In addition, the inhibiting effect of rapeseed peptides on ACE activity was noticeable in some rat organs in vivo. Nevertheless, when compared to captopril group, the potential synergy of rapeseed peptides with captopril did not cause a further decrease in ACE activity in the organs but their synergy further improved levels of NO (12.7%) and endothelial nitric oxide synthase (74.1%) in rat serum. Further studies of some peptides identified from rapeseed peptides showed that some of the rapeseed peptides (Cys-Leu, Val-Ala-Pro) could markedly increase contents of NO and endothelial nitric oxide synthase. CONCLUSIONS: Rapeseed peptides have antihypertensive activity and they showed potential synergy with captopril in antihypertensive performance in vivo. The synergy was not from ACE inhibition but from other pathways, like improvement in endogenous vasodilator contents. © 2020 Society of Chemical Industry.

[Study on the structure of defatted wheat germ protein isolate under ultrasonic treatment].

The structure changes of defatted wheat germ protein Isolate (DWGP) treated by ultrasonic was determined by FTIR and fluorescence spectra, and the effect of its structure changes on the high-efficient enzymatic hydrolysis was studied. Research showed that the efficiency of hydrolysate could be improved by ultrasonic treatment. Compared with control group, inhibitory activity of the hydrolysate was increased by 23.96% after the treatment of 600 W for 10 min. The fluorescence intensity of DWGP after ultrasonic treatment was found discovered to be changed. An appropriate ultrasonic treatment can unfold the protein molecule and make the chromogenic groups uncovered, which contribute to the acquirement of the higher-activity inhibitory peptide. The effects of various ultrasonic power and time on the secondary structure of DWGP were quantitatively determined via analysis of the amide I changes of infrared spectra using curve fitting method. Content of beta-sheet was decreased and beta-turn was increased after ultrasonic treatment, which could be the main factor to make the prepared inhibitory peptides high efficient. The results provide a theoretical basis for the mechanism research of enzymatic hydrolysis of ultrasonic treated protein.