Angiotensin I-converting enzyme inhibitory and antioxidant properties of rapeseed hydrolysates

Journal of Functional Foods

Sari Mäkinen¹  Juha Matti Pihlava¹  Tessa Johannson¹  Anne Pihlanto¹  E. Vegarud Gerd² 

[1] MTT Agrifood Research Finland, Biotechnology and Food Research, Alimentum, FI-31600 Jokioinen, Finland;Norwegian University of Life Sciences, Department of Chemistry, Biotechnology and Food Science, N-1432 Ås, Norway;

关键词: Rapeseed by-product hydrolysates;    Bioactive peptides;    Protein;    Angiotensin I-converting enzyme inhibition;    Enzymatic hydrolysis;   

DOI  :  

来源: DOAJ

【 摘 要 】

This study investigates the angiotensin I-converting enzyme (ACE) inhibitory and antioxidative activities of protein hydrolysates prepared from industrial defatted rapeseed meal using various proteolytic enzymes. The hydrolysate generated by Alcalase displayed the highest ACE-inhibitory activity (IC50 0.02 mg/ml) as well as high inhibitory capacity against lipid oxidation in a liposomal model. The Alcalase hydrolysate was fractionated using stepwise solid-phase extraction into three fractions (SP10, SP30, SP60), of which the hydrophobic fractions possessed the highest ACE-inhibitory activity. Subjecting these fractions to ultra filtration with 3000 Da molecular weight cut off (MWCO) membrane revealed that ACE-inhibitory activity was concentrated in the permeate. The ACE-inhibitory peptides in Alcalase hydrolysate exhibited good stability in an in vitro digestion model using human gastric and duodenal fluids. Kinetics studies gave moderate Ki values (0.2–0.3 mg/ml) and an uncompetitive pattern of ACE inhibition for the Alcalase hydrolysate and peptide fractions. Our results indicate the defatted rapeseed meal is a potential source of ACE-inhibitory compounds for use in functional foods.

【 授权许可】

Unknown