Angiotensin Converting Enzyme Inhibitory Activity of Blue Lupin (Lupinus angustifolius) Proteins. (29th May 2020)

• Record Type: Journal Article
• Authors: Yee, Chin; Yee, Chew; Ismail, Amin; Theng, Toh; Azlan, Azrina
• Is Part Of: Current developments in nutrition. Volume 4(2020)Supplement 2
• Page Start: 492
• Page End: 492
• Publication Date: 2020-05-29
• Subjects: Nutrition -- Periodicals; Nutritional Physiological Phenomena; Nutrition; Periodicals; Periodicals; Fulltext; Internet Resources; Periodicals; 612.3
• DOI: 10.1093/cdn/nzaa045_125
• Languages: English
• ISSNs: 2475-2991

Abstract

Abstract: Objectives: To evaluate the ACE inhibitory activity of protein hydrolysates derived from lupin Methods: Methods used are spectrophotometer to assay the ACE activity, electrophoresis for estimation of protein molecular weight, and HPLC for determining products of ACE activity. Results: The results revealed that the lupin flour was abundant in protein (43.3 g/100 g). Results from sequential Osborne extraction procedure showed that lupin protein comprised of 46% salt-soluble globulin, 27% water-soluble albumin, 18% alkaline-soluble glutelin and 7% alcohol-soluble prolamin fractions. Furthermore, lupin protein was rich in lysine but limiting in methionine. Hydrolysates prepared using Alcalase exhibited higher ACE inhibitory activities compared with those prepared using Flavourzyme, showing IC50 values ranging from 0.10 to 0.21 mg/mL. However, there was no significant difference in IC50 values between the hydrolysates prepared using Alcalase for 4, 10 and 16 h of hydrolysis times. Conclusions: The results suggested that globulin was the major contributing protein fraction on ACE inhibitory effect in lupin protein. The lupin protein hydrolysates with potent ACE inhibitory activities can be incorporated into the daily diet to prevent hypertension. Funding Sources: Ministry of Education Malaysia.