Nutritional composition and angiotensin converting enzyme inhibitory activity of blue lupin (Lupinus angustifolius)

Abstract

The nutritional, protein and amino acid compositions of blue lupin (Lupinus angustifolius) flour were studied. The angiotensin converting enzyme (ACE) inhibitory activity of lupin protein isolate (LPI) hydrolysates prepared using Alcalase and Flavourzyme, and the Osborne protein fractions hydrolysates prepared using Alcalase were determined. Lupin flour was high in protein (43 g/100 g) and dietary fiber (34 g/100 g) but low in carbohydrate (4.8 g/100 g) and ash (3.4 g/100 g). Results from a sequential Osborne extraction procedure showed that lupin protein was comprised of 56% globulin, 26% albumin and 19% glutelin, while prolamin was only found in trace amounts. Lupin protein was high in Lys but limiting in Met. SDS-PAGE analysis suggested that protein hydrolysis catalyzed using Alcalase was more effective than Flavourzyme as shown by the presence of lower molecular weight peptides in the former. LPI hydrolysates prepared using Alcalase showed high ACE inhibitory activities with IC50 values ranging from 0.10 to 0.21 mg/ml. The results suggested that the globulin fraction was the main contributor towards the ACE inhibitory activity observed in lupin protein.

Techno-Functional, Nutritional and Environmental Performance of Protein Isolates from Blue Lupin and White Lupin

“…In the case of white lupin, values of 2.58 and 2.64 g/100 g protein have been reported for flour [80,81] and 1.68 g/100 g protein for protein isolate [56]. The proportion of SAAs has been found to increase [42,55,78] and also to decrease [79] during isolation of lupin proteins, indicating that at least some of the variation observed is due to differences in processing conditions. Additionally, Sujak et al [75] compared AA profiles of whole lupin beans of various cultivars, and on average white lupins were found to be slightly higher in SAAs than blue lupins.…”

“…Lupin proteins, as well as most other legume proteins, are generally relatively low in SAAs [55,56,77]. However, literature values vary for SAA content, particularly with blue lupin; for flours, values of 1.52-4.8 g/100 g protein have been reported, and for protein isolates values of 1.61-4.2 g/100 g protein have been found [55,78,79]. In the case of white lupin, values of 2.58 and 2.64 g/100 g protein have been reported for flour [80,81] and 1.68 g/100 g protein for protein isolate [56].…”

Multifunctional in vitro bioactive properties: Antioxidant, antidiabetic, and antihypertensive of protein hydrolyzates from tarwi (Lupinus mutabilis Sweet) obtained by enzymatic biotransformation

“…In addition, Chin et al. (2019) for protein hydrolyzates of L. angustifolius using Alcalase reported values of IC 50 ranging from 0.10 to 0.21 mg/ml. Chirinos et al.…”

“…& Arnoldi (2014) evaluated the ACE inhibitory activity of hydrolyzates obtained by pepsin digestion of proteins from chickpea, common bean, lentil, two lupine: L. albus and L. angustifolius, pea, and soybean and reported IC 50 values of 0.67, 0.63, 0.61, 0.27, 0.23, 0.59, and 0.22 mg/ ml, respectively. In addition, Chin et al (2019) for protein hydrolyzates of L. angustifolius using Alcalase reported values of IC 50 ranging from 0.10 to 0.21 mg/ml. Chirinos et al (2018) for cañihua protein hydrolyzates obtained by sequential use of Neutrase-Alcalase for 180 min reported an IC 50 value of 0.18 mg/ml, being this value higher than those obtained for a quinoa protein hydrolyzate using Neutrase for 120 min (IC 50 = 0.080 mg/ml) (Chirinos et al, 2020).…”

Functional properties of Australian blue lupin (Lupinus angustifolius) protein and biological activities of protein hydrolysates

“…The angiotensin converting enzyme (ACE) inhibitors reduce the activity of ACE and produce a vasorelaxing effect on blood vessels (Barbana & Boye, 2011; Kamran, Salampessy, & Reddy, 2016; Kuba, Tana, Tawata, & Yasuda, 2005; Nasri et al, 2013; Paiva, Lima, Neto, & Baptista, 2016; Rho, Lee, Chung, Kim, & Lee, 2009; Shahidi & Zhong, 2008). Therefore, inhibition of ACE is very important in regulating blood pressure in hypertensive subjects (Boschin, Scigliuolo, Resta, & Arnoldi, 2014a; Chin et al, 2019; Hong et al, 2008; Lavoie & Sigmund, 2003; Luna‐Vital, Mojica, González de Mejía, Mendoza, & Loarca‐Piña, 2015; Mäkinen, Streng, Larsen, Laine, & Pihlanto, 2016; Shahidi & Zhong, 2008). During the past decade, several ACE inhibitory peptides (ACEIPs)/antihypertensive peptides were derived from various food proteins with significant activity in reducing blood pressure and treating cardiovascular diseases (Balti et al, 2015; Boschin, Scigliuolo, Resta, & Arnoldi, 2014a; Nongonierma & FitzGerald, 2016; Shahidi & Zhong, 2008).…”