Abstract
Distilled spent grain (DSG), the biggest by-product of the Chinese liquor industry, is rich in protein (167.8 g/kg DSG dry weight (DW)). Accounting for 60% of the total protein, prolamins are isolated from dried DSG (DDSG). In this study, angiotensin-converting enzyme (ACE) inhibitory peptides were screened from the prolamin hydrolysates of DDSG using two independent active-directed separations, ultrafiltration and reversed phase high performance liquid chromatography (RP-HPLC) coupled with ACE inhibitory activity evaluation. Six novel ACE inhibitory peptides, AVQ, YPQ, NQL, AYLQ, VLPVLS, and VLPSLN, were successfully identified and quantified from the active RP-HPLC fractions. AVQ and YPQ exhibited the highest activity, having the concentration inducing 50% inhibition (IC50) values for ACE of 181.0 and 220.0 μM, respectively. It was observed that VLPVLS was the most abundant peptide (16.96 mg/g DW) in prolamins. The results indicated that prolamin hydrolysates from DDSG could be served as a source of ACE inhibitory peptides.
Highlights
Hypertension is one of the well-defined risk factors of cardiovascular disease, with about 30%adults worldwide suffer from high blood pressure [1,2]
It was obviously observed that the angiotensin-converting enzyme (ACE) inhibitory activity of ultrafiltration hydrolysate was not directly correlated with molecular weight distribution range (Table 3), which was consistent with the findings reported previously [12,31]
This study evaluated the ACE inhibitory capacity of ultrafiltration and reversed phase high performance liquid chromatography (RP-HPLC) fractions derived from dried DSG (DDSG)-PI hydrolysates, which were produced by Alcalase, Neutrase, and Flavourzyme
Summary
Hypertension is one of the well-defined risk factors of cardiovascular disease, with about 30%adults worldwide suffer from high blood pressure [1,2]. 3.4.15.1), a zinc-containing dipeptide carboxypeptidase, is a key rate-limiting enzyme for the regulation of blood pressure through the renin-angiotensin system (RAS) and kinin–kallikrein system (KKS). As part of RAS, ACE hydrolyzes an inactive angiotensin I to vasoconstrictor angiotensin II while ACE inactivates the hypotensive bradykinin with strong vasodilation in the KKS [3,4]. ACE inhibitors were expected to inhibit the formation of the vasoconstrictor angiotensin II and enhance bradykinin vasodilation (hypotension) properties [5]. Food-derived ACE inhibitors such as peptides with high ACE inhibitory activity are believed safer than drugs with related side effects, such as cough and angioedema [6]. In order to a continuous dietary intake, ACE inhibitory peptides derived from food proteins are expected to be isolated. The most strategy to induce the release of antihypertensive peptides in vitro is enzymatic digestion (hydrolysis)
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