Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2019 Sep 4;8(9):390.
doi: 10.3390/foods8090390.

In Vitro Production and Identification of Angiotensin Converting Enzyme (ACE) Inhibitory Peptides Derived from Distilled Spent Grain Prolamin Isolate

Dong Wei  1 , Wenlai Fan  2 , Yan Xu  1
Affiliations

In Vitro Production and Identification of Angiotensin Converting Enzyme (ACE) Inhibitory Peptides Derived from Distilled Spent Grain Prolamin Isolate

Dong Wei et al. Foods. .

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.

Keywords: ACE inhibitory peptides; AVQ; Prolamin isolate hydrolysates; RP-HPLC; YPQ; baijiu (Chinese liquor); distilled spent grain (DSG).

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Degree of hydrolysis (DH) of DDSG-PI hydrolysates treated by three proteolytic enzymes.
Figure 2
Figure 2
Angiotensin converting enzyme (ACE) inhibitory activity of DDSG-PI hydrolysates as a function of hydrolysis time using different proteases. Key: (A), Flavourzyme; (B), Neutrase; (C), Alcalase. Hydrolysates were taken at 0, 0.5, 1, 2, 3, 4, and 5 h, freeze-dried, and then ACE inhibitory activity was measured at a final concentration of 1 mg/mL (based on dry weight (DW)). All data were presented as means ± SD (n = 3). Samples with different letters in the same sample group showed significant differences (p < 0.05).
Figure 3
Figure 3
Reversed phase high performance liquid chromatography (RP-HPLC) elution profile of Alcalase-generated DDSG-PI hydrolysate (<1 kDa) after ultrafiltration. The eluates were collected by every tube and combined into eight different fractions labeled I–VIII.
Figure 4
Figure 4
ACE inhibition of different fractions after semi-preparative RP-HPLC. Elutes were combined into eight fractions and analyzed for ACE inhibitory activity at a final concentration of 0.5 mg/mL (based on DW). All data were presented as means ± SD (n = 3). Different letters indicated the significant difference at p < 0.05.
Figure 5
Figure 5
Mass spectrometry (MS) spectra of peak at 14.08 min by full scan-survey mode. Key: (A), at low collision energy (6 eV); (B), at high collision energy (20 eV).
Figure 6
Figure 6
MS/MS spectrum of the peptide (m/z = 494.2608) in a single charge mode.
See this image and copyright information in PMC

References

    1. Balti R., Bougatef A., Sila A., Guillochon D., Dhulster P., Nedjar-Arroume N. Nine novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) muscle protein hydrolysates and antihypertensive effect of the potent active peptide in spontaneously hypertensive rats. Food Chem. 2015;170:519–525. doi: 10.1016/j.foodchem.2013.03.091. - DOI - PubMed
    1. So P.B.T., Rubio P., Lirio S., Macabeo A.P., Huang H.Y., Corpuz M.J.A.T., Villaflores O.B. In vitro angiotensin I converting enzyme inhibition by a peptide isolated from Chiropsalmus quadrigatus Haeckel (box jellyfish) venom. Toxicon. 2016;119:77–83. doi: 10.1016/j.toxicon.2016.04.050. - DOI - PubMed
    1. Lopez-Fandino R., Otte J., van Camp J. Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE-inhibitory activity. Int. Dairy J. 2006;16:1277–1293. doi: 10.1016/j.idairyj.2006.06.004. - DOI
    1. Eriksson U., Danilczyk U., Penninger J.M. Just the beginning: Novel functions for angiotensin-converting enzymes. Curr. Biol. 2002;12:R745–R752. doi: 10.1016/S0960-9822(02)01255-1. - DOI - PubMed
    1. Rabelo E.R., Rohde L.E., Schaan B.D., Rubira M.C., Ruschel K.B., Plentz R.D.M., Consolim-Colombo F.M., Irigoyen M.C., Moreno H. Bradykinin or acetylcholine as vasodilators to test endothelial venous function in healthy subjects. Clinics. 2008;63:677–682. doi: 10.1590/S1807-59322008000500017. - DOI - PMC - PubMed

LinkOut - more resources