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Review

Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review

1
Department of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, Indonesia
2
Department of Food Science and Technology, The Ohio State University, 2015 Fyffe Rd, Columbus, OH 43210, USA
*
Author to whom correspondence should be addressed.
Academic Editor: Maria Atanassova
Molecules 2021, 26(13), 3822; https://doi.org/10.3390/molecules26133822
Received: 18 May 2021 / Revised: 19 June 2021 / Accepted: 21 June 2021 / Published: 23 June 2021
The Angiotensin-I-converting enzyme (ACE) is a peptidase with a significant role in the regulation of blood pressure. Within this work, a systematic review on the enzymatic preparation of Angiotensin-I-Converting Enzyme inhibitory (ACEi) peptides is presented. The systematic review is conducted by following PRISMA guidelines. Soybeans and velvet beans are known to have high protein contents that make them suitable as sources of parent proteins for the production of ACEi peptides. Endopeptidase is commonly used in the preparation of soybean-based ACEi peptides, whereas for velvet bean, a combination of both endo- and exopeptidase is frequently used. Soybean glycinin is the preferred substrate for the preparation of ACEi peptides. It contains proline as one of its major amino acids, which exhibits a potent significance in inhibiting ACE. The best enzymatic treatments for producing ACEi peptides from soybean are as follows: proteolytic activity by Protease P (Amano-P from Aspergillus sp.), a temperature of 37 °C, a reaction time of 18 h, pH 8.2, and an E/S ratio of 2%. On the other hand, the best enzymatic conditions for producing peptide hydrolysates with high ACEi activity are through sequential hydrolytic activity by the combination of pepsin-pancreatic, an E/S ratio for each enzyme is 10%, the temperature and reaction time for each proteolysis are 37 °C and 0.74 h, respectively, pH for pepsin is 2.0, whereas for pancreatin it is 7.0. As an underutilized pulse, the studies on the enzymatic hydrolysis of velvet bean proteins in producing ACEi peptides are limited. Conclusively, the activity of soybean-based ACEi peptides is found to depend on their molecular sizes, the amino acid residues, and positions. Hydrophobic amino acids with nonpolar side chains, positively charged, branched, and cyclic or aromatic residues are generally preferred for ACEi peptides. View Full-Text
Keywords: angiotensin-I-converting enzyme (ACE); bioactive peptide; endopeptidase; enzymatic hydrolysis; exopeptidase; soybean; velvet bean angiotensin-I-converting enzyme (ACE); bioactive peptide; endopeptidase; enzymatic hydrolysis; exopeptidase; soybean; velvet bean
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MDPI and ACS Style

Sitanggang, A.B.; Putri, J.E.; Palupi, N.S.; Hatzakis, E.; Syamsir, E.; Budijanto, S. Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review. Molecules 2021, 26, 3822. https://doi.org/10.3390/molecules26133822

AMA Style

Sitanggang AB, Putri JE, Palupi NS, Hatzakis E, Syamsir E, Budijanto S. Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review. Molecules. 2021; 26(13):3822. https://doi.org/10.3390/molecules26133822

Chicago/Turabian Style

Sitanggang, Azis B., Jessica E. Putri, Nurheni S. Palupi, Emmanuel Hatzakis, Elvira Syamsir, and Slamet Budijanto. 2021. "Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review" Molecules 26, no. 13: 3822. https://doi.org/10.3390/molecules26133822

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