Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review
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 f...
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MDPI AG
2021-06-01
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| Series: | Molecules |
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| author | Azis Boing Sitanggang Jessica Eka Putri Nurheni Sri Palupi Emmanuel Hatzakis Elvira Syamsir Slamet Budijanto |
| author_facet | Azis Boing Sitanggang Jessica Eka Putri Nurheni Sri Palupi Emmanuel Hatzakis Elvira Syamsir Slamet Budijanto |
| author_sort | Azis Boing Sitanggang |
| collection | DOAJ |
| description | 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 <i>Aspergillus</i> 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. |
| first_indexed | 2024-03-10T10:08:47Z |
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| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T10:08:47Z |
| publishDate | 2021-06-01 |
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| record_format | Article |
| series | Molecules |
| spelling | doaj.art-b8fa892d249146a6a38428b7672d03322023-11-22T01:20:53ZengMDPI AGMolecules1420-30492021-06-012613382210.3390/molecules26133822Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic ReviewAzis Boing Sitanggang0Jessica Eka Putri1Nurheni Sri Palupi2Emmanuel Hatzakis3Elvira Syamsir4Slamet Budijanto5Department of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, IndonesiaDepartment of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, IndonesiaDepartment of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, IndonesiaDepartment of Food Science and Technology, The Ohio State University, 2015 Fyffe Rd, Columbus, OH 43210, USADepartment of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, IndonesiaDepartment of Food Science and Technology, Kampus IPB Darmaga, IPB University, Bogor 16680, IndonesiaThe 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 <i>Aspergillus</i> 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.https://www.mdpi.com/1420-3049/26/13/3822angiotensin-I-converting enzyme (ACE)bioactive peptideendopeptidaseenzymatic hydrolysisexopeptidasesoybean |
| spellingShingle | Azis Boing Sitanggang Jessica Eka Putri Nurheni Sri Palupi Emmanuel Hatzakis Elvira Syamsir Slamet Budijanto Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review Molecules angiotensin-I-converting enzyme (ACE) bioactive peptide endopeptidase enzymatic hydrolysis exopeptidase soybean |
| title | Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review |
| title_full | Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review |
| title_fullStr | Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review |
| title_full_unstemmed | Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review |
| title_short | Enzymatic Preparation of Bioactive Peptides Exhibiting ACE Inhibitory Activity from Soybean and Velvet Bean: A Systematic Review |
| title_sort | enzymatic preparation of bioactive peptides exhibiting ace inhibitory activity from soybean and velvet bean a systematic review |
| topic | angiotensin-I-converting enzyme (ACE) bioactive peptide endopeptidase enzymatic hydrolysis exopeptidase soybean |
| url | https://www.mdpi.com/1420-3049/26/13/3822 |
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