BIOPEP-UWM: Report
| ID | 7872 |
| Name | peptide from soybean protein isolates: beta-conglycinin and glycinin |
| sequence |
| Function: | |||
| Antioxidative | |||
| Number of residues | 2 |
Activity code | ao |
| Activity : | antioxidative |
|||
| Chemical mass | 294.3453 | Monoisotopic mass | 294.1574 | |
| EC50 : | 0.00 µM |
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| Bibliographic data: | |
| Authors | |
| Beermann C., Euler M., Herzberg J., Stahl B. | |
| Title | |
| Anti-oxidative capacity of enzymatically released peptides from soybean protein isolate. Eur. Food Res. Technol., 229 (2009), 637–644. | |
| Year | Source |
| 2009 | Journal |
| Additional information: |
| BIOPEP-UWM database of bioactive peptides SMILES: [H][C@](N)(CC(C)C)C(=O)N[C@@]([H])(Cc1ccc(O)cc1)C(O)=O InChI=1S/C15H22N2O4/c1-9(2)7-12(16)14(19)17-13(15(20)21)8-10-3-5-11(18)6-4-10/h3-6,9,12-13,18H,7-8,16H2,1-2H3,(H,17,19)(H,20,21)/t12-,13-/m0/s1 InChIKey=LHSGPCFBGJHPCY-STQMWFEESA-N The synthetic peptide analogue in a concentration of 3,4 mM revealed significant radical scavenging properties of 18.3%. Peptide obtained by hydrolysis of a soybean protein isolate (Danone Research, Friedrichsdorf, Germany) by use of trypsin. Found in hydrolysates of sardine muscle proteins. Matsufuji H., Matsui T., Seki E., Osajima K., Nakashima M., Osajima Y., 1994, Angiotensin I-converting enzyme inhibitory peptides in an alkaline proteinase hydrolysate derived from sardine muscle. Biosci. Biotech. Biochem., 58, 2244-2245 Found in amaranth proteins: Barba de la Rosa A. P., Barba Montoya A., Martínez-Cuevas P., Hernández-Ledesma B., León-Galván M. F., De León-Rodríguez A., González C., 2010, Tryptic amaranth glutelin digests induce endothelial nitric oxide production through inhibition of ACE: antihypertensive role of amaranth peptides. Nitric Oxide, 23, 106-111 Found in bovine collagen hydrolysate: Herregods G., Van Camp J., Morel N., Ghesquière B., Gevaert K., Vercruysse L., Dierckx S., Quanten E., Smagghe G., 2011, Angiotensin I-converting enzyme inhibitory activity of gelatin hydrolysates and identification of bioactive peptides. J. Agric. Food Chem., 59, 552-558 Inhibitor of Angiotensin-Converting Enzyme (ACE) (EC 3.4.15.1) (MEROPS ID: M02-001) according to the AHTPDB database; the BindingDB database; the BIOPEP-UWM database of bioactive peptids (ID 3381); the BRENDA database; the ChEMBL database; the EROP-Moscow database; the PubChem database Inhibitor of Renin (EC 3.4.23.15) (MEROPS ID A01.007) according to the BIOPEP-UWM database of bioactive peptides (ID 9470) Bitter peptide according to the BIOPEP-UWM database of sensory peptides and amino acids (ID 482) |
| Database reference: |
| ACToR: ID 968-21-8 AHTPDB: ID 1096, 1173, 1354, 1358, 1361, 1408, 1976, 2958, 3053, 3055, 3178, 3387, 3520, 3856, 3993, 4099, 4717, 5163, 5546, 5613, 5773, 6174, 6365 BindingDB: ID 50348865 BioPepDB: ID biopep00936 BIOPEP-UWM database of bioactive peptides: ID 3381; 9470 BIOPEP-UWM database of sensory peptides and amino acids: ID 482 BRENDA: Ligand Leu-Tyr ChEBI: ID 73591 ChEMBL: ID CHEMBL56099 ChemIDplus: ID 968-21-8 ChemSpider: ID 63589 |