BIOPEP-UWM: Report
| ID | 7873 |
| 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: N[C@H](C(=O)N[C@H](C(=O)O)Cc1ccc(cc1)O)[C@H](CC)C InChI=1S/C15H22N2O4/c1-3-9(2)13(16)14(19)17-12(15(20)21)8-10-4-6-11(18)7-5-10/h4-7,9,12-13,18H,3,8,16H2,1-2H3,(H,17,19)(H,20,21)/t9-,12-,13-/m0/s1 InChIKey: MUFXDFWAJSPHIQ-XDTLVQLUSA-N The synthetic peptide analogue in a concentration of 3,4 mM revealed significant radical scavenging properties of 16,7%. 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 Binding DB database; the BIOPEP-UWM database of bioactive peptides (ID 7873); the BRENDA database; the ChEMBL database; the EROP-Moscow database; the PlantPepDB database |
| Database reference: |
| AHTPDB: ID 1070; 1098; 1150, 1287, 1348, 1353, 1373, 1377, 1411, 1440, 1495, 1510, 1818, 1855, 1903, 1934, 1948, 2583, 2734, 2778, 2956, 2988, 2992, 3064, 3166, 3171, 3197, 3504, 3781, 3962, 4083, 4226, 4248, 4253, 4259, 4450, 4487, 4652, 4947, 4955, 4956, 4957, 5156, 5598, 5661, 6140, 6143, 6176, 6263, 6268, 6282, 6367, 6879 Binding DB: ID 50038069 BioPepDB: ID biopep00619 BIOPEP-UWM database of bioactive peptides: ID 3383 BRENDA: Ligand Ile-Tyr ChEBI: ID 74326 ChEMBL: ID CHEMBL91090 ChemSpider: ID 5730945 EROP-Moscow: ID E01439 FeptideDB: ID 3383; 7873 J-GLOBAL: ID 200907037450857360 Metabolights: ID MTBLC74326 Metabolomics Workbench: ID 71683 Nikkaji: ID J535.351C PlantPepDB: ID PPepDB_3792 PubChem: CID 7408194 SATPdb: ID satpdb18728 SureChEMBL: ID SCHEMBL4261778 ZINC: ID ZINC000004899517 |