Your browser doesn't support javascript.
loading
Montrer: 20 | 50 | 100
Résultats 1 - 1 de 1
Filtre
Ajouter des filtres








Gamme d'année
1.
Electron. j. biotechnol ; 37: 18-24, Jan. 2019. tab, ilus, graf
Article Dans Anglais | LILACS | ID: biblio-1049076

Résumé

BACKGROUND: The 11S globulin from amaranth is the most abundant storage protein in mature seeds and is well recognized for its nutritional value. We used this globulin to engineer a new protein by adding a four valinetyrosine antihypertensive peptide at its C-terminal end to improve its functionality. The new protein was named AMR5 and expressed in the Escherichia coli BL21-CodonPlus(DE3)-RIL strain using a custom medium (F8PW) designed for this work. RESULTS: The alternative medium allowed for the production of 652 mg/L expressed protein at the flask level, mostly in an insoluble form, and this protein was subjected to in vitro refolding. The spectrometric analysis suggests that the protein adopts a ß/α structure with a small increment of α-helix conformation relative to the native amaranth 11S globulin. Thermal and urea denaturation experiments determined apparent Tm and C1/2 values of 50.4°C and 3.04 M, respectively, thus indicating that the antihypertensive peptide insertion destabilized the modified protein relative to the native one. AMR5 hydrolyzed by trypsin and chymotrypsin showed 14- and 1.3-fold stronger inhibitory activity against angiotensin I-converting enzyme (IC50 of 0.034 mg/mL) than the unmodified protein and the previously reported amaranth acidic subunit modified with antihypertensive peptides, respectively. CONCLUSION: The inserted peptide decreases the structural stability of amaranth 11S globulin and improves its antihypertensive activity.


Sujets)
Peptides/métabolisme , Protéines/métabolisme , Globulines/métabolisme , Antihypertenseurs/métabolisme , Graines , Température , Milieux de culture , Amaranthus , Stabilité protéique , Composés phytochimiques
SÉLECTION CITATIONS
Détails de la recherche