| Products/Services Used | Details | Operation |
|---|---|---|
| Peptide Synthesis | Okara by-product was provided by Nutre (Aveiro, Portugal), Alcalase 2.4 L FG (a density of 1.17 g/mL) was ordered from Novozymes (Bagsvaerd, Denmark), Cynara cardunculus extract (a density of 1.14 g/mL) was obtained from Formulab (Maia, Portugal). Trolox, 2,2′-amino-di (2-ethyl-benzothiazoline sulfonic acid-6) ammonium salt (ABTS), o-Phthalaldehyde, o-Phthalic dicarboxaldehyde, Benzene-1,2-dicarboxaldehyde (OPA), and amino acid standards were purchased from Sigma Chemical Co. (St. Louis, MO, USA). Proteins standards (Thyroglobulin, 669 kDa; Ferritin, 440 kDa; Aldolase, 158 kDa; Conalbumin, 75 kDa; Ovalbumin, 43 kDa; Carbonic anhydrase, 29 kDa; Ribonuclease A, 13.7 kDa; Aprotinin, 6.5 kDa) were purchase from GE Healthcare (USA) and an antihypertensive peptide with the sequence KGYGGVSLPEW (99.7%) (1.2 kDa) was ordered from GenScript (China). All other reagents and chemicals used were of analytical grade. | Get A Quote |
Enzymatic hydrolysis of dried okara (autoclaved and non-autoclaved) with Alcalase (AL) and Cynara cardunculus extract (CY) was studied, assessing the impact of heat treatment and hydrolysis on potential antioxidant and antihypertensive activities of final hydrolysates. This study showed that the thermal treatment (sterilization at 121 °C, 1 atm and 15 min) facilitated the enzymatic access to substrate and increased the degree of hydrolysis (DH), especially for AL (37.9%) when compared to CY (3.6%). The antioxidant activity of dried Okara (either autoclaved or not) when hydrolysed with AL was higher (4.2 mg Trolox/mL) than that observed for CY. Additionally, the potential ACE-inhibitory activity was h... More
