## 2 Materials and Methods
### Bioactive Compounds
Then, the mix was vortexed and read on a UV-Vis spectrophotometer (Thermo Fisher Scientific, G10S model, MA, USA) at 412 nm using a quartz cell. The results were expressed in mM equivalent of GSH mL\({}^{-1}\) min\({}^{-1}\) total protein\({}^{-1}\). The measurement of the enzymatic activity of ascorbate peroxidase was carried out according to what was established by [PERSON] and [PERSON] [30]. The measurement was made in two moments (at time 0 (T0) and at time 1 (T1)). At T0, a mix of 100 \(\upmu\)L of extract, 500 \(\upmu\)L of ascorbate (10 mg L\({}^{-1}\)), 400 \(\upmu\)L of H\({}_{2}\)SO\({}_{4}\) (5%), and 1 mL of H\({}_{2}\)O\({}_{2}\) (100 mM) were placed in a test tube and then vortexed for 30 s. The absorbance was measured in a UV-Vis spectrophotometer (Thermo Fisher Scientific, G10S model, MA, USA) at 266 nm with a quartz cell. At T1, 100 \(\upmu\)L of extract, 500 \(\upmu\)L of ascorbate (10 mg L\({}^{-1}\)), and 1 mL of H\({}_{2}\)O\({}_{2}\) (100 mM) were added to the previous mixture and vortexed for 1 min at a temperature of 26 \({}^{\circ}\)C. To stop the reaction, 400 \(\upmu\)L of H\({}_{2}\)SO\({}_{4}\) (5%) was added, and the absorbance was measured. Ascorbate peroxidase determination is based on the quantification of the ascorbate oxidation rate by means of the absorbance difference (T0 - T1). The enzymatic activity was expressed as U per total proteins (mg g\({}^{-1}\)), where U is equal to \(\upmu\)mol QE of oxidized ascorbate per milliliter per minute. The glutathione peroxidase (QE 1.11.1.9) enzyme was determined with the method modified by [PERSON] and [PERSON] [31] and adapted by [PERSON] et al. [29] using H\({}_{2}\)O\({}_{2}\) as the substrate. A mix of 200 \(\upmu\)L of extract, 400 \(\upmu\)L of GSH (0.1 mM), and 200 \(\upmu\)L of Na\({}_{2}\)HPO\({}_{4}\) (0.067 M) were placed in a test tube. The mixture was preheated in a water bath at 25 \({}^{\circ}\)C for 5 min, then 200 \(\upmu\)L of H\({}_{2}\)O\({}_{2}\) (1.3 mM) was added to start the catalytic reaction for 10 min at a temperature of 26 \({}^{\circ}\)C. The reaction was stopped by the addition of 1 mL of 1% trichloroacetic acid. The mixture was placed in an ice bath for 30 min and then centrifuged at 1008\(\times\)\(g\) for 10 min at 4 \({}^{\circ}\)C. To assess the glutathione peroxidase, 480 \(\upmu\)L of the supernatant, 2.2 mL of Na\({}_{2}\)HPO\({}_{4}\) (0.32 M), and 320 \(\upmu\)L of 5,5-dithio-bis-2-nitrobenzoic acid dye (DTNB) of 1 mM were placed in a test tube. The absorbance was measured by a UV-Vis spectrophotometer (Thermo Fisher Scientific, G10S model, MA, USA) at 412 nm with a quartz cell. The results are expressed in U per total proteins (mg g\({}^{-1}\)), where U is equal to mM equivalent of GSH per milliliter per minute. The determination of superoxide dismutase (QE 1.15.1.1) enzymatic activity was carried out using the SOD Cayman 706002(r) kit. A mix of 20 \(\mu\)L of extract, 200 \(\mu\)L of the radical detector (tetrazolium salt), and 20 \(\mu\)L of xanthine oxidase solution were placed in a microplate. The microplate was covered with a transparent cover (kit), stirred for 10 s, and then incubated at 26 \({}^{\circ}\)C for 30 min. The absorbance was then measured at a length of 450 nm using a plate reader (BioTek, ELx808 model, VT, USA). The principle of the test is based on the use of a tetrazolium salt for the detection of superoxide radicals generated by xanthine oxidase and hypoxanthine. One unit of SOD is defined as the amount of enzyme needed to exhibit 50% dismutation of the superoxide radical. The results are expressed in U mL\({}^{-1}\) by the total proteins (mg g\({}^{-1}\)). The catalase (QE 1.11.1.6) enzymatic activity was quantified by the spectrophotometric method used by [PERSON] et al. [32]. The measurement was carried out in two steps (at time 0 (T0) and at time 1 (T1)).