## Materials and Methods
### Biochemical Analysis  
To assess protein content, the Bradford assay [44] was performed in a 96-well flat-bottom plate to quantify soluble protein. Briefly, 190 uL of Bradford reagent (Comassie Blue G-250 in methanol, H\({}_{3}\)PO\({}_{4}\), and ultrapure water) was added to each well along with 10 uL of each sample extract or standards. The absorption was read at 595 nm (microplate reader; BioRad, Benchmark, Los Alamitos, CA, USA) indicating protein-binding to Coomassieie Brilliant Blue G-250. A calibration curve was constructed using bovine serum albumin as protein standard (0-2 mg\(\cdot\)mL\({}^{-1}\) BSA, Sigma, Saint Louis, MO, USA). Acetylcholinesteraseerase (AchE) activity was determined with a modified method initially proposed by [PERSON] et al. [45] and adapted to 96-well plates [46]. Briefly, 25 uL of brain extract or assay buffer (for blanks) was added to two microplate wells, and then 250 uL of an acetylthiocholine fresh reaction mixture (50 mM phosphate buffer 8.0, 75 mM acetylthiocholine iodide solution and 1.0 mM 5,5\({}^{\prime}\)-dithiobis (2-nitrobenzoic acid)) was added into each microplate well. The microplate was gently shaken for 30 s and the absorbance was read (415 nm) every minute for 10 min. AchE activity was expressed as nmol\(\cdot\)min\({}^{-1}\cdot\)mg\({}^{-1}\) protein (after normalization using samples' crude protein content). Catalase (CAT) activity was assessed using a method adapted from [PERSON] and [PERSON] [47], which measures the rate of removal of H\({}_{2}\)O\({}_{2}\). Briefly, 20 uL of sample extract, 100 uL of assay buffer (100 mM KH\({}_{2}\)PO\({}_{4}\), pH 7.0), 30 uL of methanol, and 20 uL of H\({}_{2}\)O\({}_{2}\) (as substrate) were shaken in darkness for 20 min at ambient temperature. Then, 30 uL of 10 M KOH and 30 uL of 34.2 M Purpald (prepared in 0.5 M KCl) were added and incubated for 10 min in the same conditions. To finalize the reaction, 10 uL of 65.2 mM potassium periodate (prepared in 0.5 M KOH) was added, and the absorbance was read at 540 nm wavelength. A blank and a positive control were performed in each sample batch in order to validate the method. Eight standards from 4.25 mM formaldehyde were prepared with concentrations ranging from 0-100 uM to perform a calibration curve. Formaldehyde concentration in the sample was determined using the equation obtained from linear regression of the standard curve, formaldehyde (uM) = ((sample absorbance - y intercept)/slope) \(\times\) (0.17/0.02), where 0.17 corresponds to the extinction coefficient and 0.02 corresponds to the total volume in each well plate. Then, CAT activity was calculated assuming that one unit is the amount of enzyme that causes the formation of 1.0 nmol of formaldehyde per minute. Thus, CAT activity was expressed in nmol\(\cdot\)min\({}^{-1}\cdot\)mg\({}^{-1}\) protein = (uM of sample/20 min) \(\times\) sample dilution \(\times\) protein content. Superoxide dismutase (SOD) activity was determined using a spectrophotometric method described in detail elsewhere [48]. Briefly, to each microplate well, 10 uL of sample or SOD standard (Sigma-Aldrich, Germany) and a mixture of 200 uL of 50 mM phosphate buffer (pH 7.4), 10 uL of 3 mM xanthine, 10 uL of 0.75 mM nitroblue tetrazolium (NBT), and 10 uL of 100 muL xanthine oxidase solution (XOD) were added. A negative control (without sample or SOD standard) was also assayed. Sample absorbance was read at 540 nm every minute for 15 min. SOD activity was expressed as inhibition percentage (% SOD inhibition) calculated with the following formula: (Abs\(\cdot\)min\({}^{-1}\) of negative control - Abs\(\cdot\)min\({}^{-1}\) of sample)/(Abs\(\cdot\)min\({}^{-1}\) of negative control) \(\times\) 100. To assess lipid peroxidation (LPO), a procedure was adapted according to the thiobarbituric acid reactive species (TBARS) principle [49].