## 2 Materials and Methods
### Analytical Methods  
**Inhibition of AChE and BChE**  
First, the dry mass of each sample was adjusted to 0.23 mg/mL using Tris-HCl buffer (50 mM, pH 8.0), and all reagent solutions were prepared in the same Tris-HCl buffer. Enzyme activities were measured in a 96-well microplate reader (Tecan Sunrise, Grodig, Austria) using a modified spectrophotometric method as described in [PERSON] et al. [40; 41] except that the test solution was composed of 0.035 mL of the studied sample, 0.035 mL of ATChI (or BTCh) solution, 0.08 mL of Tris-HCl buffer, 0.02 mL of AChE (or BChE) solution, and 0.175 mL of 0.3 mM DTNB solution. The absorbance (405 nm, 22 \({}^{\circ}\)C) was read after 30 (AChE) or 10 min (BChE). In blank (negative) samples, Tris-HCl buffer replaced the studied sample. Spontaneous hydrolysis of the substrate was monitored using blank samples composed of 0.175 mL DTNB, 0.035 mL ATChI (or BTCh), and 0.135 mL Tris-HCl buffer. The false-positive effect was verified according to [PERSON] et al. [42]: after the addition of ATChI (BTCh), buffer, and the enzyme, the sample was left for 30 (AChE) or 10 min (BChE). Then, the test solution was added, followed by direct addition of DTNB and measurement of the absorbance. Each solution was analyzed in eight replicates. The inhibitory activity was expressed as proposed previously [43] using serine equivalents (nM serine) required to exert the same inhibitory activity. In short, the anticolinesterase activities of 12 solutions of serine at 7.1 nM-7.27 uM were measured followed by the production of the calibration curves. **Preparation of samples for the antioxidant activity testing. ** Each studied sample was finely ground in the laboratory mortar to obtain homogeneity, and deionized water was added to obtain 0.23 g of the dry mass/mL. **Antioxidant activity (ABTS)**  
The original method of [PERSON] et al. [44] was used with slight modifications. All reagents (prepared in 5 mM of phosphate buffer, pH 7.0) were present in the reaction mixture at final concentrations: ABTS 0.15 mM, myoglobin 0.0025 mM, and H\({}_{2}\)O\({}_{2}\) 0.375 mM. The studied sample (0.03 cm\({}^{3}\)) was mixed with 0.03 cm\({}^{3}\) of the buffer and 0.28 cm\({}^{3}\) of ABTS/myoglobin reagent followed by the addition of 0.023 cm\({}^{3}\) of H\({}_{2}\)O\({}_{2}\) to start the reaction. Absorbance was read every 1 min (700 nm, 20 \({}^{\circ}\)C) using a 96-well microplate reader (Tecan Sunrise, Grodig, Austria) for 30 min, and the time of 15 min of the reaction was taken for calculations of the TEAC value (all samples reached plateau). Blanks containing buffer instead of samples were simultaneously run in order to subtract the background. For calibration curve (y = 20.171x + 0.822), 15 Trolox solutions (water/ethanol 1:1 \(v\)/\(v\); 0.6 mmol\(\cdot\)dm\({}^{-3}\)-0.03 mmol\(\cdot\)dm\({}^{-3}\)) were used as an antioxidative standard. Total antioxidant activity was expressed in equivalent Trolox concentration (TEAC value) that inhibited the increase in the absorbance equally to the studied solution. All samples were run in eight replicates. Antioxidant activity (DPPH)  
The method of [PERSON] et al. (2018) was used with some minor modifications. A volume of 0.01 cm\({}^{3}\) of the sample was mixed with 0.1 cm\({}^{3}\) of DDI water and 0.2 cm\({}^{3}\) of DPPH solution in methanol (0.06 mmol\(\cdot\)dm\({}^{-3}\)). Absorbance was read at 515 nm every min (20 \({}^{\circ}\)C, microplate reader, Tecan Sunrise, Austria) until 20 min of the reaction, and the time of 10 min of the reaction was taken for calculations of the TEAC value (plateau). Blanks containing the test sample or buffer were simultaneously run followed by subtraction of background absorbances of studied samples. For calibration curve (y = 18,823x + 0.443), 15 Trolox solutions (water/ethanol 1:1 \(v/v\); 0.6 mmol\(\cdot\)dm\({}^{-3}\)-0.03 mmol\(\cdot\)dm\({}^{-3}\)) were used as an antioxidative standard.