## 3 Results
### In Silico Molecular Docking and Simulation Studies  
According to in silico molecular docking and simulation studies, eight hydrogen bonds and a \(\pi\)-\(\pi\) stacking interaction were formed between C2 and the crystal structure of 1 EVE. The interactions between the ligand and the enzyme, bonds formed and bond lengths are summarized in Table 3. The molecular interaction between luteolin-7-glucose (C2) and acetylcholinesteraseies is shown in Scheme 1.  
\begin{table}
\begin{tabular}{c c c c c c c} \hline \hline
**Test** & & & & & & \\
**Samples** & _E. coli_ & _K. pneumoniae_ & _P. aeruginosa_ & _P. mirabilis_ & _S. aureus_ & _E. faecalis_ \\ \hline C1 & 800 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & 25 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & \(\geq\)1600 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & \(\geq\)1600 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & 3.12 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & 6.25 \(\mathrm{\SIUnitSymbolMicro g}\)/mL \\ \hline C2 & \(\geq\)1600 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & 25 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & \(\geq\)1600 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & 3.12 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & 3.12 \(\mathrm{\SIUnitSymbolMicro g}\)/mL \\ \hline Sulfamerazine & \(\geq\)1600 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & \(\geq\)1600 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & \(\geq\)1600 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & 6.25 \(\mathrm{\SIUnitSymbolMicro g}\)/mL & 3.12 \(\mathrm{\SIUnitSymbolMicro g}\)/mL \\ \hline \hline \end{tabular}  
C1; Apigenin-7-glucose, C2; Luteolin-7-glucose.  
\end{table}
Table 1: Antimicrobial activities of components.  
\begin{table}
\begin{tabular}{c c c c} \hline \hline
**Test Material** & **\%** & **\%** & **\%** \\
**(100 \(\mathrm{\SIUnitSymbolMicro g}\)/mL)** & **Acetylcholinesterase** & **Butyrylcholinesterase** & **Tyrosinase** \\
**Inhibition** & **Inhibition** & **Inhibition** & **Inhibition** \\ \hline C1 & 30 \(\pm\) 3 & 13 \(\pm\) 4 & 24 \(\pm\) 1.1 \\ \hline C2 & 65 \(\pm\) 2 & 36 \(\pm\) 3 & 32 \(\pm\) 2.4 \\ \hline KA & - & - & 92 \(\pm\) 1.2 \\ \hline DH & 84 \(\pm\) 3 & 92 \(\pm\) 2 & - \\ \hline \hline \end{tabular}  
C1; apigenin-7-glucose, C2; luteolin-7-glucose, KA: kojic acid (positive control), DH: donepez1 hydrochloride (positive control).  
\end{table}
Table 2: Percentage inhibitory effect of C1 and C2.  
\begin{table}
\begin{tabular}{c c c c} \hline \hline
**Ligand-Enzyme** & **Enzyme Residues** & **Ligand Interaction Site** & **Distance (A\({}^{\text{\SIUnitSymbolMicro g}}\))** & **Interaction** \\ \hline C2-1 EVE & PHE288 (NH\({}_{2}\)) & 4-Oxo of benzopyran & 2.26 & H-bond \\ \hline C2-1 EVE & ARG289 (C=O) & 5-OH of benzopyran & 2.64 & H-bond \\ \hline C2-1 EVE & SER286 (C=O) & 5-OH of benzopyran & 2.63 & H-bond \\ \hline C2-1 EVE & SER286 (C=O) & 3-OH of glucose & 2.41 & H-bond \\ \hline C2-1 EVE & ASP72 (CO-OH) & 3-OH of phenyl & 1.71 & H-bond \\ \hline C2-1 EVE & ASP72 (CO-OH) & 4-OH of phenyl & 1.94 & H-bond \\ \hline C2-1 EVE & ASP285 (CO-OH) & 4-OH of glucose & 1.59 & H-bond \\ \hline C2-1 EVE & ASP285 (CO-OH) & 5-OH of glucose & 1.90 & H-bond \\ \hline \hline \end{tabular}  
C2-1 EVE & TYR334 (Ph) & Benzene of 2- (3, 4-dihydroyphenyl) & 3.67 & \(\pi\)-\(\pi\) stacking \\ \end{tabular}  
\end{table}
Table 3: The interactions between the ligand and the enzyme, bonds formed and bond length.