## 3 Results and Discussion
### In Silico Analysis of the Isolated Major Protein from 'Senorita' Banana Extracts
\begin{table}
\begin{tabular}{c c c c c} \hline \hline \multirow{2}{*}{**Digestion Hours**} & \multicolumn{4}{c}{**ACE Inhibition (\%)**} \\ \cline{2-5}  & **Captopril** & **Crude** & **Partially Purified** & **Purified** \\ \hline
0 & 99.72 \(\pm\) 0.71 \({}^{\text{a}}\) & 85.20 \(\pm\) 6.80 \({}^{\text{b,b}}\) & 21.78 \(\pm\) 0.37 \({}^{\text{b,e,f,c}}\) & 21.74 \(\pm\) 2.69 \({}^{\text{b,c}}\) \\
3 & \(-\) & 28.03 \(\pm\) 3.63 \({}^{\text{c,b}}\) & 11.30 \(\pm\) 0.67 \({}^{\text{c,c}}\) & 29.14 \(\pm\) 0.99 \({}^{\text{c,b}}\) \\
4 & \(-\) & 33.60 \(\pm\) 4.75 \({}^{\text{c,d,b}}\) & 15.89 \(\pm\) 1.54 \({}^{\text{d,e,c}}\) & 31.25 \(\pm\) 0.91 \({}^{\text{c,d,b}}\) \\
12 & \(-\) & 33.73 \(\pm\) 2.79 \({}^{\text{c,d,b}}\) & 18.86 \(\pm\) 1.64 \({}^{\text{e,f,c}}\) & 34.39 \(\pm\) 0.11 \({}^{\text{d,e,b}}\) \\
24 & \(-\) & 41.07 \(\pm\) 2.25 \({}^{\text{d,b}}\) & 22.06 \(\pm\) 2.24 \({}^{\text{f,c}}\) & 36.73 \(\pm\) 2.35 \({}^{\text{e,b}}\) \\ \hline \hline \end{tabular}  
* The mean \(\pm\) SD values of three determinations in the column if followed by the same superscript letters are not significantly different at 5% level of significance using ordinary one-way ANOVA followed by [PERSON]’s test. The letters before the comma shows [PERSON]’s multiple comparison result in the given column while the letters after the comma shows [PERSON]’s multiple comparison result in the given row.  
\end{table} 
Table 2: ACE inhibition (%) of crude, partially purified and purified protein extracts at 0, 3, 4, 12, and 24 h of digestion *. Figure 4: Comparison of ACE inhibition (%) of crude, partially purified and purified protein extracts at different digestion hours. For the partially purified extract samples, the same trend in the activities of the crude extract samples was observed. However, the observed activities were found to be the lowest among the three sample groups. Table 2 shows that there was an observable significant three-fold decrease in the activity of the undigested crude sample when partially purified. Partial purification removed non-protein contaminants and unprecipitated proteins from the crude extract. The removal of these components, which might have ACE inhibitory activity, decreased significantly the activity of the undigested partially purified sample. On the other hand, the increase in the activity of the purified sample could be associated to the peptides inhibiting the ACE to have more effective interaction due to the decrease in the sample components that have prevented otherwise [32]. For the purified extract samples, there was an increase in activity starting from the undigested sample up to the 24-h digest. This trend was different to the other two sample groups. Purified samples were primarily composed of the major protein, as a result, the activities observed had only reflected the characteristic activity of the major protein. In silico analysis of the putative protein showed that enzymatic hydrolysis of the protein will release bioactive peptides that can inhibit ACE, thus, prolonging the hydrolysis of the protein through increased digestion period released more bioactive peptides resulting to an observable increase in activity. Determination of the Radical Scavenging Activity by 2,2-Diphenyl-1-picrylhydrazyl (DPPH) Assay as a Basis of Antioxidant Activity  
For the effect of digestion time on antioxidant activity of the protein extracts, a decrease in the activity of the partially purified and purified samples was observed as the digestion time was increased, whereas the activity of the crude samples continued to increase up to the four hour digestion time before it significantly decreased at the 12 h and 24 h digestion time (Figure 5).