## 2 Results and Discussion
### In silico Predictions of potential antioxidative peptides from linear organs hydrolysates.
\begin{table}
\begin{tabular}{c c c c} \hline \hline
**Sample** & **Peptide Sequence** & **Name of Peptide Appears in the Data Base** & **Bioactive Sequence** & **Location of Fragmentation** \\ \hline  & ACE inhibitor from Alaskan pollack skin & GP & (1–2), (4–5), (7–8) \\  & ACE inhibitor & GR & (10–11) \\  & ACE inhibitor & MG & (12–13) \\  & ACE inhibitor & TG & (9–10) \\  & ACE inhibitor & PG & (3–4) \\  & ACE inhibitor from wheat gladin & GPP & (1–3) \\  & ACE inhibitor & PT & (8–9) \\  & ACE inhibitor & PP & (2–3) \\  & ACE inhibitor & RG & (6–7) \\ GPGGPGPGM & ACE inhibitor from Alaskan pollack skin & GP & (1–2), (4–5), (6–7) \\  & ACE inhibitor & GM & (8–9) \\  & ACE inhibitor & GG & (3–4) \\  & ACE inhibitor & PG & (2–3), (5–6), (7–8) \\ APDMAFPR & ACE inhibitor & FP & (6–7) \\  & ACE inhibitor & PR & (7–8) \\  & AFP & (5–7) \\  & ACE inhibitor & AF & (5–6) \\  & ACE inhibitor & AP & (1–2) \\  & ACE inhibitor & DM & (3–4) \\ GGFPGG & ACE inhibitor & FP & (4–5) \\  & ACE inhibitor from Alaskan pollack skin & GP & (7–8) \\  & ACE inhibitor & GF & (3–4) \\  & ACE inhibitor & GG & (2–3), (6–7) \\  & ACE inhibitor & PG & (5–6), (8–9) \\ GPGMMGP & ACE inhibitor & GM & (4–5) \\  & ACE inhibitor & MG & (6–7) \\  & ACE inhibitor & PG & (3–4) \\  & ACE inhibitor & MM & (5–6) \\ GPPGASGPLGIAGSM & ACE inhibitor from Alaskan pollack skin & GPL & (7–9) \\  & ACE inhibitor from Alaskan pollack skin & PLG & (8–10) \\  & ACE inhibitor from Alaskan pollack skin & GP & (1–2), (7–8) \\  & ACE inhibitor from Alaskan pollack skin & PL & (8–9) \\  & ACE inhibitor from soy hydrolysate & IA & (11–12) \\  & ACE inhibitor & GI & (10–11) \\  & ACE inhibitor & GA & (4–5) \\  & ACE inhibitor & AG & (12–13) \\  & ACE inhibitor & GS & (13–14) \\  & ACE inhibitor & SG & (6–7) \\  & ACE inhibitor & LG & (9–10) \\  & ACE inhibitor & PG & (3–4) \\ ACE inhibitor from wheat gladin & GPP & (1–3) \\  & ACE inhibitor & PP & (2–3) \\  & ACE inhibitor & LGI & (9–11) \\  & ACE inhibitor & SGP & (6–8) \\ GPSGPP & ACE inhibitor from Alaskan pollack skin & GP & (1–2), (4–5), (7–8) \\  & ACE inhibitor & SG & (3–4) \\  & ACE inhibitor & PG & (6–7) \\  & ACE inhibitor from wheat gladin & GPP & (6–7) \\  & ACE inhibitor & PP & (4–6) \\  & ACE inhibitor & PP & (5–6) \\  & ACE inhibitor & SGP & (3–5) \\ \hline \hline \end{tabular} G—Glycine, P—Proline, Q—Glutamine, W—Tryptophan, L—Leucine, D—Aspartic acid, F—Phenylalanine, T—Trreonine, M—Melthionine, A—Alanine, R—Arginine, S—Serine, I—Isooleucine, K—Lysine.  
\end{table} 
Table 4: _Cont._It is evident that all active fragments are either dipeptides or tripeptides. Presence of hydrophobic amino acid residues is the crucial structural feature for ACE inhibitory potential [28]. Hydrophobic amino acids including P (proline), M (methionine), L (leucine), I (isoleucine), F (phenylalanine), and A (alanine) were identified in the predicted potent amino acid sequences. In addition, positioning of hydrophobic amino acids or branched chain amino acid residues at the C-terminal of the sequence and N-terminal aliphatic amino acids are some of the major structural features which favors the ACE binding function [29]. These characteristic features were exhibited in predicted sequences of flower and internal organs. The highest number of potential ACE inhibitory dipeptides, and tripeptides (17) were found in sequence GPPGASPPLGIAGSM from flower. Furthermore, all the other predicted ACE inhibitory peptides shared similar structural features, including the presence of hydrophobic amino acid residues in the sequence. In addition, occurrence of consecutive proline-proline dipeptide in the sequence is markedly effective for antihypertensive activities [7]. The effect of proline towards the ACE inhibitory activity associates with its imidazole ring that exhibits strong interaction with the amino acid residues at the active centers of ACE [30].