Summary and Conclusion

Using in silico analysis, it was found that all three storage proteins, 2S albumin, 7S

globulin and 11S globulin of sesame seeds exhibited antihypertensive activity upon subject

to enzyme actions of pepsin, trypsin, chymotrypsin and thermolysin.

The protein concentration of the extracted crude sesame seed protein is 2.023

mg/mL. The crude protein isolated was determined to possibly contain the 7S and 11S

globulin based on the SDS-PAGE profile. The analysis showed intense bands of 11S

globulin with estimated acidic (27-32 kDa) and basic (19.9 kDa) subunits and 7S globulin

of 40-50 kDa. Further purification was made using ammonium sulfate precipitation,

dialysis and gel filtration chromatography. The storage protein of sesame seed, 11S

globulin, is the probable component isolated in the partially purified protein containing

acidic (29-31 kDa) and basic (20 kDa) subunits as shown from the SDS-PAGE profile.

Crude and partially purified proteins were used for protein digestion, ACE assay

and antimicrobial assay. Enzymes (pepsin, thermolysin, trypsin and chymotrypsin) were

used to digest the samples for 2, 4, 12 and 24 hours. Densitometric analysis of each sample

showed increasing degree of digestion of the proteins as time increases.

In the ACE assay, all samples exhibited varying potential ACE inhibitory activities

with the 4-hour crude digest as the highest among all of the samples. This reveals that more

potential ACE inhibitory peptides have been released at 4-hour digest. Also, results suggest