Vansiri Ngamsiriudom.. Cationic peptides derived from rice protein hydrolysate for antibacterial capacity. Master's Degree(Food Science). Kasetsart University. Office of the University Library. : Kasetsart University, 2022.
Cationic peptides derived from rice protein hydrolysate for antibacterial capacity
Abstract:
Antimicrobial peptides (AMPs) can be classified based on amino acid concentration into proline-, tryptophan-, arginine-, histidine-, lysine-, and glycinerich AMPs. In this study, the globulin and glutelin fraction of rice protein from germinated rice (GR) was interested as various amino acids were surged during germination. Data from MALDI-MSI indicated that various hydrophobic amino acids increased around 2.4-16.1 folds especially at 96 h. The globulin fraction of GR and rice bran (RB) showed the highest % inhibition against B. cereus (60.8%, 57.9%) and V. cholerae (55.6%, 50.6%). The glutelin fraction of commercial rice protein (CR) inhibited only B. cereus (51.7%). After fractionated by ion exchange chromatography, the unbound fraction of GR globulin showed the highest % inhibitory againt V. parahaemolyticus and V. cholerae (20.7%, 24.4%). The inhibitory effect of rice protein hydrolysates depended on concentration and type of amino acids, sequence, and hydrophobicity of peptide rather than protein charges. In a food model, the unbound fraction of GR globulin had the highest inhibitory effect against V. cholerae (0.51-2.47 log reduction) followed by cationic fraction of GR globulin (0.21-1.71 log reduction). The unbound fraction of RB globulin exhibited the highest inhibitory effect against V. parahaemolyticus (0.26-1.61 log reduction) followed by cationic fraction of GR globulin (0.29-1.15 log reduction). The peptide sequences that exhibited the highest hydrophobicity were TAPEEQIREL (hydrophobicity 6.8), followed by ASEEQVREL (5.5) and VEPVKEEQTQ (5.1). The peptides concentration used (100 µg/mL) was much lower than the consumers unacceptable bitter taste concentration ever reported.
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