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Abstract

Bioactive peptides are produced from soy milk protein hydrolysis using trypsin. The research began with the preparation and separation of soy milk protein, followed by fractionation using ammonium sulphate, protein hydrolysis, and SDS-PAGE analysis of protein hydrolysates. Fractions exhibiting the highest degree of hydrolysis were further fractionated by SPE and tested to determine the antibacterial activity Staphylococcus aureus and Escherichia coli. The peptide sequence of the active peptide as an antibacterial was identified, employing LC-HRMS. The mode of action between active peptides and bacterial membran was analysed using molecular dynamics (MD) simulation. The findings displayed that F15 contained the highest protein concentration before hydrolyzed, which was 2774.52 ppm, and the degree of hydrolysis of F15 was recorded at 36%. Meanwhile, the antibacterial activity test against S. aureus and E. coli bacteria showed that the FP1 exhibited the highest inhibition zone, measuring 7.19 mm, with a MIC of 8.81 ppm. Furthermore, SEM results showed that E. coli bacteria treated with FP1 changed the morphology of the cell membrane. HRMS analysis of SMF1 identified two peptides: IITSLGVK (P1) and AKEMHIDAANTREYSIDHQSSNMDSDVAASHIDTV (P2). MD simulation results indicate that peptides P1 and P2 successfully interacted with the lipid membrane head groups of E. coli bacteria. Compared to peptide P2, peptide P1 demonstrated greater complex stability and cohesiveness.

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Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.

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