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SITI NUR HIKMAH

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Abstrak (Bhs. Indonesia)

Penyakit infeksi masih menjadi penyebab utama tingginya angka kematian, sedangkan penggunaan antibiotik sebagai obat dapat berisiko memicu resistensi bakteri. Peptida antibakteri (AMPs) merupakan alternatif antibiotik alami yang lebih aman dan memiliki mekanisme kerja berbeda. Penelitian ini bertujuan mengetahui aktivitas antibakteri peptida hasil hidrolisis enzimatis kacang tunggak (Vigna unguiculata L. Walp.) menggunakan enzim tripsin serta mengidentifikasi urutan asam amino pada fraksi paling aktif. Peptida dipisahkan dengan kolom SPE-PEP, diuji aktivitas antibakterinya, kemudian fraksi terbaik dianalisis menggunakan LC-HRMS. Hasil penelitian menunjukkan bahwa derajat hidrolisis menggunakan tripsin sebesar 86%. Uji antibakteri menunjukkan bahwa fraksi 75 
memiliki aktivitas tertinggi terhadap S. aureus sebesar 2,10 mm dan fraksi 100 terhadap E. coli sebesar 1,79. Fraksi dengan aktivitas tertinggi mengandung 21 sekuens, diantaranya yaitu QQDEESQQEGVIVQLKR, NILEASFGSDYKEINR, MSSYIDSAFR, GQSNPFYFNSDR, EINRVLFGEGQQQQGEESQEEGVIVELKR, EGALLLPHYNSEAMVMLVVNEGEANAELVGVR, GVPYWIFNTGDEALATVTLLDTSSEDNQLDQSPR, ELNIFLDYVDINKGGLLLPHYNSK, NISEYPSVELVMEKPNGPVWR, NGLQMPSYSPYSQMIIAIQGK, KALSSSQNEPLNLR, KQTESYFVNAQPQQK, DASTGLHWTNLLKR, SGSPIYSNTLGR, AMVMLVMNR, QFSQGHVLLIPR, LAIPVNNPHK, NLNSQSFPALK, SSTQLQNLR, TKQIQNLENYRVVEFK, dan NPFYFSSNR.

Abtrak (Bhs. Inggris)

Infectious diseases remain one of the leading causes of high mortality, while the use of antibiotics as treatment carries the risk of promoting bacterial resistance. 
Antimicrobial peptides (AMPs) are a promising natural alternative to conventional antibiotics because they are considered safer and possess a different mechanism of action. This study aimed to evaluate the antibacterial 
activity of peptides produced through the enzymatic hydrolysis of cowpea (Vigna unguiculata L. Walp.) using trypsin and to identify the amino acid sequences present in the most active peptide fraction. The peptides were separated using an SPE-PEP column, their antibacterial activity was evaluated, and the most active fraction was subsequently analyzed by LC-HRMS. The results showed that the degree of hydrolysis achieved using trypsin was 86%. Antibacterial assays demonstrated that fraction 75 exhibited the highest activity against S. aureus, with an inhibition zone of 2.10 mm, whereas fraction 100showed the highest activity against E. coli, with an inhibition zone of 1.79 mm. The fraction with the highest antibacterial activity contained 21 peptide sequences, were identified as: QQDEESQQEGVIVQLKR, NILEASFGSDYKEINR, MSSYIDSAFR, GQSNPFYFNSDR, EINRVLFGEGQQQQGEESQEEGVIVELKR, EGALLLPHYNSEAMVMLVVNEGEANAELVGVR, GVPYWIFNTGDEALATVTLLDTSSEDNQLDQSPR, ELNIFLDYVDINKGGLLLPHYNSK, NISEYPSVELVMEKPNGPVWR, NGLQMPSYSPYSQMIIAIQGK, KALSSSQNEPLNLR, KQTESYFVNAQPQQK, DASTGLHWTNLLKR, SGSPIYSNTLGR, AMVMLVMNR, QFSQGHVLLIPR, LAIPVNNPHK, NLNSQSFPALK, SSTQLQNLR, TKQIQNLENYRVVEFK, and NPFYFSSNR.

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