Analisis In Silico Struktur Enzim Endo-1,4-Β-Glucanase Pada Bakteri Fervidobacterium Nodosum dan Bacillus Subtilis

In Silico Analysis of Endo-1,4-β-Glucanase Enzyme Structure on Fervidobacterium nodosum and Bacillus subtilis

Enzim endo-1,4-β-glucanase yang banyak ditemukan pada organisme hipertermofilik dan termofilik dapat menghidrolisis ikatan glikosidik-β-1,4 dalam selulosa menjadi glukosa dengan aktivitas degradasi yang berbeda. Penelitian ini bertujuan untuk mengetahui struktur protein dan similaritas enzim endo 1,4-β-glucanase bakteri Fervidobacterium nodosum dan Bacillus subtilis yang diisolasi dari sumber mata air panas dan fermentasi pakan ternak, berdasarkan urutan sekuen asam amino dan struktur tiga dimensi. Penelitian ini merupakan penelitian deskriptif menggunakan sekuen asam amino kedua enzim yang diperoleh dari situs National Center of Biotechnology Information (NCBI) melalui data mining, kemudian dianalisis similaritasnya dengan aplikasi Clustal Omega untuk menyejajarkan urutan protein yang berbeda serta memperoleh area lestari. Selanjutnya struktur tiga dimensi kedua enzim yang diperoleh dari Template pada SWISS MODEL workspace dianalisis secara deskriptif. Hasil penelitian menunjukkan similaritas enzim endo 1,4-β-glucanase pada kedua bakteri sebesar 21,72%. Empat motif yang ditemukan pada struktur tiga dimensi diduga mempengaruhi perubahan aktivitas katalitik, stabilitas dan pembentukan a-helix pada kedua struktur protein. Perbedaan struktur tiga dimensi enzim endo-1,4-β-glucanase pada kedua bakteri diduga mempengaruhi aktivitasnya sehingga diharapkan mampu memberikan kontribusi terhadap penelitian kedepannya terkait perbedaan aktivitas degradasi enzim dari organisme yang berbeda

Kata Kunci: bakteri;enzim endo-1,4- β-glucanase; in silico

Endo 1,4-β-glucanase enzymes which are commonly found in hyperthermophilic and thermophilic organisms can hydrolyze 1-4-glicosidic bonds in cellulose into glucose with different degradation activities. This study aims to determine the protein structure and similarity of the endo 1,4-β-glucanase enzyme of bacteria Fervidobacterium nodosum and Bacillus subtilis isolated from hot springs and fermented animal feed, based on amino acid sequences and three-dimensional structures. This study is a descriptive study using the amino acid sequences of the two enzymes obtained from NCBI (National Center of Biotechnology Information) website through data mining, then analyzed for similarity with the Clustal Omega application to align different protein sequences and obtain conserved areas. Furthermore, the three-dimensional structure of the two enzymes obtained from the SWISS MODEL workspace was analyzed descriptively. The result showed the similarity of the endo 1,4-β-glucanase enzyme in the two bacteria was 21,72%. The four motifs found in the three-dimensional structure are thought to affect changes in catalytic activity, stability and alpha-helix formation in both protein structures. The difference in the three-dimensional structure of the endo-1,4- β-glucanase enzyme in the two bacteria is thought to affect its activity so that it is expected to be able contribute to future research related to differences in enzyme degradation activity of different organisms.

Key Words: bacteria; the endo 1,4-β-glucanase enzyme; in silico