| Popis: |
>MOvergrowth of Candida tends to produce high levels of secondary metabolites affecting the immersion of infectious and degenerative diseases. Biofilm’s existence as a virulence factor of Candida makes it challenging to overcome causing multidrugresistant issues. Studies on the effectiveness of Candida antibiofilm drug candidates should be supported by data related to model structure and molecular interaction within the eradication process of biofilm through homology modeling and in-silico docking. This study aims to determine molecular interactions between 1,3-β-glucanase Achatina fulica in which the substrate is, through homology modeling and docking studies within the biofilm matrix eradication process. The alignment results show that mkafGlu1 is a new representative of the Glycoside Hydrolase 16 family (GH16) with EC 3.2.1.39. MKAFGlu1 enzymes are 1,3-1,6-β-glucanase able to cleave 1,3-β- dan 1,6-β-glycosidic bonds. This in-silico docking study also shows that mkafGlu1 has high specificity towards laminarin (substrate 1,3-1,6-β-glucanase) and that the enzyme of MKAFGlu1 works based on a retention mechanism in its reaction to the substrate. The result of the recombinant enzyme of 1,3-β-glucanase novel genes can hydrolyze the substrate of 1,3-β-glucan as one of the biofilm matrix components, opening up an opportunity for new medicine as an antibiofilm candidate. |
