Desulfurization protein named DszC from Rhodococcus erythropolis is the key enzyme for biodesulforization of dibenzothiophene
(DBT) in 4S pathway, which is a pathway with four enzymes. DszC enzyme biodesulfurizes DBT and its derivatives in oil
components and biphasic systems. It functions well at the oil- water interface. In this study point mutation performed in DszC
enzyme regarding to increase protein hydrophobicity and stability for application in immobilized form. 3D model of DszC
predicted using Phyre2, SAM-T08 and M4t servers. I-Mutant 2 server used to determine potential spots for point mutation, and
Molegro Virtual Docker (MVD) used for performing point mutation on 3D model. Hydrophobicity plots generated by Bioedit
version 188.8.131.52 in Kyte-Doolittle scale indicated that protein hydrophobicity is increased after mutation. Also protein stability
increased 26.11 units in scale of DDC2.