Arli Aditya Parikesit - Design of Candida antarctica Lipase B Thermostability Improvement by Introducing Extra Disulfide Bond Into the Enzyme

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      Publication Details (including relevant citation   information):

      Tambunan, Usman Sumo Friend, Randy, Ahmad, Parikesit, Arli   Aditya, 2014, Online Journal of Biological   Sciences. 14 (2), pp 108-108


      andida Antarctica Lipase B (CALB) is extensively studied in   enzymatic production of biodiesel, pharmaceutical products,   detergents and other chemicals. One drawback of using CALB is its   relatively low optimum temperature at 313 K (40°C). The objective   of this research is to design CALB mutant with improved   thermostability by introducing extra disulfide bond. Molecular   dynamic simulation was conducted to get better insight into the   process of thermal denaturation or unfolding in CALB. Thermal   denaturation of CALB was accelerated by conducting simulation at   high temperature. Molecular dynamic simulation of CALB was   performed with GROMACS software package at 300-700 K. Prediction   of possible mutation was done using “Disulfide by DesignTM”   software. Selection of mutated residues was based on flexibility   analysis of CALB. From those analyses, three mutants were   designed, which are Mutant-1 (73LeuCys/151AlaCys), Mutant-2   (155TrpCys/294GluCys) and Mutant-3 (43ThrCys/67SerCys).   Parameters that were used to compare the thermostability of   mutant with wild type enzyme were Root Mean Square Deviations   (RMSD), Solvent Accessible Surface Area (SASA), Radius of   gyration (Rg) and secondary structure. Molecular dynamic   simulation conducted on those three mutants showed that Mutant-1   has better thermostability compared to wild type CALB. We   proposed the order of mutant thermostability improvement as   follows: Mutant-1, Mutant-2 and Mutant-3, with Mutant-1 having   better potential thermostability improvement and Mutant-3, the   least stable

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