Molecular characterization and application of lipase from Bacillus sp. PU1 and investigation of structural changes based on pH and temperature using MD simulation
| Autor: | Venkatesan Arul, Dasari Ankaiah, Syed Ibrahim Basheer Ahamed, Palanichamy Esakkiraj, Balraj Meleppat, Repally Ayyanna, Christian Bharathi Antonyraj |
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| Rok vydání: | 2017 |
| Předmět: |
Protein Conformation
alpha-Helical 0106 biological sciences 0301 basic medicine Bacillus Molecular Dynamics Simulation 01 natural sciences Biochemistry Serine 03 medical and health sciences Structural Biology 010608 biotechnology Lipase Molecular Biology chemistry.chemical_classification Bacteria biology Chemistry Temperature Biofilm General Medicine Hydrogen-Ion Concentration biology.organism_classification Enzyme assay 030104 developmental biology Enzyme Biofilms biology.protein Protein Conformation beta-Strand Mesophile |
| Zdroj: | International Journal of Biological Macromolecules. 103:47-56 |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2017.04.111 |
| Popis: | A gene coding lipase from Bacillus sp. PU1 was cloned and expressed in E. coli BL21(DE3) pLysS. The purified lipase has a molecular weight of 23kDa, is highly alkaline (pH range 8-10) and mesophilic (20-50°C). Three dimensional structure of the lipase was modeled by comparative homology and identified as a typical serine lipase by the presence of conserved Ser77, Asp133, His156. The molecular stability and behavior of the lipase was carried out using MD simulation studies at different pH and temperature was performed in comparison with biochemical analysis. Structural modifications of the lipase under these conditions were trapped by dihedral based FEL analysis and the functional loops (loop-H5/B4 and loop-H6/B5 of lipase) are identified which would cause the catalytic behavior of the lipase by high flexibility. Further characteristic feature of lipase are observed as follows; SDS completely inhibits the lipase activity and enzyme activity is enhanced with non-ionic surfactants. The lipase was highly stable in different organic solvents and also it could tolerate NaCl (0.4-0.8M). This enzyme was found to disrupt the biofilm of tested pathogenic bacterial strains. |
| Databáze: | OpenAIRE |
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