10.6084/m9.figshare.7370783.v1 Ayesha Sadaf Ayesha Sadaf Jasneet Grewal Jasneet Grewal Isha Jain Isha Jain Arti Kumari Arti Kumari Sunil K. Khare Sunil K. Khare Stability and structure of <i>Penicillium chrysogenum</i> lipase in the presence of organic solvents Taylor & Francis Group 2018 Enzyme structure lipase organic solvents Penicillium chrysogenum 2018-11-21 14:44:34 Dataset https://tandf.figshare.com/articles/dataset/Stability_and_structure_of_i_Penicillium_chrysogenum_i_lipase_in_the_presence_of_organic_solvents/7370783 <p>The present work describes the enzymatic properties of <i>Penicillium chrysogenum</i> lipase and its behavior in the presence of organic solvents. The temperature and pH optima of the purified lipase was found to be 55 °C and pH 8.0 respectively. The lipase displayed remarkable stability in both polar and non-polar solvents upto 50% (v/v) concentrations for 72 h. A structural perspective of the purified lipase in different organic solvents was gained by using circular dichroism and intrinsic fluorescence spectroscopy. The native lipase consisted of a predominant α-helix structure which was maintained in both polar and non-polar solvents with the exception of ethyl butyrate where the activity was decreased and the structure was disrupted. The quenching of fluorescence intensity in the presence of organic solvents indicated the transformation of the lipase microenviroment <i>P. chrysogenum</i> lipase offers an interesting system for understanding the solvent stability mechanisms which could be used for rationale designing of engineered lipase biocatalysts for application in organic synthesis in non-aqueous media.</p>