Emulating structural stability of Pseudomonas mendocina lipase: in silico mutagenesis and molecular dynamics studies.

The need of alkaline detergent-stable lipases has been growing rapidly as they are highly attractive for the production of detergents, biodiesel, pharmaceuticals agents, and various other applications. Lipase from Pseudomonas mendocina (PML) is one such candidate with triglyceride activity and non-homologous with other reported Pseudomonas lipases. The present work provides insights on the role of amino acids toward structural stability of PML. PML was subjected to mutagenesis through in silico point mutations for emulating its structural stability, the foremost property to enhance biophysiochemical properties for industrial process. The structural effects of identified mutants on PML have been analyzed through comparative atomistic molecular dynamics simulations on wild type and mutants. The in silico mutants P187A and P219A were found to stabilize their respective local dynamics and improved the structural stability of PML. The current study sheds light on the rational engineering of PML through in silico methodologies to improvise its structural stability as well as prototype for rational engineering of the lipases.