Sankar_2020_Int.J.Biol.Macromol_164_3546

Lipase is a versatile enzyme found in microorganisms, animals and plants. It has applications in a wide variety of fields ranging from the food industry to the pharmaceutical. For these applications, mainly microbial lipases are exploited in great detail. On the other hand lipases from the plant source have been characterized to a much lesser extent. Although many plant lipase sequences have been reported in UniProtKB, till date there is no report on the crystal structure of any plant lipase. In view of very limited availability of structural information on plant lipases, in this study, we modeled the three-dimensional structure of seven plant lipases and studied the conformational changes under four different solvents at two different temperatures. Most lipases have a lid domain and its movement is implicated in the interfacial activation of lipases. Among the 56 conditions tested in this study, some lipases at certain condition exhibit the lid domain movement thus implying the functional importance. Laborious purification and minimal yield are the likely reasons for poor characterization of plant lipases. In this scenario, the results of computational studies on plant lipases under different environmental conditions will provide useful data for subsequent in vitro functional studies.