RESUMEN

Biodiesel is a renewable, sulfur-free, toxic-free, and low carbon fuel which possesses enhanced lubricity. Transesterification is the easiest method employed for the production of biodiesel, in which the oil is transformed into biodiesel. Biocatalyst-mediated transesterification is more advantageous than chemical process because of its non-toxic nature, the requirement of mild reaction conditions, absence of saponification, easy product recovery, and production of high-quality biodiesel. Lipases are found to be the primary enzymes in enzyme-mediated transesterification process. Currently, researchers are using lipases as biocatalyst for transesterification. Lipases are extracted from various sources such as plants, microbes, and animals. Biocatalyst-based biodiesel production is not yet commercialized due to high-cost of purified enzymes and higher reaction time for the production process. However, research works are growing in the area of various cost-effective techniques for immobilizing lipase to improve its reusability. And further reduction in the production cost of lipases can be achieved by genetic engineering techniques. The reduction in reaction time can be achieved through ultrasonic-assisted biocatalytic transesterification. Biodiesel production by enzymatic transesterification is affected by many factors. Various methods have been developed to control these factors and improve biodiesel production. This report summarizes the various sources of lipase, various production strategies for lipase and the lipase-mediated transesterification. It is fully focused on the lipase enzyme and its role in biodiesel production. It also covers the detailed explanation of various influencing factors, which affect the lipase-mediated transesterification along with the limitations and scope of lipase in biodiesel production.

RESUMEN

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.

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RESUMEN

Carica papaya latex is one of the most studied sources of plant lipases. However, the complexity of the matrix composition makes it difficult to isolate and purify the lipolytic enzymes present in Carica papaya latex. Therefore, diverse strategies have been developed to study the catalytic properties of these enzymes.Recently the first lipase from Carica papaya latex (CpLip1) has been successfully cloned and expressed in order to study their catalytic properties. In order to improve the catalytic properties and increase the potential for its use at industrial scale.In this chapter, a practical protocol to recombinant CpLip1 lipase is given.

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