Lipases are water-soluble enzymes that act on insoluble substrates and catalyze the hydrolysis of long-chain triglycerides. Lipases play a vital role in the food, detergent, chemical, and pharmaceutical industries. In the past, fungal lipases gained significant attention in the industries due to their substrate specificity and stability under varied chemical and physical conditions. Fungal enzy...

Yarrowia lipolytica is a very important yeast because many strains from this yeast are able to produce the extracelular lipases. Cold active lipase is one of the important and widely used enzymes whose spectrum of applications has widened in many industries such as in detergent formulations, food industry, leather processing, environmental bioremediations, and fine chemical synthesis as well as...

1. The size of two bacterial lipases was studied by SDS/PAGE, sedimentation velocity and sedimentation equilibrium to test for possible self-association behaviour. 2. Mr values of selected lipases were obtained from SDS/PAGE and sedimentation-velocity measurements, together with an absolute determination by sedimentation equilibrium 3. The Mr values obtained in a variety of aqueous solvents ind...

Lipases are the most versatile industrial enzymes and are known to bring about a range of bioconversion reactions. This compendium throws light on the developments in the field of fermentation of lipases and their scale up. Recently, interests have been shown on solid-state fermentation of lipases in order to facilitate the use of low cost agricultural wastes as substrates. Whole cell immobiliz...

Lipolytic activity was associated with Candida lipolytica in several early studies (Long, 1936; Long & Hammer, 1938, 1939), and the influence of culture conditions on lipase production has been described by Peters & Nelson (1948). Studies on the intracellular lipases (Lloyd et al., 1971) indicated that C. lipoiytica grown in liquid media with glucose as a carbon source contained five distinct l...

The present study was conducted to evaluate the feasibility of enzymatic hydrolysis of carotenoid esters from Tagetes erecta using lipases from the yeast of Yarrowia lipolytica, with the aim of obtaining free lutein. The optimal concentrations of seven nutrients, considering the production of lipases relative to biomass (Yp/x) as the response variable, were determined in flask fermentations. In...

The structural elucidations of microbial lipases have been of prime interest since the 1980s. Knowledge of structural features plays an important role in designing and engineering lipases for specific purposes. Significant structural data have been presented for few microbial lipases, while, there is still a structure-deficit, that is, most lipase structures are yet to be resolved. A search for...

Lipases are of great interest for different industrial applications due to their diversity and versatility. Among different lipases, microbial lipases are preferable due to their broad substrate specificity, and higher stability with lower production costs compared to the lipases from plants and animals. In the past, a vast number of bacterial species have been reported as potential lipases pro...

Lipases and phospholipases are interfacial enzymes that hydrolyze hydrophobic ester linkages of triacylglycerols and phospholipids, respectively. In addition to their role as esterases, these enzymes catalyze a plethora of other reactions; indeed, lipases also catalyze esterification, transesterification and interesterification reactions, and phospholipases also show acyltransferase, transacyla...

Most of the companies are not currently manufacturing the detergents alone; they are producing enzyme-based detergents. More than 50% of the detergents produced in the developed countries presently contain enzymes to improve the detergency by removing tough stains. The role of a detergent lipase is to digest the lipidic molecules from the soiled substrates. Most of the chemical detergent ingred...