Lipases have many applications in biotechnology, thanks to their ability of acylglycerides hydrolysis. They alsp possess the unique feature of acting at the lipid-water interface, which distinguishes them from esterases. Commercially useful lipases are produced by microorganisms with the extracellular lipase being produced by many bacteria including Pseudomonas. The greatest production of lipas...

Abstract There are growing demands by the biodiesel companies to get cheap lipase formulation, preferably in liquid forms, which can give an answer their needs. Thus, many commercial or home-produced enzymes being used this process free form. Among these enzymes, Eversa is a formulation derived from Thermomyces lanuginosus designed for enzymatic production. The potential of promising enzyme her...

866 Autophagy 2009; Vol. 5 Issue 6 We have all learned in textbooks that “lysosomes contain hydrolases able to degrade all types of intracellular molecules which include proteases, glycosidases, nucleotidases and lipases.” To date, the only logical explanation for the presence of lipases inside of lysosomes was for the degradation of lipoproteins internalized by endocytosis, and for the breakdo...

Thermal stability of wild type Humicola lanuginosa lipase (wt HLL) and its two mutants, W89L and the single Trp mutant W89m (W117F, W221H, and W260H), were compared. Differential scanning calorimetry revealed unfolding of HLL at T(d)=74.4 degrees C whereas for W89L and W89m this endotherm was decreased to 68.6 and 62 degrees C, respectively, demonstrating significant contribution of the above T...

Chimeric molecules between human lipoprotein lipase (LPL) and rat hepatic lipase (HL) were used to identify structural elements responsible for functional differences. Based on the close sequence homology with pancreatic lipase, both LPL and HL are believed to have a two-domain structure composed of an aminoterminal (NHz-terminal) domain containing the catalytic Ser-His-Asp triad and a smaller ...