Abstract
Lipases are carboxyl-esterases (EC 3.1.1.3.) which, in vivo, catalyze the hydrolysis of triglycerides and isoluble substrates by a heterogeneous process. In vitro, they may also hydrolyze soluble esters, but the presence of a water–lipid interface significantly increases their lipolytic activity. The commercially available crude lipase contains ca. 30% of lactose as `extender'. In fact, the addition of sugars or polyols stabilizes the biological macromolecules, thereby preventing loss of enzyme activity and increasing resistance to denaturing conditions. By means of differential scanning calorimetry (DSC) and thermogravimetry (TG), it has been possible to evaluate the composition of a commercial lipase and also to demonstrate the addition of a monohydrate α-lactose, and the time of addition.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
