Merck, 76546-10G, Lipase, immobilized on Immobead 150 from Thermomyces lanuginosus

General description
Research area: Cell Signaling

Lipase from Thermomyces lanuginosus (TLL) is a basophilic, single-chain protein and thermostable enzyme. It belongs to the alpha/beta-hydrolase fold family. TLL is roughly spherical and is made up of a central seven-stranded β-parallel sheet with five interconnecting α-helices.
Application
Lipase, immobilized on Immobead 150 from Thermomyces lanuginosus has been used: as a biocatalyst to study ultrasound-assisted transesterification of a blend of non-edible oils with methanol.
as a catalyst in the synthesis of medium chain fatty acids (MCFA) and polyunsaturated fatty acids (PUFA) rich oils by enzymatic structuring of flax seed oil.
for the resolution of chiral compounds and the transesterification production of biodiesel.
to enhance the efficiency and selectivity of the enzymatic synthesis of ethyl-(R)-2-hydroxy-4-phenylbutyrate, (R)-HPB ester.
to facilitate a chemoenzymatic process for the continuous synthesis of (S)-7-((tert-Butyldiphenylsilyl)oxy)hept-1-yn-4-ol, a crucial intermediate for Eribulin synthesis, within a packed-bed reactor setup.

Biochem/physiol Actions
Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
It participates in catalyzing the hydrolysis of triglycerides at the water-lipid interface and produces mono-, di-glycerides, and free fatty acids. Due to its versatility, this enzyme is applicable in various industries including, detergents, paper, leather, baking, fine chemicals, fuel, and biocatalysts.
Other Notes
1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 7.5 and 40°C (tributyrin, Cat. No. 91010, as substrate)