Application

Lipase A Candida antarctica, recombinant from Aspergillus oryzae has been used in the enzyme-catalyzed hydrolysis studies with 3-acetylthiohexanal. It has also been used as a biocatalyst to test its effect on the esterification of phytosterol with caprylic acid.

Biochem/physiol Actions

Lipase A from Candida Antarctica catalyzes hydrolysis of tertiary alcohols to form glycerol and fatty acids and shows selectivity for the N-acylation of β-amino esters.

Lipase A Candida antarctica (CALA) is a thermostable serine hydrolase with a higher sn-2 preference towards triglycerides. It displays excellent activity towards large substrates as well as bulky sterically hindered tertiary alcohols.

General description

Lipase A Candida antarctica (CALA) belongs to the α/β hydrolase family. The catalytic triad comprises Ser184, His366, and Asp334 residues.

Other Notes

Characterization

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 µmol oleic acid per minute at pH 8.0 and 40°C (triolein, Cat. No. 62314, as substrate); 1 U as described above is equivalent to ~0.15 U using trybutyrine, Cat. No. 91010, as substrate, at pH 8.0 and 70°C