A structural basis for enantioselective inhibition of Candida rugosa lipase by long-chain aliphatic alcohols

Structural basis of stereoselectivity in Candida rugosa lipase-catalyzed hydrolysis of secondary alcohols

Inhibition of Candida rugosa lipase by saponins, flavonoids and alkaloids

Isolation of Candida rugosa lipase isoforms

The yeast Candida rugosa is a convenient source of lipases for science and industry. Crude preparation of Candida rugosa lipase (CRL) consists of several extracellular lipases. Isoenzyme profile depends on the culture or fermentation conditions. All isoforms are coded by the lip pseudogene family; they are monomers of 534 amino acids and molecular weight of about 60 kDa. They share the same cat...

Isolation of long-chain aliphatic alcohols from beeswax using lipase-catalyzed methanolysis in supercritical carbon dioxide

Aliphatic alcohols of chain lengths of 24–34 carbons have been found to be beneficial in treating hypercholesterolemia. Approximately 40% of beeswax is long-chain esters which can be transesterified in supercritical carbon dioxide to give these alcohols and fatty acid methyl esters. The methanolysis reaction was catalyzed by an immobilized lipase from Candida antarctica in flowing supercritical...

Syntheses of enantiopure aliphatic secondary alcohols and acetates by bioresolution with lipase B from Candida antarctica.

The lipase B from Candida antarctica (Novozym 435®, CALB) efficiently catalyzed the kinetic resolution of some aliphatic secondary alcohols: (±)-4-methylpentan-2-ol, (±)-5-methylhexan-2-ol, (±)-octan-2-ol, (±)-heptan-3-ol and (±)-oct-1-en-3-ol. The lipase showed excellent enantioselectivities in the transesterifications of racemic aliphatic secondary alcohols producing the enantiopure alcohols ...