Lipases from <i>Candida </i><i>a</i><i>ntarctica</i>: Unique Biocatalysts from a Unique Origin

The specificity of the A-lipase from Candida antarctica (CALA) has been characterized to further clarify the scope of the biocatalyst. The lipase was found to exhibit an almost uniform activity towards various straight-chained primary alcohols and carboxylic acids, only exhibiting a low activity towards very short-chained acids. More interestingly, the enzyme was found to exhibit a high activity towards a surprising diversity of sterically hindered alcohols, including both secondary and tertiary alcohols. These results indicate that CALA can have a unique applicability for the conversion of highly branched substrates where most other lipases fail to display any activity. A new, potentially highly cost-effective, immobilization technology using silica-based granulation has been applied in the immobilization of the B-lipase from the same yeast (CALB). Highly stable particles were obtained with an activity comparable to that of the commercially available immobilized preparations of this enzyme.