Abstract

The review paper concerns the problem of the design and practical application oftechnological biocatalysts based on lipase fraction B from Pseudozyma (Candida) antarctica (CALB). CALB occupies an intermediate position between esterases and true interface-activated lipases that ensures its unique properties. Wide specificity in the synthesis/hydrolysis of a broad range of esters, amides and thiols characteristic of esterases is combined in this enzyme with the inherent to lipases possibility of working on oil-water interface of emulsified substrates and in the medium of organic solvents, along with high regio- and enantioseteclivity, high thermostability and tolerance to the presence of polar and non-polar solvents. The known approaches to the immobilization of CALB are discussed in terms of structure and properties of the enzyme, and the purpose of the resulting biocatalyst. The reported data on the possibilities of practical implementation of CALB biocatalysts are summarized.

Full Text
Paper version not known

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 call