Title of article :
Lipase from Rhizomucor miehei as an industrial biocatalyst in chemical process
Author/Authors :
Rodrigues، نويسنده , , Rafael C. and Fernandez-Lafuente، نويسنده , , Roberto، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2010
Abstract :
The lipase from Rhizomucor miehei (formerly Mucor miehei) (RML) is a commercially available enzyme in both soluble and immobilized form with very high activity and good stability under diverse conditions (anhydrous organic solvents, supercritical fluids, etc.). Although this lipase was initially produced to be used in food industry, in this review we will focus our attention on the application of this enzyme in organic chemistry, from biodiesel production to fine chemicals (mainly in enantio or regioselective or specific processes). After showing the enzyme features, some of the most efficient methods of RML immobilization will be commented (entrapping on reverse micelles, preparation of cross-linked RML aggregates or immobilization on pre-existing solids). Finally, the main uses of the enzyme in organic chemistry will be revised. The use of RML in the production of biodiesel will be analyzed, and compared to the performance of other lipases. The synthesis of esters of carboxylic acids as flavors is other example where RML has been successfully employed. Taking advantage of the wide specificity of the enzyme, mainly a high enantiospecificity, many examples of the use of RML in the resolution of racemic mixtures of chiral carboxylic acids, alcohols or esters will be presented. Special mention requires the use of the regioselectivity of RML, mainly the chemistry of sugars. Finally, more unusual uses of RML will be presented (anomalous substrates, novel uses, etc.). In general, this enzyme seems very adequate for esterification reactions due to its high stability in anhydrous media and good esterification activity.
Keywords :
Lipozyme RM IM , Lipolase , Lipase immobilization-stabilization , biodiesel , Resolution of racemic mixtures , Regioselective process , Sugar modifications
Journal title :
Journal of Molecular Catalysis B Enzymatic
Journal title :
Journal of Molecular Catalysis B Enzymatic