Characteristics, immobilization, and application of Candida rugosa lipase: a review
Candida rugosa lipase (CRL) is one of the lipases widely used in various food industries and studies, especially in linkage with the modification of lipids. This review discusses CRL, including CRL features (molecular biology, the structure of the enzyme protein, the flap/ lid), catalytic mechanisms and substrates specificity, CRL immobilization technologies, and various applications in lipid modifications. CRL has five isoenzymes, namely LIP1 - LIP5, then develops again into LIP1 - LIP8. However, LIP1 is the most commonly found isoenzymes. CRL has a structure similar to that of Geotricum candidum lipase, has a flap/ lid, which is an active side cover in the form of α-helix, which is relatively shorter than other lipases. The active site of the CRL consists of triads ser-209, His-449, and Glu-341, while the catalytic mechanism of the CRL is the same as the other lipases by the nucleophilic attack. CRL catalyzes triacylglycerol at all positions randomly and has hydrolysis and synthesis activities that are strongly affected by the presence of water in the reaction system. CRL can be used for various lipid modifications through hydrolysis, esterification, interesterification/transesterification, and alcoholysis/ glycerolysis reactions.