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.