Abstract
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.
Highlights
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
Candida rugosa lipase (CRL) has been widely studied, which originates from the secretion of microorganisms and is continuously enhanced with various modification and immobilization techniques to increase its utility
(including catalytic mechanisms and specificity), technology for CRL immobilization, especially discussing the latest CRL immobilization method, CRLs are more often used in an immobilized form where CRLs are trapped or bound by the support matrix namely through the formation of nanoparticles
Summary
CRL has five isoenzymes, each of which has been given a genetic code, namely LIP1 - LIP5, and develops again into LIP1 - LIP8 (Lotti et al, 1994; Vanleeuw et al, 2019). Lipase proteins in this group have a high homologous sequence (84% of similarity). The differences from these isoenzymes are probably their biochemical properties due to differences in the content of sugar groups, isoelectric pH, and hydrophobicity (Benjamin and Pandey, 1998; Lotti and Alberghina, 2007; Vanleeuw et al, 2019). LIP2 has good catalytic activity for medium and longchain fatty acids; LIP2 is suitable as cholesterol esterase. LIP3 has a homologous lid structure with LIP2 and has biocatalytic activity suitable as cholesterol esterase. LIP5 has a very good affinity for triacylglycerol substrate, and its biocatalytic activity is almost the same as LIP3 (Lotti et al, 1994; Benjamin and Pandey, 1998; Barriuso et al, 2016; Domínguez De María et al, 2006; Vanleeuw et al, 2019) while LIP6-LIP8 is still being studied until now (Kuo et al, 2015)
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