5.

12 LIPASE

Biocatalysis is booming at present era for an organic synthesis re- search due to its unique features such as enzymes are
recognized as lectivity [120–127]. These biocatalysts work at mild reaction tem- perature and can be easily incorporated in
greener reaction media [112–118]. They are non-hazardous to environment, energy saving, obtained from natural resources and
safe to use, hence they are con- sidered as a green sustainable catalyst [122–127].
Salvi and Yadav [110] used surface functionalization of SBA-15 for
immobilization of lipase CANDIDA ANTARCTICA B (CAL B) which was fur- ther used for the catalytic test to carry out synthesis of
alkyl levulinates (Table 1, entries 127,128). Zhou et al., [111] performed synthesis of long chain alkyl levulinates using CAL
B immobilized on meso-molding three-dimensional macro-porous organo-silica as a biocatalyst (Table 1, entries 129–131).
Yadav and Borkar [112] proposed kinetic model of synthesis of n-butyl levulinate for the immobilized CAL B lipase cata-
lyzed reaction (Table 1, entry 132). Lee et al., [113] performed bio- catalyzed synthesis of ethyl levulinate ester in a
solvent-free system (Table 1, entry 133). Badgujar and Bhanage [114] carried out thermo- chemical energy assessment to
synthesize levulinates using im- mobilized lipase biocatalyst CAL B (Table 1, entries 134–142). Badgujar and Bhanage [115]
performed lipase catalyzed synthesis of alkyl le- vulinates in supercritical carbon dioxide (Table 1, entries 143–150).
Various fungal and bacterial lipases are used for the present
synthesis. Among all studied lipases, CAL B showed excellent activity for this transformation. Lipase possesses the amino acid
lid at the cat- alytic active sites of lipase to pass reactants to active catalytic amino- acid triad of enzyme. However, the superior
activity of CAL B was re- cognized due to lack of ‘flap or lid’ which facilitates quite easy diffusion of the reacting molecules to
the dynamic biocatalytic sites of lipase. Moreover, most active, stable and bead immobilized form of the lipase CAL B is easily
available in market which is directly used in the reaction system. Conversely, other lipases need modifications via immobiliza-
tion process or genetic engineering to employ in reaction media, which is a task of skilful hands. Many times enzyme activity
gets lost or de- crease in immobilization or in genetic engineering process. However, immobilization process offers easy
recyclability and improves the sta- bility of enzymes towards reaction media. Thus commercially available immobilized CAL B
lipase is the most active and stable form of lipase which displayed excellent catalytic activity for synthesis of levulinate
compounds. In conclusion, the biocatalysts are non-hazardous and ab-
solutely greener in nature. The major challenging issue related with these biocatalysts is stability towards reaction media,
organic sub- strates, operational condition, reusability and cost of production. Immobilization, rational designing, protein
engineering and directed evaluation are expensive and time-consuming methodologies to im- prove or to develop the
biocatalyst for organic transformation. Further these biocatalyst developing methodologies do not offer any assurance for the
success of designing of biocatalysts and its activity.