Immobilization of lipase B from Candida antarctica on porous styrene–divinylbenzene beads improves butyl acetate synthesis

Abstract

A new biocatalyst of lipase B from Candida antarctica (MCI-CALB) immobilized on styrene-divinylbenzene beads (MCI GEL CHP20P) was compared with the commercial Novozym 435 (immobilized lipase) in terms of their performances as biocatalysts for the esterification of acetic acid and n-butanol. The effects of experimental conditions on reaction rates differed for each biocatalyst, showing different optimal values for water content, temperature, and substrate molar ratio. MCI-CALB could be used at higher acid concentrations, up to 0.5 M, while Novozym 435 became inactivated at these acid concentrations. Although Novozym 435 exhibited 30% higher initial activity than MCI-CALB for the butyl acetate synthesis, the reaction course was much more linear using the new preparation, meaning that the MCI-CALB allows for higher productivities per cycle. Both preparations produced around 90% of yield conversions after only 2 h of reaction, using 10% (mass fraction) of enzyme. However, the main advantage of the new biocatalyst was the superior performance during reuse. While Novozym 435 was fully inactivated after only two batches, MCI-CALB could be reused for six consecutive cycles without any washings and keeping around 70% of its initial activity. It is proposed that this effect is due to the higher hydrophobicity of the new support, which does not retain water or acid in the enzyme environment. MCI-CALB has shown to be a very promising biocatalyst for the esterification of small-molecule acids and alcohols.

Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase

“…CALB is a hydrolase enzyme (33 kDa) [14] that is widely used in biocatalysis [15][16][17] due to its broad substrate range, high activity and stability. CALB has been successfully immobilized by several methods [18][19][20] onto various solid supports [21][22][23][24]. SBA-15 possesses a hexagonal structure with pore diameters of ca.…”

Immobilization of Proteins in Poly-Styrene-Divinylbenzene Matrices: Functional Properties and Applications

“…In a first report lipase B from C. antarctica, immobilized on MCI GEL CHP20P was compared with the commercial Novozym 435 as biocatalysts for the esterification of acetic acid and n-butanol [13]. Lipase immobilized on MCI GEL CHP20P could be used under more acidic conditions, up to 0.5 M, while Novozym 435 became inactivated under these conditions.…”

“…Although Novozym 435 exhibited higher initial activity than MCI-CALB (30%) for the butyl acetate synthesis, the reaction course was more straighforward with new preparation, implying higher productivities per cycle for MCI-CALB. [13]. The primeval advantage of the new biocatalyst is its superior performance in its recycling.…”

“…This occurs, for example, in the production of biodiesel or esterification reactions [10][11][12]. Thus, the use of a very hydrophobic support may reduce and even eliminate this problem [13], compensating a decrease in the enzyme thermostability (Fig. 2).…”

Optimization Method for The Synthesis of Fatty Amide Surfactants from Oleic Acid Catalyzed by Immobilized Lipase

“…Lipase (triacylglycerol hydrolases; EC 3.1.1.3) is extensively used due to their regio-, stereo-, substrate-specificities milder reaction conditions and relatively lower energy requirement 2,4 . Lipase-catalyzed reactions have been carried out in suitable organic solvents or under solvent-free conditions at hydrolysis reaction 6 , esterification 7,8,9 and amidification 3,5,10 . Most of the work on lipasecatalyzed amidification reported in the literature is based on the reactions using fatty ester substrate.…”