Immobilization of Lipase from Candida rugosa on Synthetic Polymer Beads for Use in the Synthesis of Fatty Esters

Abstract

Lipase from Candida rugosa was immobilized on three different supports, i.e. Amberlite XAD7, poly(methylmethacrylate) (PMMA) and celite. With the conditions tested, maximum adsorption can be achieved after 30 min. The activities of the immobilized lipases were determined by the esterification reaction of oleic acid and butanol. The immobilized lipases were found to be very effective in the esterification reaction. The immobilized activities generally were high in apolar organic solvents with log P values from 2•0 to 4•0. The preference for fatty acids as acyl donors differed in all cases of immobilized lipases. Lipase immobilized on XAD7 and PMMA exhibited high preference of acyl donors (fatty acids) with chain lengths 12-18 and 8-18, respectively. Lipase immobilized on celite, however, showed high activity in all cases of fatty acids. The nucleophile (alcohol) selectivity studies showed that lipase immobilized on XAD7 and celite was more accessible to alcohols of chain lengths 3-12. However, lipase immobilized on PMMA showed a significant preference towards alcohols of chain lengths from 3 to 10.

Hydrolysis of oils in the Wadi Hanifah River in Saudi Arabia by free and immobilized Staphylococcus aureus ALA1 lipase

“…The maximum binding of the enzyme to CaCO 3 (95%) was achieved after incubation for 40 min. This was consistent with prior descriptions for the immobilization of R. oryzae and C. rugosa lipases to CaCO 3 and AmberliteXAD7, respectively [11,26].…”

Application of advanced materials as support for immobilisation of lipase fromCandida rugosa

“…However, these findings indicated that lipase remained immobilised on LDH even after washing with 20 mL of hexane, indicating that LDHs are suitable as supports for immobilisation of lipase. Similar results have been reported by Basri et al (1996) in studying the abilities of polymer beads to hold the enzyme after a few cycles of washing with organic solvent. This provides additional advantages for the LDHs.…”

Purification, biochemical characterization and performance evaluation of an alkaline serine protease from Aspergillus flavus MTCC 9952 mutant

“…On the other hand, the lower activities of protease in the polar solvents could be due to the fact that these solvents could strip the essential water layer around the enzyme, which is important for enzyme catalysis (Basri et al, 1996). As it has early been recognized that water is necessary to preserve the active conformation of the enzyme and determine the catalytic activity (Klibanov, 1989;Yamane et.…”