Enzyme immobilisation technology is an effective means to improve sugar ester production through the employment of biocatalysts. In the present study, immobilisation of Candida rugosa (CRL) lipase onto amino-activated mica is performed via covalent bonding (namely Amino-CRL) and the cross-linking of lipases into nano-reactors through physical adsorption (namely NER-CRL). Free and immobilised lipases were tested for their esterification activities. Specific activities for Amino-CRL and NER-CRL increased by 2.4 and 2.6-fold, respectively, upon immobilisation. Extending this work, immobilised lipases have novel capabilities in the synthesis of sugar esters. The optimised conditions for sugar fatty acid ester syntheses are 48 h at 2:1 of molar ratio of lactose sugar to capric acid at 55 C. Furthermore, a high operational stability with half-lives of over 13 and 10 runs was achieved for NER-CRL and Amino-CRL, respectively, indicating the efficiency of the immobilisation process. (C) 2011 Elsevier Ltd. All rights reserved.

The kinetics of wax ester synthesis from oleic acid and oleyl alcohol using immobilized lipase from Candida antartica as catalyst was studied with different types of impeller (Rushton turbine and AL-hydrofoil) to create different mixing conditions in 21 stirred tank reactor. The effects of catalyst concentration, reaction temperature, and impeller tip speed on the synthesis were also evaluated. Rushton turbine impeller exhibited highest conversion rate at lower impeller tip speed as compared to AL-hydrofoil impeller. A second-order reversible kinetic model from single progress curve for the prediction of fractional conversion at given reaction time was proposed and the corresponding kinetic parameter values were calculated by non-linear regression method. The results from the simulation using the proposed model showed satisfactory agreement with the experimental data. Activation energy shows a value of 21.77 Kcal/mol. The thermodynamic parameters of the process, enthalpy and entropy, were 21.15 Kcal/mol and 52.07 cal/mol.K, respectively.

BACKGROUND: Adipate esters are used as low-temperature and low-viscosity plasticizers for polyvinyl chloride and its copolymers. In this work, optimization of lipase-catalyzed production of dilauryl adipate was carried out using response surface methodology (RSM) based on a four-factor-five-level central composite rotatable design (CCRD). Immobilized lipase from Candida antarctica (Novozym 435) was used as catalyst in this reaction. Various reaction parameters affecting the synthesis of adipate ester, including alcohol/acid molar ratio, amount of enzyme, temperature and reaction time, were investigated. RESULTS: Statistical analysis showed that the amount of enzyme was less significant than the other three factors. The optimal conditions for the enzymatic reaction were obtained at 5.7:1 substrate molar ratio using 0.18g of enzyme at 53.1 degrees C for 282.2 min. Under these conditions the esterification percentage was 96.0%. CONCLUSIONS: The results demonstrated that response surface methodology can be applied effectively to optimize the lipase-catalyzed synthesis of adipate ester. The optimum conditions can obtained be used to scale up the process. (C) 2008 Society of Chemical Industry

Mica was modified either by acid treatment, grafting with aminopropyl-, octyl-, vinyl-, mercapto- and glycidoxy-triethoxysilanes, and activation of pre-treated support with glutaraldehyde (Glu). The derivatives were characterized by X-ray diffraction (XRD), infra-red spectroscopy (FTIR), surface area and porosity analysis, scanning electron microscopy coupled with energy dispersive X-ray (SEM-EDX) and transmission electron microscopy (TEM) techniques. The modified micas were used for immobilization of lipase from Candida rugosa (CRL). Activity of the lipase was determined by esterification and exhibited the improved activity than the free enzyme following the order; Amino-CRL>Glu-Amino-CRL>Octyl-CRL>Vinyl-CRL>Glycidoxy-CRL>Mercapto-CRL>Mica-CRL Lipase immobilized mica showed enhanced protein loading (up to 8.22 mg protein/g support) and immobilization (up to 78%) compared to the free lipase and unmodified mica. (C) 2009 Elsevier B.V. All rights reserved.