Candida rugosa lipase (CRL) is an important industrial enzyme that is successfully utilized in a variety of hydrolysis and esterification reactions. This work describes the optimization of immobilization conditions (enzyme/support ratio, immobilization temperature, and buffer concentration) of CRL on the anionic resin Amberjet® 4200-Cl, using enantioselectivity (E) as the reference parameter. The model reaction used for this purpose is the acylation of (R,S)-1-phenylethanol. Optimal conditions for immobilization have been investigated through a response surface methodology (RSM) and artificial neural network (ANN). The coefficient of determination (R(2)) and the root mean square error (RMSE) values between the calculated and estimated responses were respectively equal to 0.99 and 0.06 for the ANN training set, 0.97 and 0.2 for the ANN testing set, and 0.94 and 0.4 for the RSM training set. Both models provided good quality predictions, yet the ANN showed a clear superiority over RSM for both data fitting and estimation capabilities.
International audienceThe objective of this study was to evaluate the immobilization of lipase on an organic matrix by reticulation method, aiming at its application in the detection of organochlorine pesticide. The biologically inactive protein of bovine serum albumin (BSA) and glutaraldehyde were used for immobilizing lipase from a microbial source ( Candida rugosa CRL ) and animal cells (porcine pancreatic lipase, PPL). Use of this immobilized preparation was extended to the realization of two different origins of a miniaturized enzymatic biosensors is presented for the electrochemical detection of a large range of organochlorine pesticide (diclofop-methyl) in phosphate buffer saline (PBS) were observed experimentally. The best responses of biosensor were obtained for PPL with a high sensitivity to organochlorine pesticide in the concentration range of 5.99*10-12 to 5.89*10-2g*L-1, whereas a linear response of CRL for diclofop-methyl was obtained. The lipase biosensors exhibits the advantage of a simple fabrication procedure, wide dynamic range and a lower detection limit (5.99*10-12 g*L-1 for diclofop-methyl). The impact of heavy metals as well as organophosphorous and other organochlorine pesticides was also studied
This work mainly focused on the production of an efficient, economical, and eco-friendly lipase (AKL29) from Actinomadura keratinilytica strain Cpt29 isolated from poultry compost in north east of Algeria, for use in detergent industries. AKL29 shows a significant lipase activity (45 U/mL) towards hydrolyzed triacylglycerols, indicating that it is a true lipase. For maximum lipase production the modeling and optimization of potential culture parameters such as incubation temperature, cultivation time, and Tween 80 (v/v) were built using RSM and ANN approaches. The results show that both the two models provided good quality predictions, yet the ANN showed a clear superiority over RSM for both data fitting and estimation capabilities. A 4.1-fold increase in lipase production was recorded under the following optimal condition: incubation temperature (37.9 °C), cultivation time (111 h), and Tween 80 (3.27%, v/v). Furthermore, the partially purified lipase showed good stability, high compatibility, and significant wash performance with various commercial laundry detergents, making this novel lipase a promising potential candidate for detergent industries.
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