The response surface methodology for optimization of Halomonas sp. C2SS100 lipase immobilization onto CaCO3 for treatment of tuna wash processing wastewater

An immobilized enzyme could exhibit selectively modified physicochemical properties, and it might offer a better environment for the enzyme activity. In this study, the immobilization yield of crude Halomonas sp. lipase was optimized to improve its stability. Thanks to its high adsorption capacity, CaCO3 has been chosen as support for the immobilization process. Furthermore, response surface methodology (RSM) was used to determine optimal conditions for the immobilization of the bacterial lipase. Five tested factors (enzyme solution, support amount, time, temperature, and acetone volume) were optimized applying a central composite design of RSM. The maximum yield of lipase immobilization was improved to 96%. Furthermore, a biochemical characterization proved a significant improvement of the immobilized lipase stability. The immobilized enzyme is more stable at extreme pH values and high temperatures than the free one. We also tested the reusability of the immobilized lipase by evaluating the recovery of the support using simple filtration. Thanks to its high stability, the immobilized lipase was invested in an effective treatment of tuna wash processing wastewater. The oil biodegradation efficiency was established at 81.5% and was confirmed by Fourier transformation infrared spectrometry. Likewise, the biological oxygen demand values were reduced which makes a possible reduction of the wastewater pollution degree.