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PEMURNIAN ENZIM LIPASE SEBAGAI BAHAN ADITIF BIODETERJEN MENGGUNAKAN KROMATOGRAFI PENUKAR ION
Natural bentonite can be used as a stationary phase because it has a layered structure that can expand and cations that can be exchanged with other ions. The activation of natural bentonite will improve the adsorption ability and expand the surface pores so that it can be used for the purification of lipase enzymes. The purification of the lipase enzyme will increase the relative activity of the enzyme so that it has the potential to be one of the additive ingredients of biodetergents. This study aims to determine the optimum ability of natural bentonite that has been activated as a stationary phase in enzyme purification to increase the activity of lipase enzyme as one of the additive ingredients of biodetergents. Purification of lipase enzymes is carried out using ion-exchange chromatography with natural bentonite as the stationary phase. Natural bentonite as a stationary phase is activated using variations in heating temperatures (200, 300, and 400°C) and HNO3 concentrations (0.5; 1; and 1.5N). The potential of lipase enzyme from PK1.1.2 isolate as a biodetergent additive was tested for its stability against exposure to commercial detergents and a washing test was carried out by adding olive oil to the fabric. Based on the results of the study, the relative activity of crude extract enzymes and purification results with non-activated bentonite elutions 1, 2 and 3 were 58%, 83%, 40% and 88% respectively with %ω only 18-52% under control (60%) so it was not qualified as a biodetergent additive. Meanwhile, the purified enzyme with activated natural bentonite is qualified as a biodetergent additive with a relative activity of 81-98.8% and %ω 63-93% above the control (60%). The highest relative activity represents the optimum ability of natural bentonite as an ion exchanger, which is when activated at a temperature of 400°C and a concentration of 0.5N.
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