Effective detoxification of patulin from aqueous solutions by immobilized porcine pancreatic lipase

Porcine pancreatic lipase (PPL) was immobilized by physical adsorption onto CaCO3. The detoxification of the immobilized PPL for patulin from aqueous solutions was investigated. Batch experiments were carried out to obtain its optimal conditions for the immobilization process and to evaluate the influence of the immobilized PPL amount, pH, temperature, initial patulin concentration and time on the detoxification. Enzyme properties were assayed by the immobilization yield and enzyme activity, and partial structures of the immobilized PPL were characterized by Fourier Transform Infrared spectroscopy (FTIR). The immobilization yield was more than 99% during 3 h at pH 5.0, 30 °C when 0.6 mg/mL of PPL was adsorbed onto 0.5 g of CaCO3. The immobilized PPL was effective in detoxification of patulin from aqueous solutions at pH 6.0, 40 °C during 42 h. Furthermore, the immobilized PPL after detoxification still kept high yield and enzyme activity, and was reusable for usage of detoxification. Detoxification properties of the immobilized PPL could represent a novel strategy for a possible application in decontaminating patulin aqueous solutions.