Biological regeneration of water and organic sorbents used in the absorption of hydrophilic and hydrophobic pollutants, respectively, was studied. In both cases biodegradation takes place in a membrane bioreactor. In the case of organic sorbents regeneration of the biodegradation process is integrated with the extraction of a given pollutant to water phase. In experiments carried out in this work, the proposed systems were tested using a strain of Pseudomonas fluorescens. For hydrophilic compounds experiments were performed using alcohols (1-butanol and 2-propanol) as model substrates. Applying the mathematical model of a membrane bioreactor elaborated previously, the values of pollutant concentration were determined and positively verified in the experiments. This system of water sorbent regeneration is fully satisfying. The process of biodegradation integrated with extraction was analysed on the basis of model compounds such as benzene and toluene. The study confirmed a possibility of organic sorbent (silicone oil) regeneration. However, due to a very high partition coefficient of benzene or toluene between the organic and aqueous phases, the process could be considered only for the case of their high concentrations in the gas directed to absorption.
In this study, β-galactosidase enzyme from Kluyveromyces fragilis was immobilised on a commercial polyethersulfone membrane surface, 10 kDa cut-off. An integrated process, concerning the simultaneous hydrolysis-ultrafiltration of whey lactose was studied and working conditions have been fixed at 55°C and pH 6.9, the same conditions that are used for the industrial process of protein concentration. For the immobilisation, best results were obtained using 5% (v/v) of glutaraldehyde solution and 0.03 M galactose; the total activity recovery coefficient (TARC) was 44.2%. The amount of immobilised enzyme was 12.49 mg with a total activity of 86.3 LAU at 37°C, using 5% (w/v) lactose solution in phosphate buffer (100 mM pH 6.9). The stability of the immobilised enzyme was approximately 585 fold higher in comparison with the stability of free enzyme. Multipoint covalent immobilisation improves the stability of the enzyme, thereby enhancing the decision to use the membrane as a filtering element and support for the enzyme immobilisation.