b-Glucosidase separation from Olea europaea fruit and its use in membrane bioreactors for hydrolysis of oleuropein

Fig. 1. SDS-page assay: lane 1, protein extract from Olea europaea (total volume 2 mL); lane 2, permeate; lane 3, retentate (total volume 2 mL); lane 4, b-glucosidase from almond. Protein mass (mg) Activity (mmol/min·mg) 1.20 1.00 Preliminary results showed that the purity of fruit extracts was improved by diafiltration. The process allowed obtaining better electrophoresis profiles and slightly improving enzyme activity in retentate solution. Immobilization of the b-glucosidase from purified solutions as well as from unpurified extracts has been performed. In the latter case, the immobilization permitted to load the enzyme and purify it at the same time.