Partitioning of acid protease from Penicillium roqueforti in aqueous two-phase system polyethylene glicol/phosphate

Abstract

The partitioning of acid protease produced by submerged fermentation of Penicillium roqueforti in the aqueous two-phase system polyethylene glycol/sodium phosphate was studied. In the system with 15% polyethylene glycol 4000/25% NaH2PO4 favourable partition coefficient and the top phase yield were obtained, 2.651 and 56.51%, respectively. The purification of acid protease from crude enzyme was optimized by optimizing separation factor. Completely randomized factorial design was applied and the system 15.54% PEG 4000/20% NaH2PO4 appeared to be optimal. Statistically calculated separation factor of 3.553, was similar to the experimentally obtained value (3.084), which indicates the possible application of the factorial design onto ATPS partition and purifycation

Liquid-liquid extraction of protease from cold-adapted yeastRhodotorula mucilaginosaL7 using biocompatible and biodegradable aqueous two-phase systems

“…As discussed, our protease recovery results are similar to or even higher than those reported by other authors, where PEG/salt ATPS were also used to purify different enzymes (38,(40)(41)(42)(43)(44)(45)(46). Furthermore, although the PF obtained in our study were generally lower than other systems reported in the literature, it is important to note that this parameter is directly related with to the initial protease/total protein ratio.…”

“…A large number of studies that analyzed the recovery of proteases in PEG/phosphate ATPS have been performed (42)(43)(44)(45)(46), in which the PF and Y values for the partitioning of the proteases were similar to the values reported by our group. However, the concentration of phosphate used in these systems was between 15-50 wt %, which leads to environmental concerns, avoiding a large industrial application.…”