REVERSED MICELLAR EXTRACTION OF CHARGED FUSION PROTEINS

We have investigated the use of charged fusion tails with the enzyme g lucoamylase in reversed micellar extraction. The addition of the charg ed tails increased the fraction of enzymatically active protein recove red at a given pH, with the tails containing the largest number of cha rges being recovered at the highest level. The series of mutations als o allows for investigation of the charge-dependent behavior of reverse d micellar extraction. However, in this case, the change in protein ch arge via fusions had a lesser impact than did the change in charge via a pH change. The difference may be due to the difficulty of partition ing the hydrodynamically larger fusion protein.