Abstract
An Escherichia coli is difficult to secret products such as recombinant enzymes, because gram-negative bacterium has double membrane structure, so some of the products are accumulated in a periplasmic space. In this study, we demonstrated that recombinant α-amylase could be released from recombinant E. coli HB101/pHI301A during cultivation by pulsed electric field (PEF) treatment. When the process of applying PEF (12 kV, 2 Hz) for 30 min with an interval of 30 min from the point of OD660=0.7, the amount of released α-amylase was reached to about 30% of total amount of -amylase which produced in cells. PEF treatment could be useful for easy release of periplasmic protein with selectivity.
