Abstract
The enzyme β-galactosidase was entrapped in poly(N-isopropylacrylamide) gel. The gel swelled or collapsed sharply upon the rise or fall of environmental pressure. The gel beads, prepared by reverse suspension polymerization, were placed in a stirred batch reactor filled with a solution of the substrate o-nitrophenol β-D-galactopyranoside. Operations under constant or cycling pressure were performed. A considerable increase in conversion rate was observed under pressure cycling operation, compared with isobaric operations at either atmospheric or high pressure. This result could be explained by the enhancement of mass transfer inside the gel beads during the pressure cycling operation.
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