Abstract
The enzyme β-galactosidase has been immobilized within thermally reversible hydrogel beads that exhibit LCST (lower critical solution temperature) behavior. The hydrogel beads containing the immobilized enzymes swell and expand below the LCST and deswell and shrink above the LCST. This behavior is reversible. The enzyme was physically entrapped in a crosslinked hydrogel of a copolymer of N-isopropylacrylamide (NIPAAm) and acrylamide (AAm), and formed as beads in an inverse suspension polymerization. The beads were placed in a packed bed column reactor which was operated in a continuous, single pass mode, either isothermally at 30 or 35°C, or with temperature cycling between 30 and 35°C. The thermal cycling significantly enhanced overall reactor enzyme activity relative to isothermal operation at either the higher or lower temperature. It is postulated that mass transfer rates within the hydrogel beads are greatly enhanced by the movement of water in and out of the beads during the expansion or collapse of the polymer chain network as temperature is cycled.
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Park, T.G., Hoffman, A.S. Effect of temperature cycling on the activity and productivity of immobilized β-galactosidase in a thermally reversible hydrogel bead reactor. Appl Biochem Biotechnol 19, 1–9 (1988). https://doi.org/10.1007/BF02921460
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DOI: https://doi.org/10.1007/BF02921460