Immobilization of lipase B within micron-sized poly-N-isopropylacrylamide hydrogel particles by solvent exchange.
The aim of the present work is the use of a water soluble enzyme in an organic solvent, still with a pronounced catalytic activity. Therefore, lipase B from Candida antarctica (CalB) is immobilized within micron-sized thermosensitive p-NIPAM hydrogel particles using a solvent exchange from polar to organic solvents. The absorbed amount of CalB is investigated at different immobilization temperatures. Confocal laser scanning microscopy (CLSM) shows that CalB is homogeneously distributed within the polymer network. An enhanced specific activity of CalB in n-hexane is achieved after immobilization within the p-NIPAM microgels. In order to get information on the supply of the substrate depending on the temperature, the activity is determined at different reaction temperatures. Additionally, the system is stable in the organic solvent, namely n-hexane, and shows a good reusability.
Technische Universität Berlin, Stranski-Laboratory for Physical and Theoretical Chemistry, Institute of Chemistry, 10623 Berlin, Germany.
Kornelia
K
Gawlitza
Changzhu
C
Wu
Radostina
R
Georgieva
Dayang
D
Wang
Marion B
MB
Ansorge-Schumacher
Regine
R
von Klitzing
D000180:Acrylic Resins / Q000737:chemistry*; D055162:Biocatalysis; D002175:Candida / Q000201:enzymology; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism; D006586:Hexanes / Q000737:chemistry; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate / Q000737:chemistry*; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D018613:Microscopy, Confocal; D012997:Solvents / Q000737:chemistry*; D013696:Temperature
D000180:Acrylic Resins; D004800:Enzymes, Immobilized; D006586:Hexanes; D012997:Solvents; C052970:poly-N-isopropylacrylamide; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate; C026385:n-hexane; D008049:Lipase