Immobilization of lipase with alginate hydrogel beads and the lipase‐catalyzed kinetic resolution of α‐phenyl ethanol
Citations Over TimeTop 23% of 2013 papers
Abstract
ABSTRACT The immobilization of enzymes is one of the key issues in both the field of enzymatic research and industrialization. In this article, we report a facile method for immobilizing Candida antarctica lipase B in an alginate carrier. In the presence of calcium cations, an enzyme–alginate suspension was crosslinked to form beads with a porous structure at room temperature, and the enzymes were well dispersed in the beads. The chiral resolution of α‐phenyl ethanol in the organic phase was tested by the enzyme–alginate beads. The effects of the reaction parameters, such as the enzyme concentration, temperature, and molar ratio of the substrate to the solvent, on the resolution behavior are discussed. Reuse cycle experiments for the chiral resolution of α‐phenyl ethanol demonstrated that the activity of the enzyme–alginate beads was maintained without marked deactivation up to five repeated cycles. © 2013 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2014 , 131 , 40178.
Related Papers
- → Highly Enantioselective Resolution of β‐Amino Esters by Candida antarctica Lipase A Immobilized in Mesocellular Foam: Application to Dynamic Kinetic Resolution.(2010)72 cited
- → Combining Pd nanoparticles on MOFs with cross-linked enzyme aggregates of lipase as powerful chemoenzymatic platform for one-pot dynamic kinetic resolution of amines(2019)30 cited
- → Enantiopure N‐Benzyloxycarbonyl‐β2‐amino Acid Allyl Esters from Racemic β‐Lactams by Dynamic Kinetic Resolution using Candida antarctica Lipase B(2015)14 cited
- → Enzyme‐Catalyzed Kinetic Resolution of 2,2,2‐Trifluoro‐1‐(heteroaryl)ethanols: Experimental and Docking Studies(2014)11 cited
- → ChemInform Abstract: Synthesis of a Novel Ruthenium(II) Complex and Its Unique Behaviors in Enzymatic Dynamic Kinetic Resolution of Secondary Alcohols.(2010)