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Stability of Solid-Supported Enzyme Catalysts for Ring-Opening Polymerization

Published

Author(s)

Sara V. Orski, Santanu S. Kundu, Kathryn L. Beers, Richard Gross

Abstract

The enzyme Candida antarctica Lipase B (CAL B), immobilized on a crosslinked poly(methyl methacrylate) (PMMA) support, catalyzes the ring-opening polymerization of ε-caprolactone to make biodegradable polyesters. Weak hydrophobic interactions of CAL B physisorbed on the PMMA surface can permit catalyst leaching, decreasing the concentration of remaining enzymes for polymerization and contaminating the polycaprolactone (PCL) product. Recycling of the solid-supported polymerization catalyst is necessary for commercialization; this requires a thorough understanding of catalyst activity, stability and surface interactions under varied reaction conditions. A quartz crystal microbalance (QCM) was used to monitor in situ adsorption at the solid-support/enzyme interface, while deconvoluting background events, such as polymer swelling or non-specific binding. A crosslinked PMMA thin film (50nm) on a QCM crystal was fabricated to mimic the hydrophobic surface of the catalyst bead. Enzyme stability and PCL binding to the CAL B surface was monitored as water content of the reaction incrementally increased.
Proceedings Title
The 6th ACS Symposium on Green Polymer Chemistry: Polymer Biocatalysis and Biobased Materials
Conference Dates
August 18-23, 2012
Conference Location
Philidelphia, PA
Conference Title
The 244th Meeting of the American Chemical Society

Keywords

enzyme catalysis, ring-opening polymerization, green chemistry, surface chemistry

Citation

Orski, S. , Kundu, S. , Beers, K. and Gross, R. (2012), Stability of Solid-Supported Enzyme Catalysts for Ring-Opening Polymerization, The 6th ACS Symposium on Green Polymer Chemistry: Polymer Biocatalysis and Biobased Materials, Philidelphia, PA, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=911005 (Accessed July 6, 2022)
Created March 19, 2012, Updated February 19, 2017