SOLID-SUPPORTED ENZYME CATALYST MODELS FOR RING-OPENING POLYMERIZATION

Published

April 27, 2012

Author(s)

Sara V. Orski, Santanu S. Kundu, Kathryn L. Beers, Richard A. 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 of CAL B at the solid-support interface, while deconvoluting background events, such as polymer swelling or non-specific binding. A crosslinked PMMA thin film (50 nm) on a QCM crystal was fabricated to mimic the hydrophobic surface of the catalyst bead. The morphology of the enzyme immobilized surface is smoother than the unmodified PMMA, indicating enzyme adsorption occurs in the outer pores of the PMMA surface.

Proceedings Title

Surfaces & Interfaces

Conference Dates

June 24-29, 2012

Conference Location

Blacksburg, VA

Conference Title

MACRO 2012: 44th Annual IUPAC World Polymer Congress

Pub Type

Conferences

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Keywords

ring-opening polymerization, enzyme catalysis, green chemistry, surfaces and interfaces

Citation

Orski, S. , Kundu, S. , Beers, K. and Gross, R. (2012), SOLID-SUPPORTED ENZYME CATALYST MODELS FOR RING-OPENING POLYMERIZATION, Surfaces & Interfaces, Blacksburg, VA, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=911097 (Accessed October 20, 2025)