Cutinase: A new biocatalyst for polyester synthesis via polycondensation reactions

POLY 675

Abul Azim, Mo Hunsen, Harald Mang, Sabine R. Wallner, swallner@poly.edu, Asa Ronkvist, Wenchun Xie, wen4192001@yahoo.com, and Richard A. Gross, rgross@poly.edu. NSF I/UCRC for Biocatalysis and Bioprocessing of Macromolecules, Department of Chemical and Biological Sciences, Polytechnic University, 6 Metrotech Center, Brooklyn, NY 11201
Enzymes, predominantly lipases, are surprisingly active for a wide range of polyester and polycarbonate synthetic reactions. As part of our search for novel enzyme-catalysts for polymer synthesis, studies have begun on members of the cutinase family. Cutinases are extra-cellular fungal enzymes whose natural function is hydrolyzing cutin ester bonds. Cutin is a lipid-polyester found in the cuticle of higher plants. The cutinase from Humicola insolens was studied for condensation polymerization reactions between several diols and diacids. Humicola insolens cutinase, immobilized on Lewatit, showed optimal activity at 70°C and catalyzed the syntheses of polyesters with Mn values up to 19 000. This discovery paves the way for a deeper investigation into cutinases to uncover their potential use as polymerization catalysts.
 

Biocatalysis in Polymer Science
8:30 AM-11:45 AM, Thursday, 14 September 2006 San Francisco Marriott -- Salon 12/13, Oral

Division of Polymer Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006