Stable biomimetic redox catalyst obtained by enzyme catalyzed amidation of Iron porphyrin

POLY 486

Subhalakshmi Nagarajan, mailtosubha@yahoo.com1, Ramaswamy Nagarajan, Ramaswamy_Nagarajan@uml.edu2, Ferdinando F. Bruno, Ferdinando_bruno@uml.edu3, Lynne A. Samuelson, Lynne_Samuelson@uml.edu3, and Jayant Kumar, Jayant_Kumar@uml.edu4. (1) Department of Chemistry, Center for Advanced Materials, University of Massachusetts, Lowell, One University Avenue, Lowell, MA 01854, (2) Center for Advanced Materials, Department of Plastics Engineering, One University Avenue, Lowell, MA 01854, (3) U.S Army Natick Soldier Center, RDECOM, Kansas Street, Natick, MA 01760, (4) Department of Physics, Center for Advanced Materials, University of Massachusetts, Lowell, One University Avenue, Lowell, MA 01854
Hematin is the stable, oxidized form of the free heme. Heme is the catalytic center of redox enzymes such as horseradish peroxidase (HRP). The use of Hematin as a catalyst for oxidative polymerization reactions has been restricted due to its limited aqueous solubility at lower pH conditions. While there have been reports on the functionalization of Hematin with poly(ethylene glycol), the esters formed are not very stable at low pH conditions. We report here the modification of Hematin with Methoxypolyethylene glycol amine. This one step synthesis was performed under solventless conditions and was catalyzed by a lipase, Novozyme–435. The amidation tremendously improved the stability of Hematin at low pH. Further, this catalyst was soluble in water and was able to catalyze the polymerization of phenol and aniline based monomers. The amide functionalized hematin serves as a robust cost-effective alternative to HRP and is stable at low pH conditions
 

Polymers from Renewable Resources
6:00 PM-8:00 PM, Tuesday, August 21, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Polymer Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007