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Low Temperature Biomass Deconstruction by Zeolite-encapsulated Enzyme Mimics

Published online by Cambridge University Press:  29 July 2011

L. Shannon Davis*
Affiliation:
Department of Chemistry, 250 Forest Drive, Georgia Southern University, Statesboro, GA, USA 30460
Thomas T. Eisenhart
Affiliation:
Department of Chemistry, 250 Forest Drive, Georgia Southern University, Statesboro, GA, USA 30460
Brianna C. Hughes
Affiliation:
Department of Chemistry, 250 Forest Drive, Georgia Southern University, Statesboro, GA, USA 30460
Amy L. Pressley
Affiliation:
Department of Chemistry, 250 Forest Drive, Georgia Southern University, Statesboro, GA, USA 30460
*
* Corresponding Author, email: sdavis@georgiasouthern.edu, phone (912) 478-5055, fax (912) 478-0699
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Abstract

Oxidation catalysis is a reaction necessary for the production of plastics and other materials that seem now essential to our everyday lives. Unfortunately, most oxidation processes suffer from poor selectivity or yields, creating unwanted byproducts and waste. In nature, oxidative enzymes like methane monooxygenase and the family of cytochromes provide a more selective method for oxidation of organic compounds. Of particular interest is the low temperature, selective oxidation of cellulosic biomass for the production of biofuels or other useful replacements for materials currently derived from petroleum feedstocks. An enzymatic approach could replace the high temperature pyrolysis technology in use today. A series of inorganic mimics of some oxidative enzymes, using transition metal – amino acid complexes encapsulated in large pore zeolites have been synthesized and examined as oxidation catalysts under benign conditions. Several of these demonstrate turnovers comparable to native enzymes in the reaction of model compounds for the oxidation of lignin and cellulose.

Type
Research Article
Copyright
Copyright © Materials Research Society 2011

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References

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