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Cellulase‐Polymer Bioconjugates to Improve Enzyme Stability for Biofuel Production
Author(s) -
Stewart Jamie,
Wright Thai,
Schmitz Benjamin,
Williams Cameron,
Makaroff Katherine,
Konkolewicz Dominik,
Page Richard C
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.951.6
Subject(s) - cellulase , cellulosic ethanol , cellulose , biofuel , chemistry , pulp and paper industry , renewable resource , polymer , renewable energy , clostridium thermocellum , microbiology and biotechnology , biochemical engineering , biochemistry , organic chemistry , engineering , biology , electrical engineering
Protein polymer hybrids are bioconjugates that offer myriad customizations. The synthesis of these molecules allows for the opportunity to enhance proteolytic stability, manipulate the pH and temperature optimums of enzymes, and construct new and exciting biomaterials. To meet the increasing demands for biofuels, including mandates set by the US Renewable Fuel Standard II (RFS2), new enzymes with improved functionality and stability are desperately needed. Chief among these needs is the RFS2 directive that sets a target of increasing bioethanol production 600‐fold by 2022 and sets a cap on bioethanol that can be produced from grains. In contrast, cellulosic bioethanol produces glucose through enzyme‐mediated degradation of cellulose to produce a precursor that can be used for ethanol production by fermentation. Cellulosic bioethanol production therefore stands as an opportunity to capitalize on an under‐utilized resource, cellulose, to produce bioethanol. To increase the rate of cellulosic bioethanol production we have utilized the cellulase Fn Cel5a from thermophilic Fervidobacterium nodosum . We have produced cellulase‐polymer conjugates with improved chemical stability. Utilizing site‐directed mutagenesis we control the location of the polymer placement. Herein we present biochemical and biophysical analyses of cellulase‐polymer conjugate stability and activity conferred by interactions between the cellulase and conjugated dimethylacrylamide‐ or acrylamide‐based polymers. Our research seeks to achieve cost‐effective mass production of glucose from cellulose. As the demand for renewable energy increases, the need for rapid and efficient production of this renewable fuel source precursor is critical. Support or Funding Information The authors acknowledge financial support from Miami University through the Robert H. and Nancy J. Blayney Professorship (to RCP).