Date of Award
University or Center
Clark Atlanta University(CAU)
Dr. Eric A. Mintz
Dr. David Logan
Dr. Myron Williams
Enzyme immobilization is a process by which an enzyme is chemically or physically attached to a carrier to impart better physical and chemical properties than free enzymes would exhibit outside of its natural environment. In addition, enzyme immobilization leads to increased stability and ease of separation from products when applied to organic synthesis or industrial processes.
In this study we attempted to immobilize laccase enzyme on bacterial cellulose by standard methods; aminopropylsilation reaction followed by crosslinking the enzyme with gluteraldehyde and by partial oxidation followed by direct reaction with the enzyme. However, both were unsuccessful.
Laccase enzyme was successfully incorporated in bacterial cellulose by adding it to growth media and Acteobactor xylinum and carrying out biosynthesis for two to three days. This process was repeated successfully with horseradish peroxidase and the photocatalyst titanium dioxide. The stability, reusability, and activity of the immobilized biocatalyst and photocatlyst were measured.
Miller, Ebony, "Immobilization of catalyst by the biosynthesis of bacterial cellulose in the presence of laccase, horseradish peroxidase, and titanium dioxide" (2014). ETD Collection for AUC Robert W. Woodruff Library. 1527.