Date of Award

5-1-2014

Degree Type

Thesis

University or Center

Clark Atlanta University(CAU)

Degree Name

M.S.

Department

Chemistry

First Advisor

Dr. Eric A. Mintz

Second Advisor

Dr. David Logan

Third Advisor

Dr. Myron Williams

Abstract

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.

Signature Location_Supplemental file.pdf (45 kB)
Notice to Users, Transmittal and Statement of Understanding

Included in

Chemistry Commons

Share

COinS