Date of Completion
Dr.Rajeswari M.Kasi,Dr.Jing Zhao
Field of Study
Master of Science
Proteins are biological molecules that have an important application as a catalyst for various reactions. The sensitivity of protein to denature at high temperature limits its industrial application where a catalyst that works at high temperature is required. Some protein denature even at optimal room temperature. The primary interest of this study is to protect the protein for thermal denaturation by stabilizing proteins within the capric acid (a ten-carbon chain fatty acid) micelle. The protein-Capric acid adducts showed reversible thermal denaturation when the Capric acid (CA) concentration was present above the critical micellar concentration (CMC). Although the secondary structure was protected for thermal denaturation the activity was lost for most of the proteins studied and SDS-PAGE gel showed that covalent modification of protein with capric acid resulted in high temperature heating. Thus a new lipoprotein material was synthesized by heating protein with capric acid (CA). Bovine serum albumin (BSA)-capric acid adduct was used in this study to build an efficient simple artificial energy transfer complex.
Keywords: Capric acid,SDS-PAGE gel,Bovine serum albumin,Antenna complex
Dharmaraj, Dhurga, "Structural and Thermal Stability Characterization of Protein-Fatty acid Adducts" (2015). Master's Theses. 713.
Dr.Challa Vijaya Kumar