Paper Title
In-Silico Studies of Glycosyltransferase Enzyme Involved in Exopolysaccharide Production

Abstract
Glycosyltransferase belongs to a family of enzymes that moves stimulated sugar moieties to the acceptor substrate. GTF genes have been involved in the formation of bacterial exopolysaccharides (EPS), capsular polysaccharide and lipopolysaccharide. They are found in both prokaryotes and eukaryotes. In humans, they are involved cell signaling, adhesion, cancer and cell wall biosynthesis. As the interest in natural polysaccharides has expanded, EPS is considered for use in drugs, food and other industries and it can be likewise valuable for the agriculture and biotechnology sectors. Thermophiles can be a novel organism for the production of EPS as they possess a lot of properties such as high metabolism, produce physically and chemically stable enzymes and lower growth but higher end-product yields than similar mesophilic species which is valuable for industries. In this study, we have compared five thermophiles and five mesophiles to analyze the differences between glycosyltransferase enzymes using the in-silico approach. According to the result of physicochemical determination, the GRAVY value is found to be higher in mesophiles than in thermophiles. The Aliphatic index is higher in thermophile which is a positive factor for the increase of thermostability of the given protein. Primary structure analysis reveals that Alanine and Isoleucine are dominant in thermophiles as compared to mesophiles. Thermophiles are seen to balance positive and negative amino acids only. Thermophiles have fewer polar amino acids which indicate that they have a tendency to decrease destabilizing amino acids. In thermophiles and mesophiles most of the structure is alpha-helix followed by random coil which indicates true enzymatic activity and structural flexibility. Keywords - Thermostability, Aliphatic index, GRAVY value, In-silico, Exopolysaccharide