STM Article Repository

Polysaccharides are natural macromolecules that consist of repeated units of different sugars. Cellulose exopolysaccharides from bacterial origin have wide applications from food to cosmetic and therefore gain the great attentions by many researchers. The pathway of cellulose production has many enzymes for catalyzing final product. Cellulose synthase A as the catalytic subunit plays the important role in this production. Pseudomonas physiochemical features of this enzyme catalytic subunit with in silico revealed that molecular weights were in the range of 78kDa to 99kDa. This catalytic subunit of the enzyme is insoluble and two disulphide bonds were observed in the structure of some of them (A0A560SVT9, A0A2N8ERT3). Furthermore aromatic residues were around 11% to 12% and Isoelectric point (pI) of pseudomonas cellulose synthases A were 8.6 (A0A1B4X6C1) to 9.74 (A0A5N9I3A8). The Aliphatic Index (AI) were in the range of 102.4 (A0A1B4X6C1) to 104.04 (A0A5N9I3A8). The Grand Average Hydropathy (GRAVY) was lower than 0.218 which indicated the insolubility of these catalytic subunits of the enzymes. The information highlighted here on structural and conformational features of Pseudomonas cellulose synthase A can provide new insight for enzyme engineering and classification towards microbial cellulose production.