Polysaccharides are normal macromolecules composed of various sugar repeat units. Bacterial cellulose exopolysaccharides have wide applications from food to cosmetics and are therefore attracting the great attention of several researchers. There are several enzymes for catalysing the final product in the cellulose processing pathway. The major role in this development is played by cellulose synthase A as the catalytic subunit. The physiochemical characteristics of Pseudomonas of this silico enzyme catalytic subunit indicated that molecular weights ranged from 78kDa to 99kDa. This catalytic enzyme subunit is insoluble and two disulphide bonds have been found in the structure of some of them (A0A560SVT9, A0A2N8ERT3). In addition, aromatic residues were about 11 percent to 12 percent and pseudomonas cellulose synthase A isoelectric point (pI) was 8.6 (A0A1B4X6C1) to 9.74 (A0A1B4X6C1) (A0A5N9I3A8). The Aliphatic Index (AI) was in the range of 102.4 to 104.04.04 (A0A1B4X6C1) (A0A5N9I3A8). The Grand Average Hydropathy (GRAVY) was lower than 0.218, suggesting the insolubility of the enzymes in these catalytic subunits. The knowledge provided here on the structural and conformation characteristics of Pseudomonas cellulose synthase A may provide new insight into enzyme engineering and microbial cellulose development classifications.
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