Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2047627 | FEBS Letters | 2015 | 6 Pages |
•Crystal structure of a carbohydrate acetylesterase (Sm23) was determined.•Hydrolysis of acetylated substrates by Sm23 and S10A mutant was investigated.•Immobilized Sm23 exhibited improved stability compared with soluble Sm23.
In many microorganisms, carbohydrate acetylesterases remove the acetyl groups from various types of carbohydrates. Sm23 from Sinorhizobium meliloti is a putative member of carbohydrate esterase family 3 (CE3) in the CAZy classification system. Here, we determined the crystal structure of Sm23 at 1.75 Å resolution and investigated functional properties using biochemical methods. Furthermore, immobilized Sm23 exhibited improved stability compared with soluble Sm23, which can be used for the design of plant cell wall degrading-systems.