Used primarily in biochemical research as a chromogenic substrate for assaying glycosidase enzymes, particularly those involved in carbohydrate degradation such as β-xylosidases. The structure mimics natural substrates, enabling measurement of enzyme activity. The nitrophenyl group serves as a chromogenic tag; upon enzymatic cleavage of the glycosidic bond, it releases a colored nitrophenol product, allowing direct monitoring of the reaction through colorimetric changes, typically at around 400 nm. The acetyl protecting groups enhance stability. Commonly employed in spectroscopic assays for real-time kinetic analysis, enzyme screening, and inhibitor studies in laboratory settings.