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Enzyme Activity Measurement for Acetylxylan Esterase

With years of exploration in enzymology assays, Creative Enzymes has emerged as a worldwide leader in the supply of enzyme activity assays. As a reliable provider, our technical enzyme experts created most suitable assay methods for virtually any enzyme application. Fully equipped with the most advanced spectrophotometric instrument, we assure the performance of our projects in a professional and timely manner. Herein, we are honored to provide the accurate enzyme assays for acetylxylan esterases.

Acetylxylan esterases (EC 3.1.1.72; AXEs) are enzymes that hydrolyze the ester linkages of the acetyl groups in positions 2 and/or 3 of the xylose moieties of the natural acetylated xylan fragments. Such acetyl ester groups are commonly found in hardwoods, cereals, and other annual plants. On the basis of their sequence similarities and tertiary structures, acetylxylan esterases have been classified into seven carbohydrate esterase (CE) families, CE1-CE7. Acetylxylan esterases also show activity towards a broad range of acetylated compounds such as xylose tetraacetate, glucose pentaacetate, as well as p-nitrophenyl acetate, α-naphtyl acetate, 7-aminocephalosporanic acid (7-ACA), and cephalosporin-C (Figure 1B). This multi-functional deacetylase activity is a common feature of the currently identified oligomeric α/β hydrolases belonging to CE7. Note that, complete biodegradation of natural acetylated xylan requires the cooperation of other enzymes along with acetylxylan esterases.

Enzyme Activity Measurement for Acetylxylan Esterase Figure 1: Reactions catalyzed by CE7 esterase family: (A) Deacetylation of short xylooligosaccharides; (B) Deacetylation of cephalosporin-C.
Reference: Krastanova I, Guarnaccia C, Zahariev S, et al. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 2005, 1748(2): 222-230.

Acetylxylan esterases have been found in and produced by a wide variety of microorganisms in nature. Among them, fungal acetylxylan esterases are most commercially important because of their high activity, good stability, and broader substrate diversity as a result of their diverse inhabitant environments in nature. Acetylxylan esterases have yet to be described in plants where they could play an important role in the process of cell wall growth and aging. In addition, acetylxylan esterases can be exploited in biofuel production and the pharmaceutic industry. Therefore, the significant utilization promotes a strong demand for monitoring the activity of acetylxylan esterases.


Having tested activities various enzymes in the past few years, Creative Enzymes is qualified for providing the most reliable enzymatic assays for acetylxylan esterases. Activities of acetylxylan esterases are assayed spectrophotometrically using either α-naphthyl acetate or p-nitrophenyl acetate as substrates. One unit of activity is defined as the amount of enzyme required to produce 1 μmol of α-naphthol or p-nitrophenol per minute. When using α-naphthyl acetate as the substrate, the released α-naphthol is determined at a wavelength of 560 nm using the most advanced spectrophotometer. When using p-nitrophenyl acetate as the substrate, the released p-nitrophenol is determined at a wavelength of 410 nm. The results of our test are assured with high accuracy by our state-of-the-art technology. We promise that the results will be delivered in the shortest span of time from the date of order submission. Overall, Creative Enzymes is your best choice of activity measurement, and we believe that we will become your most ideal research partner in the future.

Enzyme Activity Measurement for Acetylxylan Esterase Figure 2: The crystal structure of acetylxylan esterase from Geobacillus stearothermophilus.
PDB: 4JHL



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