Abstract
Colorimetric detection of reaction products is typically preferred for initial surveys of acetyl xylan esterase (AcXE) activity. This chapter will describe common colorimetric methods, and variations thereof, for measuring AcXE activities on commercial, synthesized, and natural substrates. Whereas assays using pNP-acetate, α-naphthyl acetate, and 4-methylumbelliferyl acetate (4MUA) are emphasized, common methods used to measure AcXE activity towards carbohydrate analogs (e.g., acetylated p-nitrophenyl β-d-xylopyranosides) and various acetylated xylans are also described. Strengths and limitations of the colorimetric assays are highlighted.
Key words
The original version of this chapter was revised. The erratum to this chapter is available at: DOI 10.1007/978-1-4939-6899-2_23
An erratum to this chapter can be found at http://dx.doi.org/10.1007/978-1-4939-6899-2_23
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Acknowledgments
This work was supported by a grant to G.M. from Ella and Georg Ehrnrooth foundation, Finland and an ERC Consolidator Grant to E.M. (BHIVE—648925). We thank Professor M. Tenkanen for her critical review of the manuscript.
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Mai-Gisondi, G., Master, E.R. (2017). Colorimetric Detection of Acetyl Xylan Esterase Activities. In: Abbott, D., Lammerts van Bueren, A. (eds) Protein-Carbohydrate Interactions. Methods in Molecular Biology, vol 1588. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6899-2_5
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