Abstract
β-d-Xylosidase from the ruminal anaerobic bacterium, Selenomonas ruminantium (SXA), catalyzes hydrolysis of β-1,4-xylooligosacharides and has potential utility in saccharification processes. The enzyme, heterologously produced in Escherichia coli and purified to homogeneity, has an isoelectric point of approx 4.4, an intact N terminus, and a Stokes radius that defines a homotetramer. SXA denatures between pH 4.0 and 4.3 at 25°C and between 50 and 60°C at pH 5.3 Following heat or acid treatment, partially inactivated SXA exhibits lower k cat values, but similar K m values as untreated SXA. d-Glucose and d-xylose protect SXA from inactivation at high temperature and low pH.
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Jordan, D.B., Li, XL., Dunlap, C.A., Whitehead, T.R., Cotta, M.A. (2007). β-d-Xylosidase From Selenomonas ruminantium of Glycoside Hydrolase Family 43. In: Mielenz, J.R., Klasson, K.T., Adney, W.S., McMillan, J.D. (eds) Applied Biochemistry and Biotecnology. ABAB Symposium. Humana Press. https://doi.org/10.1007/978-1-60327-181-3_9
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DOI: https://doi.org/10.1007/978-1-60327-181-3_9
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