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. et al. β-d-Xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43. Appl Biochem Biotechnol 137, 93–104 (2007). https://doi.org/10.1007/s12010-007-9042-6
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DOI: https://doi.org/10.1007/s12010-007-9042-6