An extracellular xylanase (EC 3.2.1.8) was purified approximately 20-fold from liquid cultures of Erwinia chrysanthemi strain SR120A grown with glycerol as a carbon source. Ammonium sulphate fractionation, cation-exchange chromatography (CM-Sephadex), chromatofocusing, and gel filtration (Sephadex G-75) isolated the enzyme from culture filtrates. The xylanase had a molecular mass of approximately 42 kDa and had a pI of 8.8. The pH optimum was 5.5, and the temperature optimum in a 10-min assay was 55 C. About 40% of the enzyme activity was lost after incubating for 1 h at 40 C []
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E. J. Braun (1993) studied this question.