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. 1996 Nov 1;319(Pt 3):881–886. doi: 10.1042/bj3190881

Purification and characterization of an acetyl xylan esterase produced by Streptomyces lividans.

C Dupont 1, N Daigneault 1, F Shareck 1, R Morosoli 1, D Kluepfel 1
PMCID: PMC1217870  PMID: 8920994

Abstract

The acetyl xylan esterase cloned homologously from Streptomyces lividans [Shareck, Biely, Morosoli and Kluepfel (1995) Gene 153, 105-109] was purified from culture filtrate of the overproducing strain S. lividans IAF43. The secreted enzyme had a molecular mass of 34 kDa and a pI of 9.0. Under the assay conditions with chemically acetylated birchwood xylan the kinetic constants of the enzyme were: specific activity, 715 units/mg, Km 7.94 mg/ml and Vmax 1977 units/mg. Optimal enzyme activity was obtained at 70 degrees C and pH 7.5. Hydrolysis assays with different acetylated substrates showed that the enzyme is specific for deacetylating the O-acetyl group of polysaccharides and is devoid of N-deacetylation activity. Sequential hydrolysis shows that its action is essential for the complete degradation of acetylated xylan by the xylanases of S. lividans.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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