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

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 as...

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Veröffentlicht in:	Biochemical journal 1996-11, Vol.319 (3), p.881-886
Hauptverfasser:	Dupont, C, Daigneault, N, Shareck, F, Morosoli, R, Kluepfel, D
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylesterase - biosynthesis Acetylesterase - isolation & purification Acetylesterase - metabolism characterization Chromatography, High Pressure Liquid Chromatography, Ion Exchange Cloning, Molecular enzyme activity esterases Gene Expression heat stability hydrolysis Kinetics Molecular Weight Oligosaccharides - biosynthesis Oligosaccharides - chemistry purification Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Streptomyces Streptomyces - enzymology Streptomyces lividans Substrate Specificity substrates temperature Thermodynamics xylan
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