淡紫链霉菌产生的乙酰木聚糖酯酶的纯化与特性分析
Purification and characterization of an acetyl xylan esterase produced by Streptomyces lividans.
作者信息
Dupont C, Daigneault N, Shareck F, Morosoli R, Kluepfel D
机构信息
Centre de Recherche en Microbiologie Appliquée, Université du Québec, Laval-des-Rapides, Canada.
出版信息
Biochem J. 1996 Nov 1;319 ( Pt 3)(Pt 3):881-6. doi: 10.1042/bj3190881.
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.
摘要
从淡紫链霉菌中同源克隆的乙酰木聚糖酯酶[Shareck、Biely、Morosoli和Kluepfel（1995年），《基因》第153卷，第105 - 109页]是从高产菌株淡紫链霉菌IAF43的培养滤液中纯化得到的。分泌的酶分子量为34 kDa，等电点为9.0。在以化学乙酰化桦木木聚糖为底物的测定条件下，该酶的动力学常数为：比活性715单位/毫克，Km为7.94毫克/毫升，Vmax为1977单位/毫克。在70℃和pH 7.5条件下可获得最佳酶活性。用不同乙酰化底物进行的水解试验表明，该酶对多糖的O - 乙酰基脱乙酰作用具有特异性，且没有N - 脱乙酰活性。连续水解表明，其作用对于淡紫链霉菌木聚糖酶完全降解乙酰化木聚糖至关重要。
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