芽孢杆菌属SPS-0菌株中一种中度耐热木聚糖酶的纯化与特性分析
Purification and characterization of a moderately thermostable xylanase from Bacillus sp. strain SPS-0.
作者信息
Bataillon M, Castillon N, Duchiron F
机构信息
Laboratoire de Microbiologie Industrielle, Université de Reims-Champagne-Ardenne, BP 1039, 51687, Reims Cedex, France
出版信息
Enzyme Microb Technol. 2000 Feb 1;26(2-4):187-192. doi: 10.1016/s0141-0229(99)00143-x.
A Bacillus spp. strain SPS-0, isolated from a hot spring in Portugal, produced an extracellular xylanase upon growth on wheat bran arabinoxylan. The enzyme was purified to homogeneity by ammonium sulfate precipitation, anion exchange, gel filtration, and affinity chromatography. The optimum temperature and pH for activity was 75 degrees C and 6.0. Xylanase was stable up to 70 degrees C for 4 h at pH 6.0 in the presence of xylane. Xylanase was completely inhibited by the Hg(2+) ions. beta-Mercaptoethanol, dithiothreitol, and Mn(2+) stimulated the xylanase activity. The products of birchwood xylan hydrolysis were xylose, xylobiose, xylotriose, and xylotetraose. Kinetic experiments at 60 degrees C and pH 6.0 gave V(max) and K(m)values of 2420 nkat/mg and 0.7 mg/ml.
从葡萄牙的一处温泉中分离出的一株芽孢杆菌属菌株SPS-0，在以麦麸阿拉伯木聚糖为生长底物时可产生一种胞外木聚糖酶。该酶通过硫酸铵沉淀、阴离子交换、凝胶过滤和亲和层析纯化至均一状态。其活性的最适温度和pH分别为75℃和6.0。在木聚糖存在的情况下，木聚糖酶在pH 6.0时于70℃下可稳定存在4小时。木聚糖酶完全被Hg(2+)离子抑制。β-巯基乙醇、二硫苏糖醇和Mn(2+)可刺激木聚糖酶的活性。桦木木聚糖水解产物为木糖、木二糖、木三糖和木四糖。在60℃和pH 6.0条件下进行的动力学实验得出V(max)和K(m)值分别为2420 nkat/mg和0.7 mg/ml。
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