Blanco A, Vidal T, Colom J F, Pastor F I
Department of Microbiology, Faculty of Biology, University of Barcelona, Spain.
Appl Environ Microbiol. 1995 Dec;61(12):4468-70. doi: 10.1128/aem.61.12.4468-4470.1995.
Xylanase A from the recently isolated Bacillus sp. strain BP-23 was purified to homogeneity. The enzyme shows a molecular mass of 32 kDa and an isoelectric point of 9.3. Optimum temperature and pH for xylanase activity were 50 degrees C and 5.5 respectively. Xylanase A was completely inhibited by N-bromosuccinimide. The main products of birchwood xylan hydrolysis were xylotetraose and xylobiose. The enzyme was shown to facilitate chemical bleaching of pulp, generating savings of 38% in terms of chlorine dioxide consumption. The amino-terminal sequence of xylanase A has a conserved sequence of five amino acids found in xylanases from family F.
从最近分离出的芽孢杆菌属BP - 23菌株中纯化得到木聚糖酶A，使其达到同质纯品。该酶的分子量为32 kDa，等电点为9.3。木聚糖酶活性的最适温度和pH分别为50℃和5.5。N - 溴代琥珀酰亚胺可完全抑制木聚糖酶A。桦木木聚糖水解的主要产物是木四糖和木二糖。该酶被证明有助于纸浆的化学漂白，在二氧化氯消耗方面节省了38%。木聚糖酶A的氨基末端序列具有在F家族木聚糖酶中发现的五个氨基酸的保守序列。
