State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, 100101, China.
Biotechnol Lett. 2010 Dec;32(12):1915-20. doi: 10.1007/s10529-010-0372-z. Epub 2010 Aug 21.
A xylanase gene (xyn10) from alkaliphilic Bacillus sp. N16-5 was cloned and expressed in Pichia pastoris. The deduced amino acid sequence has 85% identity with xylanase xyn10A from B. halodurans and contains two potential N-glycosylation sites. The glycosylated Xyn10 with MW 48 kDa can hydrolyze birchwood and oatspelt xylan. The enzyme had optimum activity at pH 7 and 70°C, with the specific activity of 92.5U/mg. The Xyn10 retained over 90% residual activity at 60°C for 30 min but lost all activity at 80°C over 15 min. Most tested ions showed no or slight inhibition effects on enzyme activity.
从嗜碱性芽孢杆菌 N16-5 中克隆并在毕赤酵母中表达了木聚糖酶基因（xyn10）。推导的氨基酸序列与来自嗜盐杆菌的木聚糖酶 xyn10A 具有 85%的同一性，并且包含两个潜在的 N-糖基化位点。MW 为 48 kDa 的糖基化 Xyn10 可以水解桦木和燕麦木聚糖。该酶在 pH 7 和 70°C 下具有最佳活性，比活性为 92.5U/mg。Xyn10 在 60°C 下保持超过 90%的剩余活性 30 分钟，但在 80°C 下超过 15 分钟失去所有活性。大多数测试离子对酶活性没有或只有轻微的抑制作用。
