A novel xylanase gene (denominated xynDRTY1) was identified from Tengchong hot spring by a metagenomic approach. Its amino acid sequence was 73.43% identical to a hypothetical protein from Bryobacterales bacterium. The codon-optimized XynDRTY1 gene was synthesized and overexpressed in Escherichia coli. The XynDRTY1 was purified by using Ni–NTA affinity chromatography. It exhibited activity with natural glycosides, such as beechwood xylan (21.2 ± 3 U/mg) and oat spelt xylan (8.2 ± 0.3 U/mg). Its optimum pH was determined to be 6.0 and optimum temperature of 65 ℃, along with its stability over 140% and 110% relative enzyme activity after incubation at 60 ℃ for 20 min and 120 min, respectively. Based on these findings, we believe that XynDRTY1, as thermostable xylanase, may prove useful for biotechnological applications.

通过宏基因组方法从腾冲温泉中鉴定出一个新的木聚糖酶基因（命名为xynDRTY1 ）。其氨基酸序列与来自苔藓菌目细菌的假设蛋白质具有 73.43 % 的同一性。密码子优化的 XynDRTY1 基因在大肠杆菌中合成并过表达. XynDRTY1 使用 Ni-NTA 亲和层析纯化。它对天然糖苷表现出活性，例如山毛榉木聚糖 (21.2 ± 3 U/mg) 和燕麦拼写木聚糖 (8.2 ± 0.3 U/mg)。确定其最适pH为6.0，最适温度为65 ℃，在60 ℃孵育20 min和120 min后，其相对酶活性的稳定性分别超过140%和110%。基于这些发现，我们相信作为耐热木聚糖酶的 XynDRTY1 可能证明对生物技术应用有用。