Department of Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, Lund, Sweden.
Mol Biotechnol. 2006 Jun;33(2):149-59. doi: 10.1385/MB:33:2:149.
The gene encoding an alkaline active xylanase of Bacillus halodurans S7, containing an open reading frame of 1188 nucleotides encoding 396 amino acids, was cloned and expressed in Escherchia coli. On the basis of sequence similarity, possible -10 and -35, ribosome binding, and transcription terminator regions were identified. Analysis of the deduced amino acid sequence revealed that the protein was a single domain enzyme belonging to family 10 and designated as xyn10A. The calculated molecular mass and isoelectric point (pI) of the mature peptide were 42.6 and 4.5 kDa, respectively. Xylanase activity expressed by the recombinant organism was detected in the cytoplasm, periplasm and the extracellular medium. In an 18-h old culture, about 39% of the xylanase was detected in the medium. The stability and activity profile of the recombinant xylanase was similar to the properties of the enzyme produced by the wild-type organism.
嗜盐杆菌 S7 的碱性木聚糖酶基因的编码序列，包含一个开放阅读框，编码 396 个氨基酸，该基因已在大肠杆菌中克隆和表达。根据序列相似性，可能的-10 和-35 核糖体结合和转录终止区被鉴定出来。对推导的氨基酸序列进行分析表明，该蛋白是一种属于第 10 家族的单一结构域酶，命名为 xyn10A。成熟肽的计算分子量和等电点（pI）分别为 42.6 和 4.5 kDa。重组菌表达的木聚糖酶活性在细胞质、周质和细胞外培养基中被检测到。在 18 小时的培养中，约 39%的木聚糖酶存在于培养基中。重组木聚糖酶的稳定性和活性谱与野生型酶的性质相似。
