Liaoning Provincial Key Laboratory of Carbohydrates, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China; University of Chinese Academy of Sciences, Beijing 100049, China.
College of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, China.
Int J Biol Macromol. 2018 Jun;112:937-942. doi: 10.1016/j.ijbiomac.2018.02.046. Epub 2018 Feb 9.
A new oligoalginate lyase encoding gene, designed oal17A, was cloned from marine bacterium Vibrio sp. W13, and then expressed in Escherichia coli. The recombinant Oal17A was purified by NTA-Ni resin with maximal activity at 30°C and pH7.0. Oal17A exhibited broad substrate specificity, and preferred to degrade alginate than polyM or polyG into monosaccharide acid. The specific activity of Oal17A toward alginate, polyM and polyG was 21.14U/mg, 12.31U/mg and 7.43U/mg, respectively. With features of high-level expression and broad substrate specificity, Oal17A would be a potential tool for alginate monomer production process of alginate utilizing for biofuels and bioethanol production.
从海洋细菌 Vibrio sp. W13 中克隆了一种新的寡聚海藻酸盐裂解酶编码基因，命名为 oal17A，并在大肠杆菌中表达。重组 Oal17A 经 NTA-Ni 树脂纯化，最适活性为 30°C 和 pH7.0。Oal17A 表现出广泛的底物特异性，优先将海藻酸盐降解为单糖酸，而不是聚 M 或聚 G。Oal17A 对海藻酸盐、聚 M 和聚 G 的比活性分别为 21.14U/mg、12.31U/mg 和 7.43U/mg。Oal17A 具有高水平表达和广泛底物特异性的特点，有望成为海藻酸盐单体生产过程的潜在工具，用于生物燃料和生物乙醇生产中的海藻酸盐利用。
