College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Key Laboratory of Biopesticide and Chemical Biology, Ministry of Education, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Mar Drugs. 2022 Jul 26;20(8):479. doi: 10.3390/md20080479.
The applications of alginate lyase are diverse, but efficient commercial enzymes are still unavailable. In this study, a novel alginate lyase with high activity was obtained from the marine bacteria sp. Ni1. The ORF of the B gene has 1824 bp, encoding 607 amino acids. Homology analysis shows that AlgB belongs to the PL7 family. There are two catalytic domains with the typical region of QIH found in AlgB. The purified recombinant enzyme of AlgB shows highest activity at 35 °C, pH 8.0, and 50 mmol/L Tris-HCl without any metal ions. Only K slightly enhances the activity, while Fe and Cu strongly inhibit the activity. The AlgB preferred polyM as substrate. The end products of enzymatic mixture are DP2 and DP3, without any metal ion to assist them. This enzyme has good industrial application prospects.
海藻酸钠裂解酶的应用多种多样，但高效的商用酶仍然难以获得。在本研究中，从海洋细菌 sp. Ni1 中获得了一种具有高活性的新型海藻酸钠裂解酶。B 基因的 ORF 长 1824bp，编码 607 个氨基酸。同源性分析表明 AlgB 属于 PL7 家族。AlgB 中存在两个具有典型 QIH 区域的催化结构域。纯化的 AlgB 重组酶在无任何金属离子的情况下，最适反应条件为 35°C、pH8.0 和 50mmol/LTris-HCl。只有 K 轻微提高了酶活，而 Fe 和 Cu 强烈抑制酶活。AlgB 优先作用于多聚 M 作为底物。酶混合物的终产物是 DP2 和 DP3，无需任何金属离子协助。该酶具有良好的工业应用前景。
