Three Alginate Lyases from Marine Bacterium Pseudomonas fluorescens HZJ216: Purification and Characterization
Three Alginate Lyases from Marine Bacterium Pseudomonas fluorescens HZJ216: Purification and Characterization
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海洋荧光假单胞菌 HZJ216 的三种藻酸盐裂解酶：纯化和表征
DOI：
10.1007/s12010-010-9136-4
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发表时间：
2011-06
影响因子：
3
通讯作者：
Guo, Hong
中科院分区：
文献类型：
--
作者：
Li, Liyan;Jiang, Xiaolu;Guan, Huashi;Wang, Peng;Guo, Hong
从黄海褐藻中分离到一株褐藻酸降解菌HZJ 216，经初步鉴定为荧光假单胞菌（Pseudomonasfluorescens），分离纯化了3种褐藻酸裂解酶（A、B和C），并对其生化性质进行了研究。通过SDS-PAGE测定的三种酶的分子量分别为60.25、36和23 kDa，等电点分别为4、4.36和4.59。对这些酶在不同pH和温度下的研究表明，它们在pH 7.0和35 °C下最具活性。藻酸盐裂解酶A和B在5.0-9.0的pH范围内稳定，而藻酸盐裂解酶C在5.0-7.0的pH范围内稳定。在所测试的金属离子中，Na+、K+和Mg 2+离子的加入可以增强酶活性，而Fe 2+、Fe 3+、Ba 2+和Zn 2+离子表现出抑制作用。底物特异性结果表明，藻酸盐裂解酶C对G嵌段具有特异性，而藻酸盐裂解酶A和B对M和G嵌段都具有活性。这是荧光假单胞菌胞外海藻酸裂解酶的首次报道。
Three alginate lyases (A, B, and C) from an alginate-degrading marine bacterium strain HZJ216 isolated from brown seaweed in the Yellow Sea of China and identified preliminarily as Pseudomonas fluorescens are purified, and their biochemical properties are described. Molecular masses of the three enzymes are determined by SDS-PAGE to be 60.25, 36, and 23 kDa with isoelectric points of 4, 4.36, and 4.59, respectively. Investigations of these enzymes at different pH and temperatures show that they are most active at pH 7.0 and 35 °C. Alginate lyases A and B are stable in the pH range of 5.0–9.0, while alginate lyase C is stable in the pH range of 5.0–7.0. Among the metal ions tested, additions of Na+, K+, and Mg2+ ions can enhance the enzyme activities while Fe2+, Fe3+, Ba2+, and Zn2+ ions show inhibitory effects. The substrate specificity results demonstrate that alginate lyase C has the specificity for G block while alginate lyases A and B have the activities for both M and G blocks. It is the first report about extracellular alginate lyases with high alginate-degrading activity from P. fluorescens.
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影响因子：
2.8
作者：
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通讯作者：
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