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Purification and Properties of a Glucuronan Lyase from Sinorhizobium meliloti M5N1CS (NCIMB 40472)

机译:苜蓿中华根瘤菌M5N1CS中葡萄糖醛酸聚糖裂解酶的纯化和性质(NCIMB 40472)

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摘要

A glucuronan lyase extracted from Sinorhizobium meliloti strain M5N1CS was purified to homogeneity by anion-exchange chromatography. The purified enzyme corresponds to a monomer with a molecular mass of 20 kDa and a pI of 4.9. A specific activity was found only for polyglucuronates leading to the production of 4,5-unsaturated oligoglucuronates. The enzyme activity was optimal at pH 6.5 and 50°C. Zn2+, Cu2+, and Hg2+ (1 mM) inhibited the enzyme activity. No homology of the enzyme N-terminal amino acid sequence was found with any of the previously published protein sequences. This enzyme purified from S. meliloti strain M5N1CS corresponding to a new lyase was classified as an endopolyglucuronate lyase.
机译:通过阴离子交换色谱纯化从苜蓿中华根瘤菌菌株M5N1CS中提取的葡糖醛酸聚糖裂解酶。纯化的酶对应于分子量为20 kDa,pI为4.9的单体。仅发现聚葡萄糖醛酸的特定活性,导致产生4,5-不饱和的低聚葡萄糖醛酸。酶活性在pH 6.5和50°C时最佳。 Zn2 +,Cu2 +和Hg2 +(1 mM)抑制了酶的活性。没有发现酶N末端氨基酸序列与任何先前公开的蛋白质序列具有同源性。从S.meliloti菌株M5N1CS中纯化的对应于新裂解酶的酶被分类为内聚葡萄糖醛酸裂解酶。

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