芽孢杆菌属GL1菌株的黄原胶裂解酶从黄原胶侧链释放出丙酮酸化甘露糖。
Xanthan lyase of Bacillus sp. strain GL1 liberates pyruvylated mannose from xanthan side chains.
作者信息
Hashimoto W, Miki H, Tsuchiya N, Nankai H, Murata K
机构信息
Research Institute for Food Science, Kyoto University, Uji, Kyoto 611-0011, Japan.
出版信息
Appl Environ Microbiol. 1998 Oct;64(10):3765-8. doi: 10.1128/AEM.64.10.3765-3768.1998.
Abstract
When the bacterium Bacillus sp. strain GL1 was grown in a medium containing xanthan as the carbon source, the viscosity of the medium decreased in association with growth, showing that the bacterium had xanthan-depolymerizing enzymes. One of the xanthan-depolymerizing enzymes (xanthan lyase) was present in the medium and was found to be induced by xanthan. The xanthan lyase purified from the culture fluid was a monomer with a molecular mass of 75 kDa, and was most active at pH 5.5 and 50 degrees C. The enzyme was highly specific for xanthan and produced pyruvylated mannose. The result indicates that the enzyme cleaved the linkage between the terminal pyruvylated mannosyl and glucuronyl residues in the side chain of xanthan.
摘要
当芽孢杆菌属菌株GL1在以黄原胶作为碳源的培养基中生长时，培养基的粘度随着生长而降低，这表明该细菌具有黄原胶解聚酶。其中一种黄原胶解聚酶（黄原胶裂解酶）存在于培养基中，并且发现它是由黄原胶诱导产生的。从培养液中纯化得到的黄原胶裂解酶是一种分子量为75 kDa的单体，在pH 5.5和50℃时活性最高。该酶对黄原胶具有高度特异性，并产生丙酮酸化甘露糖。结果表明，该酶切割了黄原胶侧链末端丙酮酸化甘露糖基和葡萄糖醛酸基之间的连接。
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