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Purification and characterization of microbial gellan lyase.

机译:微生物吉兰糖裂解酶的纯化和表征。

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Gellan lyase was purified from the culture fluid of soil samples incubated in a medium containing gellan as a sole carbon source. The enzyme was a monomer with a molecular mass of 140 kDa and was most active at pH 7.5 and 45 degrees C. The enzyme was highly specific to gellan and lowered the viscosity of the polymer.
机译:从在含有结冷胶作为唯一碳源的培养基中培养的土壤样品的培养液中纯化结冷胶裂解酶。该酶是分子量为140 kDa的单体,在pH 7.5和45摄氏度下最具活性。该酶对结冷胶具有高度特异性,并降低了聚合物的粘度。

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