微生物结冷胶裂解酶的纯化与表征
Purification and characterization of microbial gellan lyase.
作者信息
Hashimoto W, Inose T, Nakajima H, Sato N, Kimura S, Murata K
机构信息
Central Research Institute, Maruha Co., Tsukuba City, Japan.
出版信息
Appl Environ Microbiol. 1996 Apr;62(4):1475-7. doi: 10.1128/aem.62.4.1475-1477.1996.
Abstract
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.
摘要
结冷胶裂解酶是从在以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得到的。该酶是一种分子量为140 kDa的单体，在pH 7.5和45℃时活性最高。该酶对结冷胶具有高度特异性，并能降低聚合物的粘度。
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