从一株新分离的链格孢菌（Alternaria alternata SK37.001）中纯化和鉴定一种细胞内的α-l-鼠李糖苷酶。
Purification and characterization of an intracellular α-l-rhamnosidase from a newly isolated strain, Alternaria alternata SK37.001.
机构信息
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China; International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu 214122, China.
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China.
出版信息
Food Chem. 2018 Dec 15;269:63-69. doi: 10.1016/j.foodchem.2018.06.134. Epub 2018 Jun 28.
A strain, Alternaria alternata SK37.001, which produces an intracellular α-l-rhamnosidase, was newly isolated from citrus orchard soil. The molecular mass of the enzyme was 66 kDa, as evaluated by SDS-PAGE and 135 kDa, as determined by gel filtration, which indicated that the enzyme is a dimer. The enzyme had a specific activity of 21.7 U mg after step-by-step purification. The optimal pH and temperature were 5.5 and 60 °C, respectively. The enzyme was relatively stable at a pH of 4.0-8.0 and a temperature between 30 and 50 °C compared with other pH levels and temperatures investigated. The enzyme activity was accelerated by Ba and Al but inhibited by Ni, Cu and Co, especially Ni. The kinetic parameters of K and V were 4.84 mM and 53.1 μmol mg min, respectively. The α-l-rhamnosidase could hydrolyze quercitrin, naringin and neohesperidin, hesperidin and rutin rhamnose-containing glycosides but could not hydrolyze ginsenoside Rg2 or saiko-saponin C.
一株产细胞内 α-l-鼠李糖苷酶的链格孢菌（Alternaria alternata SK37.001），从柑橘园土壤中被新分离出来。该酶的相对分子质量经 SDS-PAGE 分析为 66 kDa，经凝胶过滤层析测定为 135 kDa，表明该酶是一个二聚体。经分步纯化后，该酶的比活力为 21.7 U/mg。最适 pH 值和温度分别为 5.5 和 60°C。与其他研究的 pH 值和温度相比，该酶在 pH 值为 4.0-8.0 和温度在 30-50°C 之间时相对稳定。Ba 和 Al 可加速酶活性，而 Ni、Cu 和 Co 则抑制酶活性，尤其是 Ni。该酶的动力学参数 K 和 V 分别为 4.84 mM 和 53.1 μmol/mg/min。该 α-l-鼠李糖苷酶能水解槲皮苷、柚皮苷和新橙皮苷、橙皮苷和芦丁鼠李糖苷，但不能水解人参皂苷 Rg2 或柴胡皂甙 C。
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