Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Technology & Business University (BTBU), Beijing 100048, China; Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University (BTBU), Beijing 100048, China.
College of Food Science and Technology, Agricultural University of Hebei, Baoding 071000, China.
Food Chem. 2017 Jan 1;214:39-46. doi: 10.1016/j.foodchem.2016.06.108. Epub 2016 Jun 30.
An intracellular naringinase from Bacillus amyloliquefaciens 11568 isolated from soil was purified, identified, and characterized. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the purified enzyme gave a single protein band corresponding to a molecular mass of 32kDa. The optimum pH and temperature for naringinase and its α-l-rhamnosidase and β-d-glucosidase activities were pH 7.5 and 45°C, respectively. The enzymes were stable below 45°C between pH 3.5 and 8.5. The Km and the Vmax of the isolated naringinase were 0.95mmol/L and 3847.3mmol/(L·min), respectively. The isolated naringinase was capable of hydrolyzing naringin, neohesperidin, and other glycosides. Additionally, a concentration of 4U/mL of the enzyme in citrus juice was sufficient to remove the naringin and alleviate the bitterness of the juice. These results provide an in-depth insight into the structure of the naringinase and the hydrolysis of naringin and other flavonoids.
从土壤中分离到的解纤维果胶杆菌 11568 产生的一种细胞内柚皮苷酶被纯化、鉴定和表征。纯化酶的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）分析显示，单一蛋白条带对应 32kDa 的分子质量。柚皮苷酶及其 α-l-鼠李糖苷酶和 β-d-葡萄糖苷酶活性的最适 pH 和温度分别为 pH7.5 和 45°C。在 3.5-8.5pH 值和 45°C 以下，酶是稳定的。分离的柚皮苷酶的 Km 和 Vmax 分别为 0.95mmol/L 和 3847.3mmol/（L·min）。分离的柚皮苷酶能够水解柚皮苷、新橙皮苷和其他糖苷。此外，在橙汁中添加 4U/mL 的酶足以去除柚皮苷并减轻果汁的苦味。这些结果深入了解了柚皮苷酶的结构以及柚皮苷和其他类黄酮的水解。
