Purification and characterization of a naringinase from a newly isolated strain of Bacillus amyloliquefaciens 11568 suitable for the transformation of flavonoids

卷:214

Zhu, Yunping ; Jia, Huiyong ; Xi, Menglu ; Xu, Liya ; Wu, Shaoming ; Li, Xiuting

Beijing Technol & Business Univ

关键词: Naringinase;    Bacillus amyloliquefaciens;    Debittering;    Naringin;    Purification;   

DOI  :  10.1016/j.foodchem.2016.06.108

学科分类：食品科学和技术

【 摘 要 】

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 32 kDa. The optimum pH and temperature for naringinase and its alpha-L-rhamnosidase and beta-D-glucosidase activities were pH 7.5 and 45 degrees C, respectively. The enzymes were stable below 45 degrees C between pH 3.5 and 8.5. The K-m and the V-max of the isolated naringinase were 0.95 mmol/L and 3847.3 mmol/(L.min), respectively. The isolated naringinase was capable of hydrolyzing naringin, neohesperidin, and other glycosides. Additionally, a concentration of 4 U/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. (C) 2016 Elsevier Ltd. All rights reserved.