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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Purification and Characterization of a Naringinase from Aspergillus aculeatus JMUdb058
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Purification and Characterization of a Naringinase from Aspergillus aculeatus JMUdb058

机译：刺曲霉JMUdb058中柚皮苷酶的纯化和鉴定

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摘要

A naringinase from Aspergillus aculeatus JMUdb058 was purified, identified, and characterized. This naringinase had a molecular mass (MW) of 348 kDa and contained four subunits with MWs of 100, 95, 84, and 69 kDa. Mass spectrometry analysis revealed that the three larger subunits were β-D-glucosidases and that the smallest subunit was an a-L-rhamnosidase. The naringinase and its a-L-rhamnosidase and β-D-glucosidase subunits all had optimal activities at approximately pH 4 and 50 °C, and they were stable between pH 3 and 6 and below 50 °C. This naringinase was able to hydrolyze naringin, aesculin, and some other glycosides. The enzyme complex had a K_m value of 0.11 mM and a k_(cat)/K_m ratio of 14 034 s~(-1) mM~(-1) for total naringinase. Its a-L-rhamnosidase and β-D-glucosidase subunits had K_m values of 0.23 and 0.53 mM, respectively, and k_(cat)/K_m ratios of 14 146 and 7733 s~(-1) mM~(-1), respectively. These results provide in-depth insight into the structure of the naringinase complex and the hydrolyses of naringin and other glycosides.
机译：纯化，鉴定和鉴定了来自刺曲霉JMUdb058的柚皮苷酶。该柚皮苷酶的分子量（MW）为348 kDa，包含四个亚基，MWs为100、95、84和69 kDa。质谱分析表明，三个较大的亚基是β-D-葡糖苷酶，最小的亚基是α-L-鼠李糖苷酶。柚皮苷酶及其α-L-鼠李糖苷酶和β-D-葡萄糖苷酶亚基均在约pH 4和50°C时具有最佳活性，并且在pH 3和6以及低于50°C时稳定。该柚皮苷酶能够水解柚皮苷，七叶皂苷和一些其他糖苷。该酶复合物的总柚皮苷酶的K_m值为0.11 mM，k_（cat）/ K_m比为14034 s〜（-1）mM〜（-1）。其α-L-鼠李糖苷酶和β-D-葡糖苷酶亚基的K_m值分别为0.23和0.53 mM，k_（cat）/ K_m比分别为14 146和7733 s〜（-1）mM〜（-1）。这些结果提供了对柚皮苷酶复合物的结构以及柚皮苷和其他糖苷水解的深入了解。

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