Purification and characterization of a novel thermostable phytase from the thermophilic Geobacillus sp TF16
Purification and characterization of a novel thermostable phytase from the thermophilic Geobacillus sp TF16
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DOI：
10.1080/10942912.2016.1203930
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发表时间：
2017-01-01
影响因子：
2.9
通讯作者：
Ertunga, Nagihan Saglam
中科院分区：
文献类型：
--
作者：
Dokuzparmak, Emre;Sirin, Yakup;Ertunga, Nagihan Saglam
采用硫酸铵沉淀和离子交换色谱法纯化了一种新的嗜热性Geobacillus sp. TF16植酸酶，并在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上检测到其单带106.04 kDa。最佳温度为85℃，最佳pH为4.0℃。该酶具有较高的耐热性，其V-max和K-m值分别为526.28 U/mg和1.31 mM。该酶具有广泛的底物选择性和对蛋白酶的抗性，并能有效水解豆浆植酸盐。这些结果表明，本研究提供了一种具有增强性能的替代植酸酶。
A novel phytase from thermophilic Geobacillus sp. TF16 was purified approximately 5-fold using ammonium sulfate precipitation and ion exchange chromatography, and determined as a single band 106.04 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Optimum temperature and optimum pH were found to be 85 degrees C and 4.0, respectively. The enzyme is highly thermostable and V-max and K-m values were calculated as 526.28 U/mg and 1.31 mM, respectively. It was also found that the enzyme exhibited a broad substrate selectivity and resistance toward proteases and effectively hydrolyzed soymilk phytate. These results suggest that this study provides an alternative phytase enzyme with enhanced properties.