• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>African Journal of Biotechnology >Purification and characterization of an extracellular esterase from a moderately halophilic bacterium, Halobacillus sp. strain LY5
【24h】

Purification and characterization of an extracellular esterase from a moderately halophilic bacterium, Halobacillus sp. strain LY5

机译：中等嗜盐细菌Halobacillus sp。的细胞外酯酶的纯化和鉴定。 LY5菌株

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

A newly moderate halophilic strain LY5 producing extracellular esterase was isolated and identified. Biochemical and physiological characterization, along with 16S rRNA gene sequence analysis placed the isolate in the genus?Halobacillus. Esterase production started from the mid-exponential phase of bacterial growth and reached a maximum level during the mid-stationary phase. The enzyme was highly active against?p-nitrophenyl esters with acyl chain lengths from C2 to C10, indicating an esterase activity. Enzyme purification was carried out by combination of 80% ammonium sulphate precipitation, diethylaminoethyl (DEAE)-cellulose ion exchange and Sephacryl S-100 gel filtration chromatography. The molecular weight of the esterase was determined to be 96 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The purified enzyme was highly active over broadranges of temperature (30 to 90°C), pH (6.0 to 12.0) and NaCl concentration (0 to 20%), showing optimal activity at 50°C, pH 10.0 and 10% NaCl. Complete inhibition of the esterase by phenylmethylsulfonyl fluoride (PMSF), phenylarsine oxide (PAO) and diethyl pyrocarbonate (DEPC) indicated that serine, cysteine and histidine residues were essential for its catalytic function. Moreover, it exhibited remarkable stability towards SDS and Triton X-100. Results from the present study indicate that the extracellular esterase from?Halobacillus?sp. LY5 may have considerable potential for industrial application from the perspectives of its properties.
机译：分离并鉴定了产生细胞外酯酶的新的中等嗜盐菌株LY5。生化和生理学表征以及16S rRNA基因序列分析将分离株置于嗜盐杆菌属中。酯酶的生产从细菌生长的指数中期开始，并在平稳中期达到最高水平。该酶对酰基链长度为C2至C10的β-硝基苯基酯具有很高的活性，表明其具有酯酶活性。酶纯化是通过80％硫酸铵沉淀，二乙氨基乙基（DEAE）-纤维素离子交换和Sephacryl S-100凝胶过滤色谱法进行的。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）确定酯酶的分子量为96kDa。纯化的酶在温度（30至90°C），pH（6.0至12.0）和NaCl浓度（0至20％）的宽范围内具有高活性，在50°C，pH 10.0和10％NaCl时显示最佳活性。苯甲基磺酰氟（PMSF），苯ar氧化物（PAO）和焦碳酸二乙酯（DEPC）对酯酶的完全抑制表明丝氨酸，半胱氨酸和组氨酸残基对其催化功能至关重要。此外，它对SDS和Triton X-100表现出显着的稳定性。本研究的结果表明，来自嗜盐菌的细胞外酯酶。从其性能的角度来看，LY5在工业上具有巨大的潜力。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号