Purification and characterization of an extracellular esterase with organic solvent tolerance from a halotolerant isolate, salimicrobiumsp. ly19
文献类型：期刊论文
| 作者 | Xin,Li; Hui-Ying,Yu |
| 刊名 | Bmc biotechnology
 |
| 出版日期 | 2013-12-10 |
| 卷号 | 13期号:1 |
| 关键词 | Halotolerant Esterase Purification Salimicrobium Organic solvent tolerance |
| ISSN号 | 1472-6750 |
| DOI | 10.1186/1472-6750-13-108 |
| 通讯作者 | Xin,li(lixin-eva@163.com) |
| 英文摘要 | Abstractbackgroundhalotolerant bacteria are excellent sources for selecting novel enzymes. being intrinsically stable and active under high salinities, enzymes from these prokaryotes have evolved to function optimally under extreme conditions, making them robust biocatalysts with potential applications in harsh industrial processes.resultsa halotolerant strain ly19 showing lipolytic activity was isolated from saline soil of yuncheng salt lake, china. it was identified as belonging to the genus of salimicrobium by 16s rrna gene sequence analysis. the extracellular enzyme was purified to homogeneity with molecular mass of 57?kda by sds-page. substrate specificity test revealed that the enzyme preferred short-chain p-nitrophenyl esters and exhibited maximum activity towards p-nitrophenyl butyrate (p-npb), indicating an esterase activity. the esterase was highly active and stable over broad temperature (20°c-70°c), ph (7.0-10.0) and nacl concentration (2.5%-25%) ranges, with an optimum at 50°c, ph?7.0 and 5% nacl. significant inhibition of the esterase was shown by ethylenediaminetetraacetic acid (edta), phenylmethylsulfonyl fluoride (pmsf) and phenylarsine oxide (pao), which indicated that it was a metalloenzyme with serine and cysteine residues essential for enzyme activity. moreover, the esterase displayed high activity and stability in the presence of hydrophobic organic solvents with log pow?≥?0.88 than in the absence of an organic solvent or in the presence of hydrophilic solvents.conclusionsresults from the present study indicated the novel extracellular esterase from salimicrobium sp. ly19 exhibited thermostable, alkali-stable, halotolerant and organic solvent-tolerant properties. these features led us to conclude that the esterase may have considerable potential for industrial applications in organic synthesis reactions. |
| 语种 | 英语 |
| WOS记录号 | BMC:10.1186/1472-6750-13-108 |
| 出版者 | BioMed Central |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2374320 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Xin,Li |
| 作者单位 | Yuncheng University; Life Science College |
| 推荐引用方式 GB/T 7714 | Xin,Li,Hui-Ying,Yu. Purification and characterization of an extracellular esterase with organic solvent tolerance from a halotolerant isolate, salimicrobiumsp. ly19[J]. Bmc biotechnology,2013,13(1). |
| APA | Xin,Li,&Hui-Ying,Yu.(2013).Purification and characterization of an extracellular esterase with organic solvent tolerance from a halotolerant isolate, salimicrobiumsp. ly19.Bmc biotechnology,13(1). |
| MLA | Xin,Li,et al."Purification and characterization of an extracellular esterase with organic solvent tolerance from a halotolerant isolate, salimicrobiumsp. ly19".Bmc biotechnology 13.1(2013). |
入库方式： iSwitch采集
来源：中国科学院大学
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。