| 论文题目: | Structural and functional analysis of a low-temperature-active alkaline esterase from South China Sea marine sediment microbial metagenomic library |
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| 作者: | Hu Yongfei, Liu Yinghui, Li Jing, Feng Yanbin, Lu Na, Zhu Baoli*, and Xue Song*. |
| 联系作者: | Zhu, Baoli* Xue, Song* |
| 刊物名称: | J Ind Microbiol Biotechnol |
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| 年份: | 2015 |
| 影响因子: | 2.78 |
| 论文下载: | 下载地址 |
| 摘要: | A low-temperature-active alkaline esterase, Est12, from a marine sediment metagenomic fosmid library was identified. Est12 prefers short- and middle-chain p-nitrophenol esters as substrate with optimum temperature and pH value of 50 degrees C and 9.0, respectively, and nearly 50 % of maximum activity retained at 5 degrees C. The hydrolysis activity of Est12 was stable at 40 degrees C. Ca2+ especially activated the activity of Est12 to about 151 % of the control. DEPC and PMSF inhibited the activity of Est12 to 34 and 25 %, respectively. In addition, Est12 was more tolerable to methanol compared to other organic solvents tested. The crystal structure of Est12 at 1.39 A resolution showed that the cap domain which is composed of an alpha-helix and a flexible region resulted in a relatively wide spectrum of substrate, with p-nitrophenol caproate as the preferred one. Furthermore, the flexible cap domain and the high percentage of Gly, Ser, and Met may play important roles in the adaptation of Est12 to low temperature. |
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