A monovalent anion affected multi-functional cellulase EGX from the mollusca, Ampullaria crossean
文献类型：期刊论文
| 作者 | Wang, J; Ding, M; Li, YH; Chen, QX; Xu, GJ; Zhao, FK |
| 刊名 | PROTEIN EXPRESSION AND PURIFICATION
 |
| 出版日期 | 2003 |
| 卷号 | 31期号:1页码:108-114 |
| 关键词 | Ampullaria crossean cellulase EGX endo-beta-1 exo-beta-1 endo-beta-1 chloride regulation monovalent anion 4-xylanase 4-glucanase 4-glucanase |
| 通讯作者 | Zhao, FK (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Key Lab Proteom, 320 Yue Yang Rd, Shanghai 200031, Peoples R China., |
| 英文摘要 | A cellulose hydrolytic enzyme was isolated from the stomach juice of Ampullaria crossean, a kind of herbivorous mollusca. The enzyme was purified 45.3-fold to homogenety by ammonium sulfate precipitation, DEAE-Sephadex A-50 column, Bio-gel P-100 gel filtration column, and-phenyl-Sepharose CL-4B column chromatography. The enzyme was designated as cellulase EGX The purified enzyme is a multi-functional enzyme with the activities of exo-beta-1,4-glucanase (14.84 U/mg for p-nitrophenyl beta-D-cellobioside), endo-beta-1,4-glucanase (40.3 U/mg for carboxymethyl cellulose), and endo-beta-1,4-xylanase (196 U/mg for soluble xylan from birch-wood). The monovalent anions such as F-, Cl-, Br-, I-, and NO3- are essential for its exo-beta-1,4-glucanase activity but have no effect on the activity for xylan, while I- higher than 5 mM would inhibit the exo-beta-1,4-glucanase activity. The monovalent anions Cl- and Br- activate its endo-beta-1,4-glucanase activity. Binding of Cl- enhances the thermostability of EGX, but does not affect its fluorescence emission spectrum. The molecular mass of EGX is 41.5 kDa, as determined by SDS-PAGE. The pI value is about pH 7.35. The xylan hydrolytic activity of EGX reaches to the maximum between pH 4.8 and 6.0 and the pNPC hydrolytic activity reaches the maximum between pH 4.8 and 5.6, while that for CMC hydrolytic activity is between pH 4.4 and 4.8. Preliminary results showed that the enzyme was secreted by the mollusca itself. (C) 2003 Elsevier Science (USA). All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology |
| 类目[WOS] | Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 关键词[WOS] | ALPHA-AMYLASE ; DEGRADATION ; SEQUENCE ; CHLORIDE ; TERMITE ; GENE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000185553900013 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2217]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Wang, J,Ding, M,Li, YH,et al. A monovalent anion affected multi-functional cellulase EGX from the mollusca, Ampullaria crossean[J]. PROTEIN EXPRESSION AND PURIFICATION,2003,31(1):108-114. |
| APA | Wang, J,Ding, M,Li, YH,Chen, QX,Xu, GJ,&Zhao, FK.(2003).A monovalent anion affected multi-functional cellulase EGX from the mollusca, Ampullaria crossean.PROTEIN EXPRESSION AND PURIFICATION,31(1),108-114. |
| MLA | Wang, J,et al."A monovalent anion affected multi-functional cellulase EGX from the mollusca, Ampullaria crossean".PROTEIN EXPRESSION AND PURIFICATION 31.1(2003):108-114. |
入库方式： OAI收割
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。