pH-dependent stability of EGX, a multi-functional cellulase from mollusca, Ampullaria crossean
文献类型：期刊论文
| 作者 | Li, WY; Wang, J; Li, YH; Ding, M; Xu, GJ; Liu, LY; Zhao, FK |
| 刊名 | ACTA BIOCHIMICA ET BIOPHYSICA SINICA
 |
| 出版日期 | 2004 |
| 卷号 | 36期号:9页码:603-608 |
| 关键词 | multi-functional cellulase stability Ampullaria crossean fluorescence spectroscopy pH-dependent structural change CD spectrum |
| 通讯作者 | Zhao, FK (reprint author), Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol,Key Lab Proteom, Shanghai 200031, Peoples R China.,fkzhao@sibs.ac.cn |
| 英文摘要 | The cellulase activity and stability of EGX, a multi-functional cellulase previously purified from the mollusca Ampullaria crossean, was systematically studied under different pH. The pH induced conformation and stability change of EGX have been investigated by using the intrinsic fluorescence, ANS fluorescence and CD spectrum. It has been found that the conformation and activity of this cellulase were strongly dependent on the pH. EGX was stable for both the enzyme activity and the conformation from pH 5.6 to pH 7.4. As shown by intrinsic and ANS fluorescence, no red shift of emission maximum occurred and a negligible intensity change was observed at pH 5.6-7.4. The activity of EGX remained about 80% in pH 5.6-7.4 and obviously decreased out of side the pH range. Urea-induced changes in EGX at pH 5.4 and pH 8.0 were measured by intrinsic fluorescence and CD spectrum. At pH 5.4, a significantly red shift of emission maximum occurred when the concentration of urea was 5 M compared to the concentration was 3 M at pH 8.0. The (x-helix at pH 5.4 was 40.51% in the absence of urea and 31.04% in the presence of 4 M urea. At pH 8.0 the (x-helix was 7.23% in the presence of 4 M urea. The data indicated that EGX was much susceptible to urea-induced unfolding at pH 8.0 and much stable at pH 5.4. The greater pH dependent stability of EGX may allow the enzyme to adequately catalyze the hydrolysis of cellulosic materials under natural or industrial extreme conditions. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | OPTICAL-ROTATORY DISPERSION ; CIRCULAR-DICHROISM ; FLUORESCENCE-SPECTRUM ; BETA-LACTOGLOBULIN ; PROTEIN ; CONFORMATION ; TRYPTOPHAN ; RESIDUES ; XYLANASE ; SITE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000223987100004 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2126]  |
| 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 | Li, WY,Wang, J,Li, YH,et al. pH-dependent stability of EGX, a multi-functional cellulase from mollusca, Ampullaria crossean[J]. ACTA BIOCHIMICA ET BIOPHYSICA SINICA,2004,36(9):603-608. |
| APA | Li, WY.,Wang, J.,Li, YH.,Ding, M.,Xu, GJ.,...&Zhao, FK.(2004).pH-dependent stability of EGX, a multi-functional cellulase from mollusca, Ampullaria crossean.ACTA BIOCHIMICA ET BIOPHYSICA SINICA,36(9),603-608. |
| MLA | Li, WY,et al."pH-dependent stability of EGX, a multi-functional cellulase from mollusca, Ampullaria crossean".ACTA BIOCHIMICA ET BIOPHYSICA SINICA 36.9(2004):603-608. |
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