Purification, characterization and molecular cloning of a novel endo-beta-1,4-glucanase AC-EG65 from the mollusc Ampullaria crossean
文献类型：期刊论文
| 作者 | Li, YH; Yin, QY; Ding, M; Zhao, FK |
| 刊名 | COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
 |
| 出版日期 | 2009 |
| 卷号 | 153期号:2页码:149-156 |
| 关键词 | Ampullaria crossean Carbohydrate-binding module 2 Cellulase Endo-beta-1 4-Glucanase Endogenesis Glycosyl hydrolase family 9 Phylogeny |
| 通讯作者 | Zhao, FK (reprint author), Chinese Acad Sci, Grad Sch, Shanghai Inst Biol Sci, Key Lab Prote,Inst Biochem & Cell Biol, Shanghai 200031, Peoples R China.,fkzhao@sibs.ac.cn |
| 英文摘要 | A novel endo-beta-1,4-glucanase, AC-EG65, with a molecular mass of 65 kDa, was purified from the gastric juice of the mollusc, Ampullaria crossean, by ammonium sulfate fractionation, anion exchange, gel filtration, hydrophobic interaction and a second round of anion exchange chromatography. AC-EG65 showed specific carboxymethyl cellulose hydrolytic activity of 13.3 U/mg protein and the optimal pH and temperature of the activity were pH 5.5-6.5 and 50-55 degrees C, respectively. From the cDNA library of A. crossean stomach tissue, eight endo-beta-1,4-glucanase genes with high similarity were successfully cloned based on the partial amino acid sequences of AC-EG65 and were classified into 3 groups: eg65-a, eg65-b, and eg65-c. The open reading frames of the groups eg65-a, eg65-b, and eg65-c were 2142 bp, 2171 bp, and 2169 bp in length, encoding 713, 723 and 722 amino acids, respectively. The eight deduced proteins consisted of a family II carbohydrate-binding module (CBM2) and a glycosyl hydrolase family 9 (GHF9) catalytic domain. More than 98% amino acid identities were shared within the same group and more than 87% sequence identities among the groups. The endogenous origins of these EGase genes were supported by PCR amplification using ovary genomic DNA as template. (C) 2009 Elsevier Inc. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Zoology |
| 类目[WOS] | Biochemistry & Molecular Biology ; Zoology |
| 关键词[WOS] | COPTOTERMES-FORMOSANUS SHIRAKI ; CLOSTRIDIUM-THERMOCELLUM ; CELLULASE GENES ; CDNA CLONING ; ENDOGLUCANASE-D ; TERMITE ; ENDO-1,3-BETA-D-GLUCANASE ; DEGRADATION ; EXPRESSION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000269764800003 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1145]  |
| 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, YH,Yin, QY,Ding, M,et al. Purification, characterization and molecular cloning of a novel endo-beta-1,4-glucanase AC-EG65 from the mollusc Ampullaria crossean[J]. COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY,2009,153(2):149-156. |
| APA | Li, YH,Yin, QY,Ding, M,&Zhao, FK.(2009).Purification, characterization and molecular cloning of a novel endo-beta-1,4-glucanase AC-EG65 from the mollusc Ampullaria crossean.COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY,153(2),149-156. |
| MLA | Li, YH,et al."Purification, characterization and molecular cloning of a novel endo-beta-1,4-glucanase AC-EG65 from the mollusc Ampullaria crossean".COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY 153.2(2009):149-156. |
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