Reversible immobilization of glucoamylase by metal affinity adsorption on magnetic chelator particles
文献类型：期刊论文
| 作者 | Wang, Feng; Guo, Chen; Liu, Hui-Zhou; Liu, Chun-Zhao |
| 刊名 | JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
 |
| 出版日期 | 2007-09-03 |
| 卷号 | 48期号:1-2页码:1-7 |
| 关键词 | glucoamylase immobilization magnetic particles metal chelating |
| ISSN号 | 1381-1177 |
| 其他题名 | J. Mol. Catal. B-Enzym. |
| 中文摘要 | Magnetic Cu2+-chelated particles, prepared by cerium initiated graft polymerization of tentacle-type polymer chains with iminodiacetic acid (IDA) as chelating ligand, were employed for glucoamylase immobilization. The particles had an obvious high adsorption capacity of glucoamylase with a great activity recovery of 84.0% after immobilization. The immobilized glucoamylase exhibited improved stability in reaction conditions over a wide pH region (pH 3.5-6.0) and a broad temperature range (45-75 degrees C). The value of the Michaelis constant (K-m) of the immobilized glucoamylase (1.77 mg/ml) was higher than that of the free one (1.07 mg/ml), whereas the maximum velocity (V-max) was lower for the adsorbed glucoamylase. Storage stability and temperature endurance of the immobilized glucoamylase were found to increase greatly, and the immobilized glucoamylase retained 75.7% of its initial activity after 30 successive batch reactions. The magnetic Cu2+-chelated particles also exhibited excellent reusability, indicating the advantage of the magnetic metal-chelated particles in biocatalytic applications. (c) 2007 Elsevier B.V. All rights reserved. |
| 英文摘要 | Magnetic Cu2+-chelated particles, prepared by cerium initiated graft polymerization of tentacle-type polymer chains with iminodiacetic acid (IDA) as chelating ligand, were employed for glucoamylase immobilization. The particles had an obvious high adsorption capacity of glucoamylase with a great activity recovery of 84.0% after immobilization. The immobilized glucoamylase exhibited improved stability in reaction conditions over a wide pH region (pH 3.5-6.0) and a broad temperature range (45-75 degrees C). The value of the Michaelis constant (K-m) of the immobilized glucoamylase (1.77 mg/ml) was higher than that of the free one (1.07 mg/ml), whereas the maximum velocity (V-max) was lower for the adsorbed glucoamylase. Storage stability and temperature endurance of the immobilized glucoamylase were found to increase greatly, and the immobilized glucoamylase retained 75.7% of its initial activity after 30 successive batch reactions. The magnetic Cu2+-chelated particles also exhibited excellent reusability, indicating the advantage of the magnetic metal-chelated particles in biocatalytic applications. (c) 2007 Elsevier B.V. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences |
| 类目[WOS] | Biochemistry & Molecular Biology ; Chemistry, Physical |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Chemistry |
| 关键词[WOS] | GLUCOSE-OXIDASE ; POLY(STYRENE) PARTICLES ; ENZYME IMMOBILIZATION ; STARCH HYDROLYSIS ; BEADS ; POLYETHYLENEIMINE ; POLYMER ; CHROMATOGRAPHY ; MICROSPHERES ; PURIFICATION |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000249091200001 |
| 公开日期 | 2013-10-15 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/3452]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 1.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100080, Peoples R China 2.Chinese Acad Sci, Inst Proc Engn, Lab Separat Sci & Engn, Beijing 100080, Peoples R China 3.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wang, Feng,Guo, Chen,Liu, Hui-Zhou,et al. Reversible immobilization of glucoamylase by metal affinity adsorption on magnetic chelator particles[J]. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,2007,48(1-2):1-7. |
| APA | Wang, Feng,Guo, Chen,Liu, Hui-Zhou,&Liu, Chun-Zhao.(2007).Reversible immobilization of glucoamylase by metal affinity adsorption on magnetic chelator particles.JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC,48(1-2),1-7. |
| MLA | Wang, Feng,et al."Reversible immobilization of glucoamylase by metal affinity adsorption on magnetic chelator particles".JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC 48.1-2(2007):1-7. |
入库方式： OAI收割
来源：过程工程研究所
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