Immobilization of glycerol dehydrogenase on magnetic silica nanoparticles for conversion of glycerol to value-added 1,3-dihydroxyacetone
文献类型：期刊论文
| 作者 | Zheng, Muqing1,2; Zhang, Songping1 |
| 刊名 | BIOCATALYSIS AND BIOTRANSFORMATION
 |
| 出版日期 | 2011-12-01 |
| 卷号 | 29期号:6页码:278-287 |
| 关键词 | Glycerol dehydrogenase superparamagnetic nanoparticles enzyme immobilization 1 3-dihydoxyacetone |
| ISSN号 | 1024-2422 |
| 其他题名 | Biocatal. Biotransform. |
| 中文摘要 | Glycerol dehydrogenase (GlyDH) which oxidizes glycerol to the value-added chemical, 1,3-dihydroxyacetone, is of interest due to the oversupply of glycerol as a by-product of the biodiesel industry. To exploit the enzymatic oxidation of glycerol industrially, silica coated magnetic Fe(3)O(4) nanoparticles were prepared and then activated with an amino-silane reagent for covalent immobilization of GlyDH via a glutaraldehyde linkage. At the optimal glutaraldehyde concentration of 0.05% (v/v), an enzyme loading of up to 57.5 mg/g-nanoparticles was achieved with 81.1% of the original activity retained. Reaction kinetic analysis indicated that the immobilized GlyDH had almost the same Michaelis-Menten constants for both NAD(+) and glycerol as the free GlyDH did. However, after immobilization the turnover number k(cat) of the GlyDH decreased from 164 s(-1) to 113 s(-1), and the reaction was 1.3-fold less sensitive to inhibition by DHA, which could compensate the decrease in k(cat). The immobilized GlyDH was also less sensitive to changes in pH and temperature, and showed a 5.3-fold improvement in thermal stability at 50 degrees C. Furthermore, excellent reusability was observed such that 10 cycles of re-use only led to 9% loss of enzyme activity. |
| 英文摘要 | Glycerol dehydrogenase (GlyDH) which oxidizes glycerol to the value-added chemical, 1,3-dihydroxyacetone, is of interest due to the oversupply of glycerol as a by-product of the biodiesel industry. To exploit the enzymatic oxidation of glycerol industrially, silica coated magnetic Fe(3)O(4) nanoparticles were prepared and then activated with an amino-silane reagent for covalent immobilization of GlyDH via a glutaraldehyde linkage. At the optimal glutaraldehyde concentration of 0.05% (v/v), an enzyme loading of up to 57.5 mg/g-nanoparticles was achieved with 81.1% of the original activity retained. Reaction kinetic analysis indicated that the immobilized GlyDH had almost the same Michaelis-Menten constants for both NAD(+) and glycerol as the free GlyDH did. However, after immobilization the turnover number k(cat) of the GlyDH decreased from 164 s(-1) to 113 s(-1), and the reaction was 1.3-fold less sensitive to inhibition by DHA, which could compensate the decrease in k(cat). The immobilized GlyDH was also less sensitive to changes in pH and temperature, and showed a 5.3-fold improvement in thermal stability at 50 degrees C. Furthermore, excellent reusability was observed such that 10 cycles of re-use only led to 9% loss of enzyme activity. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
| 关键词[WOS] | FED-BATCH PROCESS ; GLUCONOBACTER-OXYDANS ; ALCOHOL-DEHYDROGENASE ; COMMODITY CHEMICALS ; MICROBIAL SYNTHESIS ; DIHYDROXYACETONE ; OPTIMIZATION ; PURIFICATION ; STABILITY ; LIPASE |
| 收录类别 | SCI |
| 原文出处 | |
| 语种 | 英语 |
| WOS记录号 | WOS:000297345400007 |
| 公开日期 | 2013-11-28 |
| 版本 | 出版稿 |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/6371]  |
| 专题 | 过程工程研究所_研究所（批量导入） |
| 作者单位 | 1.Chinese Acad Sci, Natl Key Lab Biochem Engn, Inst Proc Engn, Beijing 100190, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zheng, Muqing,Zhang, Songping. Immobilization of glycerol dehydrogenase on magnetic silica nanoparticles for conversion of glycerol to value-added 1,3-dihydroxyacetone[J]. BIOCATALYSIS AND BIOTRANSFORMATION,2011,29(6):278-287. |
| APA | Zheng, Muqing,&Zhang, Songping.(2011).Immobilization of glycerol dehydrogenase on magnetic silica nanoparticles for conversion of glycerol to value-added 1,3-dihydroxyacetone.BIOCATALYSIS AND BIOTRANSFORMATION,29(6),278-287. |
| MLA | Zheng, Muqing,et al."Immobilization of glycerol dehydrogenase on magnetic silica nanoparticles for conversion of glycerol to value-added 1,3-dihydroxyacetone".BIOCATALYSIS AND BIOTRANSFORMATION 29.6(2011):278-287. |
入库方式： OAI收割
来源：过程工程研究所
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