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Immobilization of glycerol dehydrogenase on magnetic silica nanoparticles for conversion of glycerol to value-added 1,3-dihydroxyacetone
Alternative TitleBiocatal. Biotransform.
Zheng, Muqing1,2; Zhang, Songping1
2011-12-01
Source PublicationBIOCATALYSIS AND BIOTRANSFORMATION
ISSN1024-2422
Volume29Issue:6Pages:278-287
AbstractGlycerol 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.; 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.
KeywordGlycerol Dehydrogenase Superparamagnetic Nanoparticles Enzyme Immobilization 1 3-dihydoxyacetone
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.3109/10242422.2011.631212
URL查看原文
Indexed BySCI
Language英语
WOS KeywordFED-BATCH PROCESS ; GLUCONOBACTER-OXYDANS ; ALCOHOL-DEHYDROGENASE ; COMMODITY CHEMICALS ; MICROBIAL SYNTHESIS ; DIHYDROXYACETONE ; OPTIMIZATION ; PURIFICATION ; STABILITY ; LIPASE
WOS Research AreaBiochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS SubjectBiochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS IDWOS:000297345400007
Citation statistics
Cited Times:17[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.ipe.ac.cn/handle/122111/6371
Collection研究所(批量导入)
Affiliation1.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
Recommended Citation
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.
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