Document Detail


Bioconversion of D: -glucose into D: -glucosone by Glucose 2-oxidase from Coriolus versicolor at Moderate Pressures.
MedLine Citation:
PMID:  20872184     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Glucose 2-oxidase (pyranose oxidase, pyranose:oxygen-2-oxidoreductase, EC 1.1.3.10) from Coriolus versicolor catalyses the oxidation of D: -glucose at carbon 2 in the presence of molecular O(2) producing D: -glucosone (2-keto-glucose and D: -arabino-2-hexosulose) and H(2)O(2). It was used to convert D: -glucose into D: -glucosone at moderate pressures (i.e. up to 150 bar) with compressed air in a modified commercial batch reactor. Several parameters affecting biocatalysis at moderate pressures were investigated as follows: pressure, [enzyme], [glucose], pH, temperature, nature of fluid and the presence of catalase. Glucose 2-oxidase was purified by immobilized metal affinity chromatography on epoxy-activated Sepharose 6B-IDA-Cu(II) column at pH 6.0. The rate of bioconversion of D: -glucose increased with the pressure since an increase in the pressure with compressed air resulted in higher rates of conversion. On the other hand, the presence of catalase increased the rate of reaction which strongly suggests that H(2)O(2) acted as inhibitor for this reaction. The rate of bioconversion of D: -glucose by glucose 2-oxidase in the presence of either nitrogen or supercritical CO(2) at 110 bar was very low compared with the use of compressed air at the same pressure. The optimum temperature (55°C) and pH (5.0) of D: -glucose bioconversion as well as kinetic parameters for this enzyme were determined under moderate pressure. The activation energy (E (a)) was 32.08 kJ mol(-1) and kinetic parameters (V (max), K (m), K (cat) and K (cat)/K (m)) for this bioconversion were 8.8 U mg(-1) protein, 2.95 mM, 30.81 s(-1) and 10,444.06 s(-1) M(-1), respectively. The biomass of C. versicolor as well as the cell-free extract containing glucose 2-oxidase activity were also useful for bioconversion of D: -glucose at moderate pressures. The enzyme was apparently stable at moderate pressures since such pressures did not affect significantly the enzyme activity.
Authors:
Amin Karmali; José Coelho
Related Documents :
19416064 - Advances in high-pressure biophysics: status and prospects of macromolecular crystallog...
20649444 - The effect of argon gas pressure on ice ball size and rate of formation.
8771204 - Pressure-induced perturbation of ans-apomyoglobin complex: frequency domain fluorescenc...
1592164 - Methodology for in-process determination of residual water in freeze-dried products.
19416064 - Advances in high-pressure biophysics: status and prospects of macromolecular crystallog...
9264494 - Comparative effects of enalapril and verapamil on myocardial blood flow in systemic hyp...
Publication Detail:
Type:  Journal Article     Date:  2010-09-25
Journal Detail:
Title:  Applied biochemistry and biotechnology     Volume:  163     ISSN:  1559-0291     ISO Abbreviation:  Appl. Biochem. Biotechnol.     Publication Date:  2011 Apr 
Date Detail:
Created Date:  2011-03-03     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8208561     Medline TA:  Appl Biochem Biotechnol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  906-17     Citation Subset:  IM    
Affiliation:
Chemical Engineering and Biotechnology Research Center and Department of Chemical Engineering of Instituto Superior de Engenharia de Lisboa, Rua Conselheiro Emídio Navarro, 1959-007, Lisbon, Portugal, akarmali@deq.isel.ipl.pt.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Stable suppression of gene expression by short interfering RNAs targeted to promoter in a mouse embr...
Next Document:  Cloning and Expression of Che a 1, the Major Allergen of Chenopodium album in Escherichia coli.