| A new study of cell disruption to release recombinant thermostable enzyme from Escherichia coli by thermolysis. | |
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MedLine Citation:
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PMID: 17399834 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Extraction of intracellular protein from Escherichia coli is traditionally achieved by mechanical, chemical or enzymatic disruption technology. In this study, a novel thermolysis method was used to disrupt E. coli cells to release a recombinant thermostable esterase. We found that heat treatment of E. coli was highly effective to destroy the integrity of bacterial cell walls and release the recombinant hyperthermophilic esterase at temperatures above 60 degrees C. The effects of temperature, pH and cell concentration on the efficiency of cell disruption were examined. The most effective temperature for cell disruption was at 80 degrees C. The pH and cell concentration had only minor effect on the release of the hyperthermophilic esterase. In addition, we found that the hyperthermophilic esterase could be purified at the early stage of the thermolysis, which is a major advantage of the thermolysis method. Finally, a comparison between thermolysis and traditional methods for the disruption of cells and the release of the thermostable enzyme was made. |
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Authors:
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Xiaodong Ren; Dawei Yu; Lei Yu; Gui Gao; Siping Han; Yan Feng |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2007-02-25 |
Journal Detail:
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Title: Journal of biotechnology Volume: 129 ISSN: 0168-1656 ISO Abbreviation: J. Biotechnol. Publication Date: 2007 May |
Date Detail:
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Created Date: 2007-04-23 Completed Date: 2007-09-26 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 8411927 Medline TA: J Biotechnol Country: Netherlands |
Other Details:
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Languages: eng Pagination: 668-73 Citation Subset: IM |
Affiliation:
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Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun, PR China. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cell Membrane Permeability Enzyme Stability Escherichia coli / enzymology* Esterases / genetics, isolation & purification*, metabolism* Hot Temperature Plasmids Recombinant Proteins / isolation & purification, metabolism Thermodynamics Ultrasonics |
| Chemical | |
Reg. No./Substance:
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0/Recombinant Proteins; EC 3.1.-/Esterases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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