Document Detail

A new study of cell disruption to release recombinant thermostable enzyme from Escherichia coli by thermolysis.
MedLine Citation:
PMID:  17399834     Owner:  NLM     Status:  MEDLINE    
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.
Xiaodong Ren; Dawei Yu; Lei Yu; Gui Gao; Siping Han; Yan Feng
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-02-25
Journal Detail:
Title:  Journal of biotechnology     Volume:  129     ISSN:  0168-1656     ISO Abbreviation:  J. Biotechnol.     Publication Date:  2007 May 
Date Detail:
Created Date:  2007-04-23     Completed Date:  2007-09-26     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  8411927     Medline TA:  J Biotechnol     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  668-73     Citation Subset:  IM    
Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun, PR China.
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MeSH Terms
Cell Membrane Permeability
Enzyme Stability
Escherichia coli / enzymology*
Esterases / genetics,  isolation & purification*,  metabolism*
Hot Temperature
Recombinant Proteins / isolation & purification,  metabolism
Reg. No./Substance:
0/Recombinant Proteins; EC 3.1.-/Esterases

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

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