Document Detail

The identification and partial characterisation of a novel inducible extracellular thermostable esterase from the archaeon Sulfolobus shibatae.
MedLine Citation:
PMID:  7488139     Owner:  NLM     Status:  MEDLINE    
Extracellular esterases have so far only been reported in eubacteria, here we report the first identification and partial characterisation of a novel inducible extracellular esterase from the thermoacidophilic archaeon Sulfolobus shibatae. This esterase exhibits remarkable stability to both acid and heat. Esterase activity is induced by growth on a range of polyoxyethylenesorbitan (Tween) compounds as sole carbon source. Activity occurs over a wide temperature (25-99 degrees C) and pH (pH4.0-9.0) range and is optimal at 90 degrees C and pH6.0. It exhibits high thermal stability, with a half-life of 20 min at 120 degrees C, and shows a transient thermal activation of 60% at 90 degrees C. The thermal inactivation of function occurs by first order kinetics, and after 120 min incubation at 120 degrees C 50% of activity still remains. It is able to hydrolyse mono- and diglycerides, but is unable to hydrolyse the triglycerides olive oil and triolein, which is indicative of an esterase and not a lipase.
S Huddleston; C A Yallop; B M Charalambous
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  216     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1995 Nov 
Date Detail:
Created Date:  1995-12-21     Completed Date:  1995-12-21     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  495-500     Citation Subset:  IM    
Dept. of Biochemistry & Molecular Biology, Royal Free Hospital School of Medicine, University of London, United Kingdom.
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MeSH Terms
Enzyme Induction
Enzyme Stability
Esterases / biosynthesis,  chemistry*,  metabolism*
Hot Temperature
Hydrogen-Ion Concentration
Lipase / biosynthesis,  chemistry,  metabolism
Polysorbates / pharmacology
Sulfolobus / enzymology*
Time Factors
Reg. No./Substance:
0/Polysorbates; EC 3.1.-/Esterases; EC

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

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