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Are water-immiscibility and apolarity of the solvent relevant to enzyme efficiency?
MedLine Citation:
PMID:  18609564     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
The question of whether the solvent's water-immiscibility is relevant to enzymatic activity was addressed by assaying four different hydrolases (three lipases and one protease) in nine anhydrous solvents of similar hydrophobicities of which four were infinitely miscible with water and five were not. For no enzyme was a jump in activity observed upon a transition from water-miscible to water-immiscible solvent. The relevance of solvent apolarity to enzymatic efficiency was also examined. To this end, three groups of isomeric anhydrous solvents were selected where within each group of isomeric anhydrous solvents were selected where within each group one solvent was apolar (i.e., lacked a permanent dipole moment). For none of the four enzymes studied was activity significantly higher in apolar solvents than in their polar counterparts. Thus we conclude that often-cited solvent's immiscibility with water and apolarity by themselves are irrelevant to enzymatic activity. (c) 1993 John Wiley & Sons, Inc.
Authors:
V S Narayan; A M Klibanov
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biotechnology and bioengineering     Volume:  41     ISSN:  0006-3592     ISO Abbreviation:  Biotechnol. Bioeng.     Publication Date:  1993 Feb 
Date Detail:
Created Date:  2008-07-08     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7502021     Medline TA:  Biotechnol Bioeng     Country:  United States    
Other Details:
Languages:  eng     Pagination:  390-3     Citation Subset:  -    
Affiliation:
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139.
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