Document Detail

Lipase in aqueous-polar organic solvents: activity, structure, and stability.
MedLine Citation:
PMID:  23625694     Owner:  NLM     Status:  MEDLINE    
Studying alterations in biophysical and biochemical behavior of enzymes in the presence of organic solvents and the underlying cause(s) has important implications in biotechnology. We investigated the effects of aqueous solutions of polar organic solvents on ester hydrolytic activity, structure and stability of a lipase. Relative activity of the lipase monotonically decreased with increasing concentration of acetone, acetonitrile, and DMF but increased at lower concentrations (upto ~20% v/v) of dimethylsulfoxide, isopropanol, and methanol. None of the organic solvents caused any appreciable structural change as evident from circular dichorism and NMR studies, thus do not support any significant role of enzyme denaturation in activity change. Change in 2D [15N, 1H]-HSQC chemical shifts suggested that all the organic solvents preferentially localize to a hydrophobic patch in the active-site vicinity and no chemical shift perturbation was observed for residues present in protein's core. This suggests that activity alteration might be directly linked to change in active site environment only. All organic solvents decreased the apparent binding of substrate to the enzyme (increased Km ); however significantly enhanced the kcat . Melting temperature (Tm ) of lipase, measured by circular dichroism and differential scanning calorimetry, altered in all solvents, albeit to a variable extent. Interestingly, although the effect of all organic solvents on various properties on lipase is qualitatively similar, our study suggest that magnitudes of effects do not appear to follow bulk solvent properties like polarity and the solvent effects are apparently dictated by specific and local interactions of solvent molecule(s) with the protein.
Md Zahid Kamal; Poornima Yedavalli; Mandar V Deshmukh; Nalam Madhusudhana Rao
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2013-05-25
Journal Detail:
Title:  Protein science : a publication of the Protein Society     Volume:  22     ISSN:  1469-896X     ISO Abbreviation:  Protein Sci.     Publication Date:  2013 Jul 
Date Detail:
Created Date:  2013-06-27     Completed Date:  2014-01-16     Revised Date:  2014-07-01    
Medline Journal Info:
Nlm Unique ID:  9211750     Medline TA:  Protein Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  904-15     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 The Protein Society.
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MeSH Terms
Acetone / chemistry*
Acetonitriles / chemistry
Alcohols / chemistry*
Binding Sites
Calorimetry, Differential Scanning
Circular Dichroism
Enzyme Stability
Lipase / chemistry*,  metabolism*
Nuclear Magnetic Resonance, Biomolecular
Solvents / chemistry
Reg. No./Substance:
0/Acetonitriles; 0/Alcohols; 0/Solvents; 1364PS73AF/Acetone; EC; Z072SB282N/acetonitrile

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