Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 156, Issue -, Pages 271-279Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2020.04.033
Keywords
Surface active ionic liquids; Micellization; Lysozyme; Protein stability; Enzyme activity
Funding
- Department of Science and Technology [09/25(0039)/2011-EMR-1]
- [SR/S1/PC-11/2009]
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The present study was designed to explore the hydrophobicity and concentration dependence of imidazolium based surface active ionic liquids (SAILs) effects on the structural-functional integrity of proteins. Specifically, we investigated the impact of SAILs viz. 1-octyl-3-methylimidazolium dodecylbenzenesulfonate ([DDMIM][DBS]) and 1-dodecyl-3-methylimidazolium dodecylbenzenesulfonate ([DDMIM][DBS]) on activity, structure and stability of lysozyme. Activity measurements revealed that, in contrast to [DDMIM][DBS] that renders lysozyme either feebly active or inactive, [OMIM][DBS] significantly enhances the lysozyme activity in the concentration range of critical aggregation concentrations (CAC) to C-s (SAIL saturation concentration of protein backbone) i.e., 0.5 mM-1.35 mM. Tensiometric results in agreement with turbidity measurements inferred significant composition and concentration dependence of the lysozyme-SAIL interactions. Spectroscopic investigations revealed that compared to destabilizing behaviour of [DDMIM][DBS], [OMIM][DBS]significandy enhances both conformational as well as thermal stability of lysozyme in the CAC to C-s concentration regime. Altogether, results obtained do indicate that [OMIM][DBS], in the concentration regime of CAC to C-s, serves as art efficient stabiliser with an ability to appreciably enhance the activity, thermal stability and overall conformational stability of lysozyme. We firmly believe that [OMIM][DBS], at least in the CAC to C-s concentration ranges, can be exploited as a promising stabiliser and activity enhancer for numerous industrially important enzymes. (C) 2020 Elsevier B.V. All rights reserved.
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