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Activity of Subtilisin Carlsberg in macromolecular crowding

Paper ID Volume ID Publish Year Pages File Format Full-Text
31028 44532 2007 8 PDF Available
Title
Activity of Subtilisin Carlsberg in macromolecular crowding
Abstract

Enzymatic activity of a proteolytic enzyme Subtilisin Carlsberg (SC) in anionic sodium dodecyl sulfate (SDS) micellar medium has been explored and found to be retarded compared to that in bulk buffer. Circular dichroism (CD) study reveals that SDS, which is a potential protein denaturant, has an insignificant denaturation effect on SC. The structural integrity of the protein offers an opportunity to study the functionality of the enzyme SC in a macromolecular crowding of micelles. Dynamic light scattering (DLS) data indicates no sandwich-like micelle–SC complex formation ruling out the possibility of interaction of the enzyme with the hydrophobic core of the micelle. However, steady state and time resolved emission studies on specific and nonspecific fluorescent probes indicate the proximity effect at the surface of the enzyme due to macromolecular crowding of the micelles. The agreement of retarded enzymatic activity in the micellar crowd with a theoretical model ascribed to the facts that substrates are compartmentalized in the micelles and enzyme interacts with the micelle through stern layer.

Keywords
Subtilisin Carlsberg; SDS micelle; Enzyme kinetics; Time resolved absorption; Circular dichroism; Picosecond resolved fluorescence anisotropy
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 86, Issue 3, 1 March 2007, Pages 199–206
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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