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The differential stability of the left and right domains of papain

Sathish, H. A. and Kumar, Parigi Ramesh and Prakash, V. (2009) The differential stability of the left and right domains of papain. Process Biochemistry, 44 (7). pp. 710-716. ISSN 1359-5113

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We have investigated the differential stability of the two domains of papain, a broad specific cysteine protease, which is one of the most commonly used enzyme in various industries. The denaturant induced equilibrium unfolding of this enzyme has been investigated by different spectroscopic techniques. By site specific fluorescent labeling of one of the domain, we observed that during the unfolding process, L domain unfolds first and the R domain unfolds at a later stage. Spectroscopic studies reveal a biphasic unfolding transition, suggesting the presence of an intermediate during the unfolding process. The intermediate is observed between 1.5 and 2.5M GuHCl and between 3 and 5M in the case of urea induced unfolding. The unfolding process for both native to intermediate and intermediate to unfolded species is reversible in the case of urea unfolding, with a [Delta]G of -2.4 and -5.5kcal/mole respectively where as for GuHCl unfolding only native to intermediate species is reversible indicating the predominance of hydrophobic interactions in the stability of the molecule.

Item Type: Article
Uncontrolled Keywords: Denaturants Domains Papain Protein stability Unfolding
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
600 Technology > 08 Food technology > 24 Fruits
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 17 Jun 2009 11:35
Last Modified: 17 Oct 2018 09:15
URI: http://ir.cftri.com/id/eprint/9069

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