Mechanism of stabilization of Bacillus circulans xylanase upon the introduction of disulfide bonds

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DOIResolve DOI: http://doi.org/10.1016/j.bpc.2006.10.006
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TypeArticle
Journal titleBiophysical Chemistry
Volume125
Issue2-3
Pages453461; # of pages: 9
Subjectdisulfides; drug effects; Endo-1,4-beta Xylanases; Enzyme Stability; enzymology; LED; MUTANT; PATHWAY; Protein Denaturation; stability; Temperature
AbstractThe introduction of disulfide bonds has been used as a strategy to enhance the stability of Bacillus circulans xylanase. The transition temperature of the S100C/N148C (DS1), V98C/A152C (DS2), and A1GC/G187,C188 (cXl) in comparison to the wild type was increased by 5.0, 4.1 and 3.8 °C, respectively. Interestingly, a combination of two disulfide bonds of DS1 and cXl (cDS1, circular disulfide 1) led to a 12 °C increase in the transition temperature. Importantly, an increase in the melting point and ΔΔG values of the cDS1 mutant was cooperative. These results suggest that the mechanism of stabilization by disulfide bonds under irreversible denaturation condition is achieved through: (1) a change in the rate-limiting step on the denaturation pathway; (2) destabilizing the unfolded state without affecting the relative rate constants on the denaturation pathway (like cXl mutant); and (3) or combination of the two (cDS1 mutant).
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberDAVOODI2007
DAVOODI2006
NPARC number9374331
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Record identifier4707bd2b-388b-4109-ba2a-323378059d4c
Record created2009-07-10
Record modified2016-05-09
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