Thermostabilization of the Bacillus circulans xylanase, by the introduction of disulfide bonds

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DOIResolve DOI: http://doi.org/10.1093/protein/7.11.1379
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TypeArticle
Journal titlepeds: protein engineering design & selection
Volume7
Issue11
Pages13791386; # of pages: 8
AbstractThe thermostability of the 20 396 Da Bacillus circulans xylanase was increased by the introduction of both intra and intermolecular disulfide bridges by site-directed muta-genesis. Based on the 3-D structure of the enzyme, sites were chosen where favourable geometry for a bridge existed; in one case, to obtain favourable geometry additional mutations around the cysteine sites were designed by computer modelling. The disulfide bonds introduced into the xylanase were mostly buried and, in the absence of protein denaturants, relatively insensitive to reduction by dithiothreitol. The mutant proteins were examined for residual enzymatic activity after various thermal treatments, and were assayed for enzymatic activity at elevated temperatures to assess their productivity. Wes have examined one of these mutants by X-ray crystallography. All of the disulfide bond designs tested increased the thermostability of the B.circulans xylanase, but not all enhanced the activity of the enzyme at elevated temperatures.
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberWAKARCHUK1994
NPARC number9371113
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Record identifier0aaa469c-d235-4e05-bd4c-44531c3951e6
Record created2009-07-10
Record modified2016-05-09
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