Characterizing the pH-dependent stability and catalytic mechanism of the family 11 xylanase from the alkalophilic Bacillus agaradhaerens

The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B. circulans. Despite the alkaline versus neutral conditions under which these bacteria grow, BadX and BcX both exhibit optimal activity near pH...

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Published inCarbohydrate research Vol. 338; no. 5; pp. 415 - 421
Main Authors Poon, David K.Y., Webster, Philip, Withers, Stephen G., McIntosh, Lawrence P.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier Ltd 14.02.2003
Subjects
Bacillus - enzymology
Bacillus xylanase
Extremophile
Glycosidase
Hot Temperature
Hydrogen-Ion Concentration
pH-Dependent mechanism
Protein Denaturation
Protein stability
Xylan Endo-1,3-beta-Xylosidase
Xylosidases - metabolism
Bacillus xylanase
Glycosidase
Protein stability
Extremophile
pH-Dependent mechanism
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Abstract The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B. circulans. Despite the alkaline versus neutral conditions under which these bacteria grow, BadX and BcX both exhibit optimal activity near pH 5.6 using the substrate o-nitrophenyl β-xylobioside. Analysis of the bell-shaped activity profile of BadX yielded apparent p K a values of 4.2 and 7.1, assignable to its nucleophile Glu94 and general acid Glu184, respectively. In addition to having an ∼10-fold higher k cat/ K m value with this substrate at pH 6 and 40 °C, BadX has significantly higher thermal stability than BcX under neutral and alkaline conditions. This enhanced stability, rather than a shift in its pH-optimum, may allow BadX to hydrolyze xylan under conditions of elevated temperature and pH. Graphic
AbstractList The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B. circulans. Despite the alkaline versus neutral conditions under which these bacteria grow, BadX and BcX both exhibit optimal activity near pH 5.6 using the substrate o-nitrophenyl β-xylobioside. Analysis of the bell-shaped activity profile of BadX yielded apparent p K a values of 4.2 and 7.1, assignable to its nucleophile Glu94 and general acid Glu184, respectively. In addition to having an ∼10-fold higher k cat/ K m value with this substrate at pH 6 and 40 °C, BadX has significantly higher thermal stability than BcX under neutral and alkaline conditions. This enhanced stability, rather than a shift in its pH-optimum, may allow BadX to hydrolyze xylan under conditions of elevated temperature and pH. Graphic
The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B. circulans. Despite the alkaline versus neutral conditions under which these bacteria grow, BadX and BcX both exhibit optimal activity near pH 5.6 using the substrate o-nitrophenyl beta-xylobioside. Analysis of the bell-shaped activity profile of BadX yielded apparent pKa values of 4.2 and 7.1, assignable to its nucleophile Glu94 and general acid Glu184, respectively. In addition to having an approximately 10-fold higher kcat/Km value with this substrate at pH 6 and 40 degrees C, BadX has significantly higher thermal stability than BcX under neutral and alkaline conditions. This enhanced stability, rather than a shift in its pH-optimum, may allow BadX to hydrolyze xylan under conditions of elevated temperature and pH.
The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B. circulans. Despite the alkaline versus neutral conditions under which these bacteria grow, BadX and BcX both exhibit optimal activity near pH 5.6 using the substrate o-nitrophenyl beta-xylobioside. Analysis of the bell-shaped activity profile of BadX yielded apparent pK(a) values of 4.2 and 7.1, assignable to its nucleophile Glu94 and general acid Glu184, respectively. In addition to having an approximately 10-fold higher k(cat)/K(m) value with this substrate at pH 6 and 40 degrees C, BadX has significantly higher thermal stability than BcX under neutral and alkaline conditions. This enhanced stability, rather than a shift in its pH-optimum, may allow BadX to hydrolyze xylan under conditions of elevated temperature and pH.
Author Withers, Stephen G.
Webster, Philip
Poon, David K.Y.
McIntosh, Lawrence P.
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Keywords Bacillus xylanase
Glycosidase
Protein stability
Extremophile
pH-Dependent mechanism
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Snippet The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B....
The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B....
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SubjectTerms Bacillus - enzymology
Bacillus xylanase
Extremophile
Glycosidase
Hot Temperature
Hydrogen-Ion Concentration
pH-Dependent mechanism
Protein Denaturation
Protein stability
Xylan Endo-1,3-beta-Xylosidase
Xylosidases - metabolism
Title Characterizing the pH-dependent stability and catalytic mechanism of the family 11 xylanase from the alkalophilic Bacillus agaradhaerens
URI https://dx.doi.org/10.1016/S0008-6215(02)00486-X
https://www.ncbi.nlm.nih.gov/pubmed/12559743
https://search.proquest.com/docview/72985380
Volume 338
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