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β-d-Xylosidase from Selenomonas ruminantium: Thermodynamics of Enzyme-Catalyzed and Noncatalyzed Reactions

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Abstract

β-d-Xylosidase/α-l-arabinofuranosidase from Selenomonas ruminantium is the most active enzyme known for catalyzing hydrolysis of 1,4-β-d-xylooligosaccharides to d-xylose. Temperature dependence for hydrolysis of 4-nitrophenyl-β-d-xylopyranoside (4NPX), 4-nitrophenyl-α-l-arabinofuranoside (4NPA), and 1,4-β-d-xylobiose (X2) was determined on and off (k non) the enzyme at pH 5.3, which lies in the pH-independent region for k cat and k non. Rate enhancements (k cat/k non) for 4NPX, 4NPA, and X2 are 4.3 × 1011, 2.4 × 109, and 3.7 × 1012, respectively, at 25 °C and increase with decreasing temperature. Relative parameters k cat 4NPX/k cat 4NPA, k cat 4NPX/k cat X2, and (k cat/K m)4NPX/(k cat/K m)X2 increase and (k cat/K m)4NPX/(k cat/K m)4NPA, (1/K m)4NPX/(1/K m)4NPA, and (1/K m)4NPX/(1/K m)X2 decrease with increasing temperature.

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Authors and Affiliations

  1. Fermentation Biotechnology Research Unit, National Center for Agricultural Utilization Research, US Department of Agriculture, Agricultural Research Service, 1815 N. University Street, Peoria, IL, 61604, USA

    Douglas B. Jordan & Jay D. Braker

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  1. Douglas B. Jordan
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Correspondence to Douglas B. Jordan.

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The mention of firm names or trade products does not imply that they are endorsed or recommended by the US Department of Agriculture over other firms or similar products not mentioned.

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Jordan, D.B., Braker, J.D. β-d-Xylosidase from Selenomonas ruminantium: Thermodynamics of Enzyme-Catalyzed and Noncatalyzed Reactions. Appl Biochem Biotechnol 155, 27–43 (2009). https://doi.org/10.1007/s12010-008-8397-7

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