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Specificity and mode of action of a thermostable xylanase from bacillus amyloliquefaciens on-line monitoring of hydrolysis products

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Abstract

A thermostable xylanase purified from a strain of Bacillus amyloliquefaciens MIR 32 was characterized with respect to its substrate specificity and mode of hydrolytic action. The enzyme was highly specific for xylans as substrate and displayed no activity toward other polysaccharides, including cellulose. The enzyme exhibited Km and Vmax of 4.5 mg/mL and 0.58 mmol/min/mg, respectively, with birchwood xylan as the substrate. Microdialysis sampling with anion exchange chromatography and integrated pulsed electrochemical detection were used for rapid on-line monitoring of products during hydrolysis of oat spelt and bagasse xylan, and xylooligosaccharides. Xylobiose and xylotriose were the main end products. Xylotetraose was the smallest oligosaccharide to be acted on by the xylanase. The product pattern confirmed that the enzyme was an endoxylanase.

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Authors and Affiliations

  1. Cátedra de Microbiología Superior Facultad de Química Bioquímica y Farmacia, Universidad Nacional de Tucumán, Tucumán, Argentina

    Javier D. Breccia & Faustino Siñeriz

  2. PROIMIMIRCEN Avda. Belgrano y Caseros, 4000, Tucumán, Argentina

    Javier D. Breccia & Faustino Siñeriz

  3. Department of Analytical Chemistry, Argentina

    Nelson Torto & Lo Gorton

  4. Department of Biotechnology Center for Chemistry and Chemical Engineering, Lund University, S-221 00, P.O. Box 124, Lund, Sweden

    Rajni Hatti-Kaul

Authors
  1. Javier D. Breccia
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  2. Nelson Torto
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  3. Lo Gorton
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  4. Faustino Siñeriz
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  5. Rajni Hatti-Kaul
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Breccia, J.D., Torto, N., Gorton, L. et al. Specificity and mode of action of a thermostable xylanase from bacillus amyloliquefaciens on-line monitoring of hydrolysis products. Appl Biochem Biotechnol 69, 31–40 (1998). https://doi.org/10.1007/BF02786019

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  • DOI: https://doi.org/10.1007/BF02786019

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