Single-step purification and characterization of an extreme halophilic, ethanol tolerant and acidophilic xylanase from Aureobasidium pullulans NRRL Y-2311-1 with application potential in the food industry

- An extracellular xylanase from Aureobasidium pullulans was produced on wheat bran.
- A single step, low cost chromatographic procedure was applied for purification.
- Xylanase was purified 3.4 fold with 80% recovery to apparent homogeneity.
- Novel properties of the Aureobasidium pullulans xylanase were elucidated.
- The enzyme was extreme halophilic, ethanol tolerant and acidophilic.

An extracellular xylanase from Aureobasidium pullulans NRRL Y-2311-1 produced on wheat bran was purified by a single-step chromatographic procedure. The enzyme had a molecular weight of 21.6 kDa. The optimum pH and temperature for xylanase activity were 4.0 and 30-50°C, respectively. The enzyme was stable in the pH range of 3.0-8.0. The inactivation energy of the enzyme was calculated as 218 kJ mol−1. The xylanase was ethanol tolerant and kept complete activity in the presence of 10% ethanol. Likewise, it retained almost complete activity at a concentration range of 0-20% NaCl. In general, the enzyme was resistant to several metal ions and reagents. Mg2+, Zn2+, Cu2+, K1+, EDTA and β-mercaptoethanol resulted in enhanced xylanase activity. The Km and Vmax values on beechwood xylan were determined to be 19.43 mg ml−1 and 848.4 U ml−1, respectively. The enzyme exhibits excellent characteristics and could, therefore, be a promising candidate for application in food and bio-industries.

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