Purification and properties of xylanase fromAureobasidium

Summary The yeast-like fungusAureobasidium is a promising source of xylanase (EC 3.2.1.8) with an exceptionally high specific activity. For enzyme production in volumes of several liters, xylose was the preferred carbon source and inducer. Xylanase in clarified cultures was concentrated by reversible adsorption to cation-exchange matrix to 5% of the initial volume, and recovered at nearly 2 million IU/1. Selective conditions permitted 97% recovery of xylanase with a 1.8-fold enrichment in specific activity, to 70% of purity. The predominant xylanase species (20 kDa) was subsequently purified to >99% of homogeneity by gel filtration chromatography. Purified enzyme exhibited an isoelectric point of 8.5, and specific activity of 2100 IU/mg under optimal conditions, determined to be pH 4.5 and 45°C. The activity of purified enzyme was specific for polymeric xylan.The mention of firm names or trade products does not imply that they are endorsed or recommended by the U.S. Dept. of Agirculture over other firms or similar products not mentioned.