Heterologous expression of thermostable acetylxylan esterase gene from Thermobifida fusca and its synergistic action with xylanase for the production of xylooligosaccharides

The axe gene which encodes an acetylxylan esterase from Thermobifida fusca NTU22, was cloned, sequenced and expressed in Escherichia coli. The gene consists of 786 base pairs and encodes a protein of 262 amino acids. The deduced amino acid sequence of the acetylxylan esterase axe exhibited a high degree of similarity with BTA-hydrolase from T. fusca DSM43793, esterase from Thermobifida alba and lipase from Streptomyces albus. The optimal pH and temperature of the purified esterase were 7.5 and 60 °C, respectively. Cooperative enzymatic treatment of oat-spelt xylan by transformant xylanase and acetylxylan esterase significantly increased the xylooligosaccharides production compared with the xylanase or acetylxylan esterase action alone. The synergy of transformant acetylxylan esterase and xylanase cannot increase the production of reducing sugars from lignocellulolytic substrate, bagasse.

Research highlights
► The acetylxylan esterase gene from Thermobifida fusca NTU22, was cloned, sequenced and expressed in Escherichia coli.
► The deduced amino acid sequence of the acetylxylan esterase exhibited the highest degree of similarity with BTA-hydrolase from T. fusca DSM43793.
► The optimal pH and temperature of the purified esterase were 7.5 and 60 °C, respectively.
► Cooperative treatment of xylan by xylanase and acetylxylan esterase significantly increased the xylooligosaccharides production.
► The synergy of transformant acetylxylan esterase and xylanase cannot increase the reducing sugars production from bagasse.