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The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity

Bacteriology Group, International Centre for Genetic Engineering and Biotechnology, Area Science Park, Padriciano 99, I-34012 Trieste, Italy¹
Institute of Molecular Genetics and Genetic Engineering, Vojvode Stepe 444a, 11000 Belgrade, Yugoslavia²

Author for correspondence: Vittorio Venturi. Tel: +39 040 3757317. Fax: +39 040 226555. e-mail: venturi{at}icgeb.trieste.it

The Bacillus pumilus gene encoding acetyl xylan esterase (axe) was identified and characterized. The axe gene was expressed and the recombinant enzyme produced in Escherichia coli was purified and characterized. The recombinant enzyme displayed similar properties to the acetyl xylan esterase (AXE) purified from B. pumilus. The AXE primary structure was 76% identical to the cephalosporin C deacetylase of B. subtilis, and 40% to two recently identified AXEs from Thermoanaerobacterium and Thermotoga maritima. These four proteins are of similar size and represent a new family of esterases having a broad substrate specificity. The recombinant AXE was demonstrated to have activity on several acetylated substrates, including on cephalosporin C.

Keywords: Bacillus pumilus, acetyl xylan esterase, cephalosporin C deacetylase

Abbreviations: AXE, acetyl xylan esterase; rAXE, recombinant xylan esterase

The GenBank/EMBL/DDBJ accession number for the sequence reported in this paper is AJ249957.

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