Processing of XynE (110-kDa) of Aeromonas caviae ME-1 to 72-kDa xylanase in Escherichia coli transformant.

An extracellular 72-kDa xylanase from an Escherichia coli transformant that harbored pXED30 carrying xynE of Aeromonas caviae ME-1 was purified by extraction following SDS-PAGE to electrophoretic homogeneity. The analysis of N-terminal 10 amino acid residues (Gly-Ala-Arg-Ala-Gln-Ala-Ala-Ala-Asp-Val) revealed a 72-kDa product derived by the cleavage of Gly26-Gly27 at the N-terminal region of 110 kDa XynE. The 72-kDa xylanase from A. caviae ME-1 was found to have the same sequence as that of the N-terminal 10 amino acid residues. When OmpT-deficient E. coli mutants were used as hosts, the 72-kDa xylanase was detected in cell-free extracts, but not in the culture supernatant, suggesting that OmpT is not involved in the cleavage at the C-terminal region, but is involved in the secretion of 72-kDa xylanase to the culture medium.