Peptidases of pinworms Syphacia muris and Passalurus ambiguus

In this first report about pinworms peptidases we primarily characterize peptidases released during in vitro maintenance of two common pinworms of laboratory animals – Syphacia muris and Passalurus ambiguus. The peptidase activity obtained using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS–PAGE) showed the presence of peptidases from S. muris with a wide range of molecular size (25–110 kDa), which degrades gelatin and mucin at alkaline pH levels. P. ambiguus released serine and aspartyl peptidases degrading gelatin at all tested pH (3, 5, 7, and 9) and at acidic pH Passalurus released aspartyl and cysteine peptidases which are active against mucin.