PURIFICATION AND PARTIAL CHARACTERIZATION OF A GUT TRYPSIN‐LIKE PROTEASE FROM LARVAE OF FLESH FLY BOETTCHERISCA PEREGRIN A (DIPTERA: SARCOPHAGAE)

Abstract A 16kD protease was purified from the gut extract of larvae of Boettcherisca peregrina, after ammonium sulfate precipitation, DEAE‐Sephadex A‐25 ion‐exchange chromatography and SBBI‐Sepharose 4B affinity chromatography. The results of substrate and inhibitor specificity indicated that the protease behaved as a trypsin‐like protease. It possesses high activity against non‐specific substrate casein and Hide powder azure, and against trypsin‐specific substrates Bz‐Phe‐Val‐Arg NA, Bz‐Pro‐Phe‐Arg NA and Bz‐Val‐Gly‐Arg NA. It can be strongly inhibited by PMSF, phenymethysulfonyl fluoride (serine protease inhibitor), SBBI, soybean Bowman‐Birk inhibitor and Leupeptin (trypsin‐specific inhibitor). Activity of this protease was found to be maximal at the alkaline range of pH 8. 5–9. 5.