PURIFICATION AND PARTIAL CHARACTERIZATION OF A GUT TRYPSIN-LIKE PROTEASE FROM LARVAE OF FLESH FLY BOETTCHERISCA PEREGRIN A (DIPTERA: SARCOPHAGAE) |
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Authors: | Xiaofeng Lu Xingyong Yang Jingqiu Cheng Yan Pei |
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Institution: | Center Biotechnology, Southwesl Agricultural University, Chongqing, 400716, China |
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Abstract: | 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. |
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Keywords: | trypsin-like protease Boettcherisca peregrina purification characterization |
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