Serratia Protease |
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Authors: | Kouichi Miyata Kazutaka Maejima Katsumi Tomoda Masao Isono |
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Institution: | Microbiological Research Laboratories, Research and Development Division, Takeda Chemical Ind., Ltd., Osaka |
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Abstract: | A strain of Serratia, isolated from an intestinal canal of a silkworm, produced a large quantity of protease. The enzyme was extracellular and was named Serratiopeptidase, tentatively. Protease production of this strain was over 3 times as much as that of Serratia marcescens which was known as a protease-producing organism. The highly purified enzyme was prepared from the culture supernatant through ammonium sulfate precipitation, acetone fractionation, DEAE-cellulose column chromatography and gel filtration on Sephadex G-75.The purified enzyme moved homogeneously with a sedimentation constant, s20,w of 3.8 S in ultracentrifugation and the molecular weight was determined to be 6.0 × 104 by the Archibald method. Determination of the ultraviolet absorption spectrum indicated the E1%280 mμ,1 cm was 13.0. Neither carbohydrate nor sulfur-containing amino acid was detected in the purified enzyme preparation. The enzyme showed maximal activity at pH 9.0 and at 40°C, and was stable under lower temperatures over the pH range from 5 to 10, whereas it was unstable at 37°C in alkaline conditions. The enzyme was completely inactivated by heating at 55°C for 15 min. |
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