Purification and Characterization of Subtilisin DJ-4 Secreted by Bacillus sp. Strain DJ-4 Screened from Doen-Jang
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概要
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Bacillus sp. strain DJ-4,which produces extracellular proteases, was screened from Doen-Jang, a traditional Korean fermented food. A fibrinolytic enzyme (subtilisin DJ-4) was purified using commercial chromatographic techniques. The relative molecular mass of the isolated protein was 29 kDa by SDS-PAGE and fibrin zymography assay. The enzyme was characterized as a serine protease by an inhibitor assay on the fibrin zymography gel and by an amidolytic assay using a chromogenic substrate. The enzyme was inhibited by PMSF, but not by EDTA or leupeptin. The first 14 amino acids of the N-terminal sequence were identical to that of subtilisin BPN', but the activity of subtilisin DJ-4 was 2.2 and 4.3 times higher than those of subtilisin BPN'and subtilisin Carlsberg, respectively.
- 社団法人日本農芸化学会の論文
- 2000-08-23
著者
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Kim S‐h
Protein Engineering Group Korea Research Institute Of Bioscience And Biotechnology
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KIM SeungHo
Protein Engineering Group, Korea Research Institute of Bioscience and Biotechnology
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CHOI NackShick
Protein Engineering Group, Korea Research Institute of Bioscience and Biotechnology
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Choi Nackshick
Protein Engineering Group Korea Research Institute Of Bioscience And Biotechnology
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Kim Seung-Ho
Protein Engineering Group, Korea Research Institute of Bioscience and Biotechnology
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Choi Nack-Shick
Protein Engineering Group, Korea Research Institute of Bioscience and Biotechnology
関連論文
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- Purification and Characterization of Subtilisin DJ-4 Secreted by Bacillus sp. Strain DJ-4 Screened from Doen-Jang
- Structures of Ovine Corticotropin-Releasing Factor and Its Ala32 Mutant as Studied by CD and NMR Techniques.