Purification and characterization of subtilisin DJ-4 secreted by Bacillus sp. strain DJ-4 screened from Doen-Jang

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Title
Purification and characterization of subtilisin DJ-4 secreted by Bacillus sp. strain DJ-4 screened from Doen-Jang
Author(s)
Seung Ho Kim; Nack Shick Choi
Bibliographic Citation
Bioscience Biotechnology and Biochemistry, vol. 64, no. 8, pp. 1722-1725
Publication Year
2000
Abstract
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.
Keyword
Bacillus sp. DJ-4subtilisin DJ-4fibrin zymographyfermented food
ISSN
0916-8451
Publisher
T&F (Taylor & Francis)
DOI
http://dx.doi.org/10.1271/bbb.64.1722
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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