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Characterization of a salt-resistant fibrinolytic protease of Bacillus licheniformis HJ4 isolated from Hwangseokae jeotgal, a traditional Korean fermented seafood

Authors
Meng, YuYao, ZhuangLe, Huong GiangLee, Se JinJeon, Hye SungYoo, Ji YeonKim, Jeong Hwan
Issue Date
Oct-2021
Publisher
Academy of Sciences of the Czech Republic
Citation
Folia Microbiologica, v.66, no.5, pp 787 - 795
Pages
9
Indexed
SCIE
SCOPUS
Journal Title
Folia Microbiologica
Volume
66
Number
5
Start Page
787
End Page
795
URI
https://scholarworks.gnu.ac.kr/handle/sw.gnu/3190
DOI
10.1007/s12223-021-00878-w
ISSN
0015-5632
1874-9356
Abstract
Bacillus licheniformis HJ4 showing strong fibrinolytic activity was isolated from Hwangseokae jeotgal. aprEHJ4, a major fibrinolytic gene, was cloned by PCR, and an ORF consisting of 379 amino acids was located. The mature enzyme was expected to be 27 kDa in size after processing, but a 24-kDa protein was observed by SDS-PAGE and fibrin zymography, indicating additional processing. RT-qPCR showed that expression level of aprEHJ4 in culture with 0% salt (control) was the highest followed by culture with 8% salt (89.7% of control) and 5% salt (74.2%) at 84 h. The expression level in culture with 15% salt was 46.9%. The results matched with the fibrinolytic activity measurements of cultures and indicated that AprEHJ4 maintained significant activity in the presence of salt up to 15% (w/v). AprEHJ4 was overproduced in Escherichia coli, and mature 27 kDa protein was purified after in vitro renaturation. The optimum pH and temperature of AprEHJ4 were pH 8 and 40 celcius, respectively.
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