Properties of a fibrinolytic enzyme secreted by Bacillus subtilis JS2 isolated from saeu (small shrimp) jeotgal .

Autor: Yao Z; 1Division of Applied Life Science (BK21 Plus), Graduate School, Gyeongsang National University, Jinju, 52828 Korea., Kim JA; 1Division of Applied Life Science (BK21 Plus), Graduate School, Gyeongsang National University, Jinju, 52828 Korea., Kim JH; 1Division of Applied Life Science (BK21 Plus), Graduate School, Gyeongsang National University, Jinju, 52828 Korea.; 2Institute of Agriculture and Life Science, Gyeongsang National University, Jinju, 52828 Korea.
Jazyk: angličtina
Zdroj: Food science and biotechnology [Food Sci Biotechnol] 2017 Dec 26; Vol. 27 (3), pp. 765-772. Date of Electronic Publication: 2017 Dec 26 (Print Publication: 2018).
DOI: 10.1007/s10068-017-0299-4
Abstrakt: Bacillus species were screened to be used as starters for jeotgals , salted and fermented Korean sea foods. A strain, JS2, showing strong fibrinolytic activity was isolated from saeu (small shrimp) jeotgal , and identified as Bacillus subtilis. Bacillus subtilis JS2 grew well at 20% (w/v) NaCl concentration. SDS-PAGE of culture supernatant from JS2 showed 3 major bands of 27, 29, and 60 kDa in size. Fibrin zymography showed that the 27 kDa band was the major fibrinolytic protein. The gene, aprEJS2 , was cloned and introduced into B. subtilis WB600 using pHY300PLK. A B. subtilis transformant harboring pHYJS2 showed higher fibrinolytic activity than B. subtilis JS2. aprEJS2 was overexpressed in Escherichia coli BL21 (DE3). The optimum pH and temperature for AprEJS2 were pH 8.0 and 40 °C, respectively. Km and V max values were determined. AprEJS2 has strong α-fibrinogenase activity and moderate β-fibrinogenase activity.
Competing Interests: Compliance with ethical standardsThe authors declare that they have no conflict of interest.
Databáze: MEDLINE
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