Janthinobacterium sp. 유래 저온 활성 프로테아제 정제

In this study, purification of cold-adapted protease from Janthinobacterium sp. was investigated. First, using gradient precipitation, protease was confirmed to be deposited in the 30-80% range of ammonium sulfate. Next, DEAE-Sepharose column was used for the binding of the protease under various co...

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Veröffentlicht in:Microbiology and biotechnology letters 2018, 46(2), , pp.111-113
Hauptverfasser: 김현도, Hyun-do Kim, 최종일, Jong-il Choi
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Sprache:kor
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Zusammenfassung:In this study, purification of cold-adapted protease from Janthinobacterium sp. was investigated. First, using gradient precipitation, protease was confirmed to be deposited in the 30-80% range of ammonium sulfate. Next, DEAE-Sepharose column was used for the binding of the protease under various conditions. The optimal binding condition was found to be pH 8.5 and flow rate of 30 ml/h. Under the optimal condition, the protease was purified with 29% recovery yield. This result can be useful for the purification of other cold-adapted protein.
ISSN:1598-642X
2234-7305