Janthinobacterium sp. 유래 저온 활성 프로테아제 정제
Purification of Cold-adapted Protease from Janthinobacterium sp.
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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.
Abstract
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.
참고문헌 (13)
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