%0 Journal Article
%T Purification and characterization of extracellular halophilic protease from haloarchaea Natrinema sp.R6-5<br>极端嗜盐古生菌(Natrinema sp.)R6-5胞外嗜盐蛋白酶的纯化和性质研究
%A SHI Wan-liang
%A ZHONG Chuan-qi
%A TANG Bing
%A SHEN Ping
%A <br>石万良
%A 钟传奇
%A 唐兵
%A 沈萍
%J 微生物学报
%D 2007
%I 
%X A halophilic extracellular protease from a halophilic archaea Natrinema sp. R6-5 was purified to SDS-PAGE homogeneity using bacitracin-Sepharose 4B chromatography. A molecular mass of the purified protease subunit was 62KD determined by SDS-PAGE. The protease activity was inhibited by phenylmethylsulfonyl fluoride (PMSF), suggesting that the protease belong to serine protease. The protease exhibited optimum NaCl concentration is 3 mol/L. At the 3 mol/L NaCl concentration, the optimum temperature and the optimum pH were 45 degrees C and 8.0. The protease could keep high activity and stability in high salt environment and had potential application value.
%K Halophilic archaea
%K Extracellular halophilic protease
%K Purification
%K Properties<br>嗜盐古生菌
%K 胞外嗜盐蛋白酶
%K 纯化
%K 性质
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=2AA3B51CED64DFD0&yid=A732AF04DDA03BB3&vid=F4B561950EE1D31A&iid=CA4FD0336C81A37A&sid=8575BEDA702C4B7C&eid=D5C9DC4EF2F78008&journal_id=0001-6209&journal_name=微生物学报&referenced_num=1&reference_num=8