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Purification and Characterization of an Extracellular Cold-Active Serine Protease from the Psychrophilic Bacterium Colwellia sp. NJ341
Authors:Quan-Fu?Wang,Jin-Lai?Miao  author-information"  >  author-information__contact u-icon-before"  >  mailto:miaojinlai@.com"   title="  miaojinlai@.com"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author,Yan-Hua?Hou,Yu?Ding,Guo-Dong?Wang,Guang-You?Li
Affiliation:(1) College of life Sciences, Ocean University of China, 266003 Qingdao, P.R. China;(2) Key Laboratory of Marine Bio-active Substances, First Institute of Oceanorgarphy, State Oceanic Administration, 266061 Qingdao, P.R. China;(3) Harbin Institute of Technology, 264209 Weihai, P.R. China
Abstract:Colwellia sp. NJ341, isolated from Antarctic sea ice, secreted a cold-active serine protease. The purified protease had an apparent Mr of 60 kDa by SDS-PAGE and MALDI-TOF MS. It was active from pH 5–12 with maximum activity at 35 °C (assayed over 10 min). Activity at 0 °C was nearly 30% of the maximum activity. It was completely inhibited by phenylmethylsulfonyl fluoride.
Keywords:Antarctic  cold-active serine protease  Colwellia  psychrophilic bacteria
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