Purification and Characterization of Catalase from Marine Bacterium Acinetobacter sp YS0810
文献类型： 外文期刊
作者： Fu, Xinhua 1 ; Wang, Wei 1 ; Hao, Jianhua 1 ; Zhu, Xianglin 4 ; Sun, Mi 5 ;
作者机构： 1.Chinese Acad Fishery Sci, Minist Agr, Yellow Sea Fisheries Res Inst, Key Lab Sustainable Dev Marine Fisheries, Qingdao 266071, Peoples R China
2.Shanghai Ocean Univ, Shanghai 201306, Peoples R China
3.Weifang Med Univ, Weifang 261053, Peoples R China
4.Jiangsu Univ, Sch Elect & Informat Engn, Zhenjiang 212013, Peoples R China
5.Yellow Sea Fisheries Res Inst, Marine Prod Resource & Enzyme Engn, Qingdao 266071, Shandong, Peoples R China
期刊名称：BIOMED RESEARCH INTERNATIONAL （ 影响因子：3.411； 五年影响因子：3.62 ）
ISSN： 2314-6133
年卷期： 2014 年
页码：
收录情况： SCI
摘要： The catalase from marine bacterium Acinetobacter sp. YS0810 (YS0810CAT) was purified and characterized. Consecutive steps were used to achieve the purified enzyme as follows: ethanol precipitation, DEAE Sepharose ion exchange, Superdex 200 gel filtration, and Resource Q ion exchange. The active enzyme consisted of four identical subunits of 57.256 kDa. It showed a Soret peak at 405 nm, indicating the presence of iron protoporphyrin IX. The catalase was not apparently reduced by sodium dithionite but was inhibited by 3-amino-1,2,4-triazole, hydroxylamine hydrochloride, and sodium azide. Peroxidase-like activity was not found with the substrate o-phenylenediamine. So the catalase was determined to be a monofunctional catalase. N-terminal amino acid of the catalase analysis gave the sequence SQDPKKCPVTHLTTE, which showed high degree of homology with those of known catalases from bacteria. The analysis of amino acid sequence of the purified catalase by matrix-assisted laser desorption ionization time-of-flight mass spectrometry showed that it was a new catalase, in spite of its high homology with those of known catalases from other bacteria. The catalase showed high alkali stability and thermostability.
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