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Purification and characterization of a psychrophilic catalase from Antarctic Bacillus

文献类型： 外文期刊

作者： Wang, Wei 1 ; Sun, Mi 1 ; Liu, Wanshun 2 ; Zhang, Bin 1 ;

作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Marine Prod & Enzyme Engn Lab, Qingdao 266071, Shandong, Peoples R China

2.Ocean Univ China, Coll Marine Life Sci, Qingdao 266003, Peoples R China

关键词： activation energy (E-a);k(cat)/K-m;psychrophilic monofunctional catalase;purification;thermostability

期刊名称：CANADIAN JOURNAL OF MICROBIOLOGY （ 影响因子：2.419； 五年影响因子：2.35 ）

ISSN： 0008-4166

年卷期： 2008 年 54 卷 10 期

页码：

收录情况： SCI

摘要： Catalase from Bacillus sp. N2a (BNC) isolated from Antarctic seawater was purified to homogeneity. BNC has a molecular mass of about 230 kDa and is composed of four identical subunits of 56 kDa. The catalase showed optimal activity at 25 degrees C and at a pH range of 6-11. The enzyme could be inhibited by azide, hydroxylamine, and mercaptoethanol. These characteristics suggested that BNC is a small-subunit monofunctional catalase. The activation energy of BNC was 13 kJ/mol and the apparent k(cat)/K-m values were 3.6 x 10(6) and 4 x 10(6) L center dot mol(-1 center dot)s(-1) at 4 and 25 degrees C, respectively. High catalytic efficiency of BNC at low temperatures enables this bacterium to scavenge H2O2 efficiently. BNC exhibited activation energy, catalytic efficiency, and thermostability comparable with some mesophilic homologues. Such similarity of enzymatic characteristics to mesophilic homologues, although uncommon among the cold-adapted enzymes in general, has also been observed in other psychrophilic small-subunit monofunctional catalases.

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