Enhanced alkaline catalase production by Serratia marcescens FZSF01: Enzyme purification, characterization, and recombinant expression

文献类型： 外文期刊

第一作者： Jia, Xianbo

作者： Jia, Xianbo;Lin, Xinjian;Lin, Chenqiang;Chen, Jichen;Jia, Xianbo;Lin, Lirong;Chen, Jichen

作者机构：

关键词： Alkaline;Catalase activity;Catalase assay;Catalase gene;Catalase producing strains;Catalase purification;Catalase;Fermentation;Hydrogen peroxide;Ultrasonication

期刊名称：ELECTRONIC JOURNAL OF BIOTECHNOLOGY （ 影响因子：2.8； 五年影响因子：3.379 ）

ISSN： 0717-3458

年卷期： 2017 年 30 卷

页码：

收录情况： SCI

摘要： Background: Catalase (CAT) is an important enzyme that degrades H2O2 into H2O and O-2. To obtain an efficient catalase, in this study, a new strain of high catalase-producing Serratia marcescens, named FZSF01, was screened and its catalase was purified and characterized. Results: After optimization of fermentation conditions, the yield of catalase produced by this strain was as high as 51,468 U/ml. This catalase was further purified using two steps: DEAE-fast flowand Sephedex-G150. The purified catalase showed a specific activity of 197,575 U/mgwith a molecular mass of 58 kDa. This catalase exhibited high activity at 20-70 degrees C and pH 5.0-11.0. Km of the catalase was approximately 68 mM, and Vmax was 1886.8 mol/min mg. This catalase was further identified by LC-MS/MS, and the encoding gene was cloned and expressed in Escherichia coli BL21 (DE3) with a production of 17,267 +/- 2037 U/ml. Conclusions: To our knowledge, these results represent one of the highest fermentation levels reported among current catalase-producing strains. This FZSF01 catalase may be suitable for several industrial applications that comprise exposure to alkaline conditions and under a wide range of temperatures. (C) 2017 Pontificia Universidad Catalica de Valparaiso. Production and hosting by Elsevier B.V. All rights reserved.

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