Enhanced alkaline catalase production by Serratia marcescens FZSF01: enzyme purification, characterization, and recombinant expression
Electron. j. biotechnol
; 30: 110-117, nov. 2017. graf, tab, ilus
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| ID: biblio-1021571
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ABSTRACT
Background:
Catalase (CAT) is an important enzyme that degrades H2O2 into H2O and O2. 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 twosteps:
DEAE-fast flow and Sephedex-G150. The purified catalase showed a specific activity of 197,575 U/mg with a molecular mass of 58 kDa. This catalase exhibited high activity at 2070°C and pH 5.011.0. Km of the catalase was approximately 68 mM, and Vmax was 1886.8 mol/min mg. This catalase was further identified by LCMS/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.Palavras-chave
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LILACS
Assunto principal:
Serratia marcescens
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Catalase
Idioma:
En
Revista:
Electron. j. biotechnol
Assunto da revista:
BIOTECNOLOGIA
Ano de publicação:
2017
Tipo de documento:
Article
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Project document