Purification and Characterization of Maleate Cis-Trans Isomerase from Serratia marcescens

doi:10.3969/j.issn.1673-1689.2014.11.013

Home > Archive>Volume 33, Issue 11, 2014 >1204-1209. DOI:10.3969/j.issn.1673-1689.2014.11.013

Purification and Characterization of Maleate Cis-Trans Isomerase from Serratia marcescens
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                        10.3969/j.issn.1673-1689.2014.11.013
                    
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The gene of maleate cis-trans isomerase(MaiA) from Serratia marcescens was cloned and successfully expressed in Escherichia coli BL21(DE3) and was purified. The specific activity of the purified enzyme was 48.01 U/mg. The optimum temperature was 37 ℃ and the optimum pH was 8.4. Under the optimum condition, the Km value was 4.2 mmol/L, the Vmax value was 1.27 mmol/(L·min), the kcat value was 4.38 s-1 and the catalytic efficiency(kcat/Km) was 1.04 L/(mmol·s). Furthermore, the research showed that the MaiA had high thermostability(t1/2=1.5 h). Meanwhile, maleate could almost be converted to fumarate completely by the recombinant MaiA with high efficiency up to 99%. The results in this study will be useful for further research and industrial applications of maleate cis-trans isomerase.

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WANG Ya, CUI Wenjing, ZHOU Li, LIU Zhongmei, ZHOU Zhemin. Purification and Characterization of Maleate Cis-Trans Isomerase from Serratia marcescens[J]. Journal of Food Science and Biotechnology,2014,33(11):1204-1209.

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Online: December 19,2014
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