Cloning and Expression of D-Mannose Isomerase from Escherichia coli BL21 and its Application for D-Mannose Production

doi:10.3969/j.issn.1673-1689.2019.04.009

Home > Archive>Volume 38, Issue 4, 2019 >58-63. DOI:10.3969/j.issn.1673-1689.2019.04.009

Cloning and Expression of D-Mannose Isomerase from Escherichia coli BL21 and its Application for D-Mannose Production
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                        10.3969/j.issn.1673-1689.2019.04.009
                    
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The gene encoding D-mannose isomerase（MIase） from Escherichia coli（E. coli） BL21 was cloned into expression vector pET-28a（+），and then the recombinant plasmid was transformed into the strain E. coli BL21（DE3）. Efficient MIase intracellular expression by the recombinant E. coli BL21 was achieved with an activity of 4.2 U/mL（D-mannose forming） after IPTG induction for 6 h. The enzyme was identified as a metal-independent protein. The enzyme activity reached the maximum with a conversion rate of 25% at 40 ℃ and pH 7.5. Using D-fructose as the substrate，a Km value of 123.32 mmol/L，Vmax value of 113.64 μmol/（min·mg） and catalytic efficiency kcat/Km value of 0.691 s·mmol/L were estimated，respectively.

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HU Xing, ZHANG Tao, MU Wanmeng, MIAO Ming, JIANG Bo. Cloning and Expression of D-Mannose Isomerase from Escherichia coli BL21 and its Application for D-Mannose Production[J]. Journal of Food Science and Biotechnology,2019,38(4):58-63.

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Online: July 03,2019
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