Characterization of a recombinant l-ribose isomerase from Mycetocola miduiensis and its application for the production of l-ribulose

•l-Ribulose producing l-ribose isomerase was characterized from Mycetocola miduiensis.•Mm-LRIse showed maximum activity at 40 °C and pH 7.5 in sodium phosphate (50 mM) buffer.•Mm-LRIse showed the highest specific activity (47.40 U mg−1) with l-ribose as substrate as compared to other l-RIs.•It produced 32 % l-ribulose as the sole product from l-ribose. An enzyme, l-ribose isomerase (l-RI), mostly catalyzes the isomerization of l-ribose and l-ribulose. These so-called rare sugars are essential for the treatment of cancer and other viral diseases. In the present study, l-ribose isomerase produced from a bacterium, Mycetocola miduiensis (Mm-LRIse), by using l-ribose as a carbon source. The recombinant l-ribose isomerase gene was cloned and overexpressed from M. miduiensis and purified with an exclusive band of 32 kDa by nickel-affinity chromatography. This gene possessed 267 amino acids protein having an estimated molecular weight of 29,568.17 Da. The native molecular weight of Mm-LRIse estimated by HPLC was 134.84 kDa. The recombinant l-ribose isomerase was highly active in sodium phosphate (50 mM) buffer at 40 °C and pH 7.5, showing the specific activity up to 47.40 U mg−1. Mm-LRIse showed no significant enhancement in activity with metallic ions except Mn2+ and Co2+. The values of Km, Kcat, Kcat/Km and Vmax of Mm-LRIse against l-ribose substrate were 42.48 mM, 9259.26 min−1, 217.43 min−1 mM−1, and 277.78 U mg−1 respectively. At equilibrium, the l-ribulose transformation rate was nearly 32 % (6.34 g L−1) using 20 g L−1 of l-ribose. The results revealed that the Mm-LRIse enzyme has a potential for L-ribulose production from l-ribose.