Single-step purification, characterization and immobilization of a sucrose isomerase from Erwinia sp.

•Sucrose isomerase from Erwinia sp. was purified using only one step.•Crude and purified sucrose isomerase were successfully characterized with RSM.•Purified sucrose isomerase converted sucrose into 63% of isomaltulose.•Conversion of sucrose into isomaltulose catalyzed by immobilized enzyme was optimized.•Immobilized sucrose isomerase converted sucrose into 64% of isomaltulose.

After single-step purification to 17-fold purity, the sucrose isomerase obtained from Erwinia sp. showed specific activity of 38.75 U/mg of protein and a molecular mass of 65 kDa. The optimal pH and temperature range were 6.3 and 30–35 °C, respectively, resulting in enzymatic activities higher than 60 U/mL and 22 U/mL for the crude and purified enzymes, respectively. Both enzymatic preparations presented greater stability in the pH range 5.0–7.0 and at temperatures below 30 °C. The purified sucrose isomerase converted sucrose into 63% of isomaltulose and 30% of trehalulose at pH 6.3 and 33 °C. The optimal reaction conditions for the conversion of sucrose into isomaltulose catalyzed by the immobilized sucrose isomerase was at a pH range 6.0–6.5 and 35–40 °C.