Journal
BIOTECHNOLOGY LETTERS
Volume 43, Issue 1, Pages 261-269Publisher
SPRINGER
DOI: 10.1007/s10529-020-02999-7
Keywords
Sucrose isomerase; Isomaltulose; Biotransformation; Purification; Characterization
Categories
Funding
- Leading Innovative and Entrepreneur Team Introduction Program of Zhejiang, P. R. China [2018R01014]
- Zhejiang provincial Qianjiang talent project
Ask authors/readers for more resources
The study characterized a recombinant isomerase that can convert sucrose to isomaltulose, with the enzyme showing excellent capability for this biotransformation. Further research is needed to explore suitable heterologous expression systems in order to improve its expression level.
Objective To characterize a recombinant isomerase that can catalyze the isomerization of sucrose into isomaltulose and investigate its application for the enzymatic production of isomaltulose. Results A sucrose isomerase gene fromErwinia sp. Ejp617 was synthesized and expressed inEscherichia coliBL21(DE3). The enzymatic characterization revealed that the optimal pH and temperature of the purified sucrose isomerase were 6.0 and 40 degrees C, respectively. The enzyme activity was slightly activated by Mn(2+)and Mg2+, but partially inhibited by Ca2+, Ba2+, Cu2+, Zn(2+)and EDTA. The kinetic parameters ofK(m)andV(max)for sucrose were 69.28 mM and 118.87 U/mg, respectively. The time course showed that 240.9 g/L of isomaltulose was produced from 300 g/L of sucrose, and the yield reached 80.3% after bioreaction for 180 min. Conclusions This recombinant enzyme showed excellent capability for biotransforming sucrose to isomaltulose at the substrate concentration of 300 g/L. Further investigations should be carried out focusing on selection of suitable heterologous expression system with the aim to improve its expression level.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available