Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 139, Issue -, Pages 1002-1008Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2019.08.075
Keywords
Cellobiose 2-epimerase; MD simulation; Thermal stability; Lactulose
Funding
- Postgraduate Research & Practice Innovation Program of Jiangsu Provence [KYCX17_1406]
- National Natural Science Foundation of China [31801583]
- Natural Science Foundation of Jiangsu Province [BK20180607]
- Fundamental Research Funds for the Central Universities [JUSRP11966]
- National First-Class Discipline Program of Food Science and Technology [JUFSTR20180203]
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Cellobiose 2-epimerase (CE) is a promising industrial enzyme that can be utilized in the dairy industry. More thermostable CEs from different microorganisms are still needed for a higher lactulose productivity. This study demonstrated the feasibility to use molecular dynamics (MD) simulation as the preliminary computational filter for thermostable enzymes screening. Sequence information of eleven uncharacterized CEs were chosen to be analyzed by MD simulations. The CE from Dictyoglomus thermophilum(Dith-CE) was determined experimentally to be one of the most thermostable CEs with the highest epimerization (160 +/- 6.5 U mg(-1)) and isomerization activities (3.52 +/- 0.23 U mg(-1)) among all the reported CEs. This enzyme shows the highest isomerization activity at 85 degrees C and pH 7.0. The kinetic parameters (k(cat) and K-m) of isomerization activity of this CE are 3.98 +/- 0.3 s(-1) and 235.2 +/- 11.2 mM, respectively. These results suggest that the CE from Dith-CE is a promising lactulose-producing enzyme. (c) 2019 Elsevier B.V. All rights reserved.
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