sp. d-tagatose 3-epimerase (sDTE) catalyzes the conversion of d-tagatose to d-sorbose. It also recognizes d-fructose as a substrate for d-allulose production. The optimal temperature and pH of the purified sDTE was 50 °C and 8.0, respectively. Based on the sDTE homologous model, Glu154, Asp187, Gln213, and Glu248, form a hydrogen bond network with the active-site Mn and constitute the catalytic tetrad. The amino acid residues around O-1, -2, and -3 atoms of the substrates (d-tagatose/d-fructose) are strictly conserved and thus likely regulate the catalytic reaction. However, the residues at O-4, -5, and -6, being responsible for the substrate-binding, are different. In particular, Arg65 and Met9 were found to form a unique interaction with O-4 of d-fructose and d-tagatose. The whole cells with recombinant sDTE showed a higher bioconversion rate of 42.5% in a fed-batch bioconversion using d-fructose as a substrate, corresponding to a production of 476 g Ld-allulose. These results suggest that sDTE is a potential industrial biocatalyst for the production of d-allulose in fed-batch mode.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9059984 | PMC |
| http://dx.doi.org/10.1039/c8ra10029b | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Thermostability Enhancement of Tagatose 4-Epimerase through Protein Engineering and Whole-Cell Immobilization.
J Agric Food Chem
January 2025
School of Biotechnology and Key Laboratory of Industrial Biotechnology Ministry of Education, Jiangnan University, Wuxi 214122, China.
d-Tagatose, a rare sugar endowed with a low-calorie property, superior taste quality, and probiotic functionality, has garnered significant research attention. However, the prevailing biological production methods relying on β-galactosidase and l-arabinose isomerase face challenges including high cost and suboptimal conversion efficiency. Consequently, it is of great research significance to find efficient alternative routes for d-tagatose synthesis.
View Article and Find Full Text PDFEvaluation of cross-linkers in the design of immobilized multi isomerase cascade for the preparation of rare sugars.
Int J Biol Macromol
December 2024
School of Chemistry and Life Sciences, Suzhou University of Science and Technology, Suzhou 215009, China. Electronic address:
The cascade of sugar isomerases is one of the most practical methods for producing rare sugars, and enzyme immobilization endows it with high economic efficiency, operational convenience and reusability. However, the most employed cross-linker glutaraldehyde (GA) has the disadvantages of enzyme deactivation and limitation of substrate binding. Herein, three compounds, glyoxal, GA, and 2,5-furandicarboxaldehyde (DFF) were evaluated within a previously developed cascade comprising ribose-5-phosphate isomerase and D-tagatose-3-epimerase to prepare D-ribulose form D-xylose.
View Article and Find Full Text PDFRational design improves both thermostability and activity of a new D-tagatose 3-epimerase from Kroppenstedtia eburnean to produce D-allulose.
Enzyme Microb Technol
August 2024
School of Food Engineering, Anhui Science and Technology University, Chuzhou 233100, China; School of Biotechnology and Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, Wuxi 214122, China. Electronic address:
D-allulose is a naturally occurring rare sugar and beneficial to human health. However, the efficient biosynthesis of D-allulose remains a challenge. Here, we mined a new D-tagatose 3-epimerase from Kroppenstedtia eburnean (KeDt3e) with high catalytic efficiency.
View Article and Find Full Text PDFExploiting the biocatalytic potential of co-expressed l-fucose isomerase and d-tagatose 3-epimerase for the biosynthesis of 6-deoxy-l-sorbose.
Bioorg Chem
April 2024
School of Life Sciences, Guangzhou University, 230 Wai Huan Xi Road, Guangzhou 510006, Guangdong, China; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, Jiangsu, China. Electronic address:
6-Deoxy-l-sorbose (6-DLS) is an imperative rare sugar employed in food, agriculture, pharmaceutical and cosmetic industeries. However, it is a synthetic and very expensive rare sugars, previously synthesized by chemo-enzymatic methods through a long chain of chemical processes. Recently, enzymatic synthesis of rare sugars has attracted a lot of attention due to its advantages over synthetic methods.
View Article and Find Full Text PDFThe Engineering, Expression, and Immobilization of Epimerases for -allulose Production.
Int J Mol Sci
August 2023
Microbial Cell Bioprocessing, Bioprocessing Technology Institute, Agency for Science, Technology and Research (A*STAR), Singapore 138668, Singapore.
The rare sugar -allulose is a potential replacement for sucrose with a wide range of health benefits. Conventional production involves the employment of the Izumoring strategy, which utilises -allulose 3-epimerase (DAEase) or -psicose 3-epimerase (DPEase) to convert -fructose into -allulose. Additionally, the process can also utilise -tagatose 3-epimerase (DTEase).
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!