Background: D-Allulose is an ultra-low calorie sugar of multifarious health benefits, including anti-diabetic and anti-obesity potential. D-Allulose 3-epimerase family enzymes catalyze biosynthesis of D-allulose via epimerization of D-fructose.
Results: A novel D-allulose 3-epimerase (DaeB) was cloned from a plant probiotic strain, Bacillus sp. KCTC 13219, and expressed in Bacillus subtilis cells. The purified protein exhibited substantial epimerization activity in a broad pH spectrum, 6.0-11.0. DaeB was able to catalyze D-fructose to D-allulose bioconversion at the temperature range of 35 °C to 70 °C, exhibiting at least 50 % activity. It displaced excessive heat stability, with the half-life of 25 days at 50 °C, and high turnover number (k 367 s). The coupling of DaeB treatment and yeast fermentation of 700 g L D-fructose solution yielded approximately 200 g L D-allulose, and 214 g L ethanol.
Conclusions: The novel D-allulose 3-epimerase of Bacillus sp. origin discerned a high magnitude of heat stability along with exorbitant epimerization ability. This biocatalyst has enormous potential for the large-scale production of D-allulose.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7934257 | PMC |
| http://dx.doi.org/10.1186/s12934-021-01550-1 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Coexpression of D-Allulose 3-Epimerase and L-Rhamnose Isomerase in through a Dual Promoter Enables High-Level Biosynthesis of D-Allose from D-Fructose in One Pot.
J Agric Food Chem
January 2025
School of Food and Biological Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, PR China.
D-Allose, a rare sugar, has gained significant attention not only as a low-calorie sweetener but also for its anticancer, antitumor, anti-inflammatory, antioxidant, and other pharmaceutical properties. Despite its potential, achieving high-level biosynthesis of D-allose remains challenging due to inefficient biocatalysts, low conversion rates, and the high cost of substrates. Here, we explored the food-grade coexpression of D-allulose 3-epimerase (Bp-DAE) and L-rhamnose isomerase (BsL-RI) within a single cell using WB800N as the host.
View Article and Find Full Text PDFOptimization of fermentation conditions for whole cell catalytic synthesis of D-allulose by engineering Escherichia coli.
Sci Rep
December 2024
State Key Laboratory of Biobased Material and Green Papermaking, Qilu University of Technology, Shandong Academy of Science, Jinan, 250353, People's Republic of China.
D-allulose/D-psicose is a significant rare sugar with broad applications in the pharmaceutical, food, and other industries. In this study, we cloned the D-allulose 3-epimerase (DPEase) gene from Arthrobacter globiformis M30, using pET22b as the vector. The recombinant E.
View Article and Find Full Text PDFEnhancing Stability and Catalytic Activity of d-Allulose 3-Epimerase through Multistrategy Computational Design and Cross-Regional Advantageous Mutations.
J Agric Food Chem
January 2025
College of Light Industry and Food Engineering, Guangxi University, 100 Daxue Road, Nanning 530004, Guangxi, China.
d-Allulose 3-epimerase (DAEase) derived from has excellent properties in the catalytic production of d-allulose, a rare sugar with unique biological functions. However, the industrial application of DAEase (Cb-DAEase) for d-allulose production is hindered by its low enzyme activity, poor long-term thermostability, and pH tolerance. In this study, we identified potential noncatalytic residues in Cb-DAEase using methods such as proline substitution, surface charge engineering, and surface residue prediction.
View Article and Find Full Text PDFConstruction of the Thermostable D-Allulose 3-Epimerase from M30 by Protein Engineering Method.
J Appl Glycosci (1999)
November 2024
1 Matsutani Chemical Industry Co., Ltd.
D-Allulose 3-epimerase catalyzes C-3 epimerization between D-fructose and D-allulose was found in strain M30. The enzyme gene was cloned, and its recombinant enzyme and the mutant variants were expressed in Using the information of the sequence and model structure, we succeed in the improvement of melting temperature for the enzyme without significant loss of the enzyme activity by protein engineering method. The melting temperatures were increased by 2.
View Article and Find Full Text PDFGut Microbial Utilization of the Alternative Sweetener, D-Allulose, via AlsE.
bioRxiv
November 2024
College of Computer, Mathematical and Natural Sciences, University of Maryland, College Park, Maryland, USA.
D-allulose, a rare sugar with emerging potential as a low-calorie sweetener, has garnered attention as an alternative to other commercially available alternative sweeteners, such as sugar alcohols, which often cause severe gastrointestinal discomfort. D-allulose-6-phosphate 3-epimerase (AlsE) is a prokaryotic enzyme that converts D-allulose-6-phosphate into D-fructose-6-phopshate, enabling its use as a carbon source. However, the taxonomic breadth of AlsE across gut bacteria remains poorly understood, hindering insights into the utilization of D-allulose by microbial communities.
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!