The Characterization of a Novel D-allulose 3-Epimerase from Blautia produca and Its Application in D-allulose Production

• Published in: Foods Vol. 11; no. 20; p. 3225
• Main Authors: Tang, Xinrui, An, Yingfeng, Iqbal, Muhammad Waheed, Cong, Hongri, Zhang, Guoyan, Zhang, Yufei, Ravikumar, Yuvaraj, Zabed, Hossain M, Zhao, Mei, Zhou, Haixing, Qi, Xianghui
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 15.10.2022; MDPI
• Subjects: biochemical characterization; Biosynthesis; Biotransformation; Blautia; Blautia produca; Carbon dioxide; Catalysis; Cloning; Cobalt; Conversion; D-allulose; D-allulose 3-epimerase; Diabetes; E coli; Enzymes; Epimerase; Food; Food science; Fructose; Genomes; Metals; Microorganisms; Pharmaceutical industry; Phylogenetics; Probiotics; Proteins; Substrates; United States > US; China; Blautia produca; biochemical characterization; D-allulose; D-allulose 3-epimerase; biotransformation; probiotics
• ISSN: 2304-8158; 2304-8158
• DOI: 10.3390/foods11203225

D-allulose is a natural rare sugar with important physiological properties that is used in food, health care items, and even the pharmaceutical industry. In the current study, a novel D-allulose 3-epimerase gene (Bp-DAE) from the probiotic strain was discovered for the production and characterization of an enzyme known as Bp-DAE that can epimerize D-fructose into D-allulose. Bp-DAE was strictly dependent on metals (Mn and Co ), and the addition of 1 mM of Mn could enhance the half-life of Bp-DAE at 55 °C from 60 to 180 min. It exhibited optimal activity in a pH of 8 and 55 °C, and the values of Bp-DAE for the different substrates D-fructose and D-allulose were 235.7 and 150.7 mM, respectively. Bp-DAE was used for the transformation from 500 g/L D-fructose to 150 g/L D-allulose and exhibited a 30% of conversion yield during biotransformation. Furthermore, it was possible to employ the food-grade microbial species for the production of D-allulose using a technique of whole-cell catalysis to circumvent the laborious process of enzyme purification and to obtain a more stable biocatalyst. This method also yields a 30% conversion yield.