Characterization of a d-psicose 3-epimerase from Dorea sp. CAG317 with an acidic pH optimum and a high specific activity

Development of food‐grade expression system for d‐allulose 3‐epimerase preparation with tandem isoenzyme genes in Corynebacterium glutamicum and its application in conversion of cane molasses to D‐allulose

“…The problem of internal homologous recombination can be circumvented by constructing gene cassettes using the isoenzymes of DAE, which catalyze the same reaction but with low‐similarity sequence. In addition, those isoenzymes exhibit different biochemical properties in terms of substrate affinity, catalytic efficiency and optimum reaction conditions (Yoshida et al, ; Zhang et al, ; Zhu et al, ). Combinatorial expression of multiple DAEs in one cell would broaden the biochemical properties and enhances the total catalytic efficacy in the conversion of fructose comparing with the strain expressing only a single DAE.…”

Recent advances in d -allulose: Physiological functionalities, applications, and biological production

“…Among all ketose 3-epimerases reported, DPEase from Treponema primitia as well as DPEase from Dorea sp., exhibited the highest optimum temperature of 70 C (Zhang, Zhang, Jiang, & Mu, 2016;Zhang et al, 2015), while DTEase from Rhodobacter sphaeroides showed the lowest optimum temperature of 40 C (Zhang et al, 2009). It is generally known that an elevated operating temperature is required for the industrial production of rare sugars, because high reaction temperatures could induce higher reactivity (a higher reaction rate and lower diffusional restrictions), lower viscosity, higher stability, higher process yield (increased solubility of substrates and products and a favorable equilibrium displacement during endothermic reactions), and less contamination (Mozhaev, 1993).…”

“…DPEase, T. primitia DPEase and Dorea sp. DPEase (Zhang et al, 2016;Zhang, Fang, Zhang, et al, 2013;Zhang et al, 2015). In addition, the thermostability might be increased through molecular modification.…”

“…In the past two years, the neutral C. bolteae DPEase (pH 7.0) and the acidic Desmospora sp. DPEase (pH 6.0) have been characterized in our research group through a screening method (Jia et al, 2014;Zhang et al, 2015). Dorea sp.…”

“…DPEase, T. primitia DPEase and Dorea sp. DPEase, metal ion is an essential cofactor for catalysis (Jia et al, 2014;Mu et al, 2011;Mu et al, 2013;Zhang, Fang, Zhang, et al, 2013;Zhang et al, 2015;Zhang et al, 2016); they required Co 2þ as the optimum metal ion. Clostridium scindens DPEase is also metal-dependent, but the optimum metal ion is Mn 2þ (Zhang, Fang, Xing, et al, 2013).…”