Enzymatic fructose removal from D‐psicose bioproduction model solution and the system modeling and simulation

Abstract

BACKGROUND The rare sugar D‐psicose has important physiological functions, and has been used as an ingredient in foods and dietary supplements. It can be mass produced from D‐fructose in industry. However, separation of D‐psicose from D‐fructose is difficult. RESULTS In this research, a reaction purification system consisting of two continuous stirred tank reactors (CSTR) containing immobilized glucose isomerase (GI) and glucose oxidase (GOD), respectively, for D‐fructose removal was constructed. Using this system D‐fructose was transformed into gluconic acid and separated from D‐psicose easily using anion exchange resin. Modeling and simulation was carried out for this system and the model was verified by experiments and used in process predictions. CONCLUSION D‐Psicose can be efficiently purified using the proposed reaction purification system. The final purity of the D‐psicose is 91.2%, which meets the need for crystallization to obtain highly purified product. The mathematical model developed for this system can simulate and predict the process well, which is useful in process analysis, prediction, and optimization to save time and costs compared with laboratory experiments. © 2017 Society of Chemical Industry

Research Advances of d-allulose: An Overview of Physiological Functions, Enzymatic Biotransformation Technologies, and Production Processes

“…Li et al constructed a reaction purification system consisting of two continuously stirred tank reactors, which respectively contained immobilized glucose isomerase and glucose oxidase for the removal of d -fructose. In this system, d -fructose is converted to gluconic acid and is easily separated from d -allulose by anion exchange resins [ 139 ].…”

Review on D-Allulose: In vivo Metabolism, Catalytic Mechanism, Engineering Strain Construction, Bio-Production Technology

“…Further, the purity of D-allulose reaches 98.3% via an approach of DTF-Ca 2+ cation exchange chromatography (Xing et al, 2011). For the mixed system of D-allulose and D-fructose, D-fructose is first transformed into gluconic acid, and then D-allulose of 91.2% purity is obtained by anion exchange resin (Li et al, 2018b).…”

Engineering Escherichia coli for d-Allulose Production from d-Fructose by Fermentation

“…Enzymes that have been found to catalyze this reaction include d -tagatose 3-epimerase (DTEase) and d -allulose 3-epimerase (DPEase), of which DPEase appears to be superior to DTEase in terms of substrate specificity, but its poor thermostability limits DPEase application in d -allulose production . A few studies suggested that random and site-directed mutagenesis of DPEase might result in a modest improvement in thermal resistance. , Also, several attempts have been made to synthesize d -allulose from d -glucose through a two-step enzymatic cascade catalyzed successively by d -xylose isomerase and DTEase or DPEase. , Whether using d -fructose or d -glucose as a substrate, it generally requires immobilization as a way for stabilization and reuse of enzymes, as well as ion-exchange chromatography for separation of d -allulose from sugar mixtures …”

“…Also, there are more impurities contained in fermentation broth than in the enzymatic method. The generation of byproducts may further increase the difficulty of product separation. , …”

“…27,28 Whether using D-fructose or D-glucose as a substrate, it generally requires immobilization as a way for stabilization and reuse of enzymes, 29 as well as ion-exchange chromatography for separation of D-allulose from sugar mixtures. 30 Although these enzymatic methods have advantages of conversion rate and product purification, production and immobilization of enzymes are costly and time-consuming; especially, the thermostability of key enzymes has not yet been completely addressed, reducing the reusability of the prepared biocatalyst. Microbial fermentation, by contrast, may be an ideal alternative to enzymatic conversion for producing Dallulose.…”