Journal
BIOCHEMICAL ENGINEERING JOURNAL
Volume 161, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bej.2020.107654
Keywords
D-tagatose; Co-immobilization; alpha GP&PGM; One-pot production
Funding
- National Nature Science Foundation of China [31871745]
- National First-Class Discipline program of Food Science and Technology [JUFSTR 20180203]
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D-tagatose (D-tag) is a natural yet rare hexose that can be used as a functional sweetener owing to its hypoglycemic and anticaries properties. A four-step enzymatic cascade reaction was performed to synthesize D-tagatose from maltodextrin. In this study, we constructed a catalytic cascade system by co-immobilizing alpha-glucan phosphorylase (alpha GP) and phosphoglucomutase (PGM) on Duolite A568 exchange resin to produce glucose 6-phosphate (G6P), a precursor of D-tagatose. Our results showed that the thermal stability of co-immobilized alpha GP&PGM was enhanced comparing to free enzymes. Co-immobilized alpha GP&PGM retained 63.4% activity after incubating at 75 degrees C for 36 h, whereas free enzymes retained only 12% activity. Moreover, the relative activity of co-immobilized alpha GP&PGM was consistently maintained above 78.5% after eight cycles of reuse, and its storage stability was approximately eleven times higher than that of the free enzymes after storage at 4 degrees C for 60 days. Notably, we successfully co-immobilized dual enzymes on the resin using poly (ethylene glycol) diglycidyl ether, which was found to be more effective than glutaraldehyde. The results suggested that co-immobilized alpha GP&PGM could act as a promising catalyst for the one-pot production of G6P and be used in the starting pathway for the further production of D-tagatose.
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