In vitro kinetic analysis reveals that sulfonyl-containing sweeteners boost glucose oxidase activity by lowering allostery activation energy, highlighting novel strategies for enzyme modulation.
Elucidating the catalytic mechanism of glucose oxidase (GOD) and modulating its activity are critical for biomedicine and food production. This study demonstrates that sulfonyl-containing sweeteners enhance GOD activity and catalytic efficiency. Rapid kinetic analysis of allosteric transitions and redox reactions revealed that glucose recognition follows the induced-fit model: glucose induces conformational changes in GOD, enabling the redox reaction. The sweeteners increase GOD’s conformational flexibility and substrate affinity while reducing the activation energy for allostery. This facilitates the transition between active and inactive states and accelerates the catalytic function of flavin adenine dinucleotide toward the substrate. These findings provide deeper insights into GOD catalysis and regulation, opening new avenues for its diverse applications.
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Sun et al. (2026) studied this question.
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