Quantitative assessment of oxidoreductase and catalase enzymatic activity in model systems for catalyzed degradation of glucose and hydrogen peroxide
Year: 2025
Type: article
Abstract: The study quantitatively characterizes the process parameters that enable glucose removal via the glucose oxidase/catalase (GO/CAT) enzymatic system in acidic model solutions. Screening across a pH range of 4.0 to 5.5 and temperatures from 25 to 50 °C identified pH 5.5 and 40 °C as optimal for GO, with activity at pH 5.0 reduced by only 2.5%. Under these conditions, catalase retained 86.5% of its maximal activity. Dissolved oxygen concentration was found to be a key factor that impacts glucose conversion. Without oxygenation (initial dissolved oxygen concentration of 7.5–8.0 mg/L), 6-hour reactions achieved 29.0% glucose removal. Additional oxygenation (9.5–11.0 mg/L), using 1000 U GO with varying CAT activities (0, 1000, 3000, 4500 U), yielded glucose reductions of 2.9%, 57.0%, 75.9%, and 93.4%, respectively, from an initial glucose concentration of 27 g/L. At an oxygen concentration of 12.5–14.0 mg/L with 1000 U GO and 3000 U CAT, complete glucose oxidation was achieved within 4 hours. Hydrogen peroxide exhibited concentration-dependent inhibition of GO at pH 5.5/40 °C, with relative activities of 82.6%, 80%, and 70.4% at 45, 60, and 75 mmol/L H 2 O 2 , respectively. Thermal stability assessment revealed that GO retained 90.4% of its activity after 6 hours, whereas CAT retained 96.9%. Pasteurization (90 °C, 10 min) fully inactivated GO but caused 84.9% CAT activity. These findings establish practical operational guidelines — GO:CAT ≥ 1:3 and oxygen concentration > 9.5 mg/L for efficient glucose depletion under slightly acidic pH conditions and elevated temperature conditions. • Glucose oxidase, catalase, and oxygen lead to a significant reduction in glucose content • Oxygen and catalase are required to enhance the reaction capacity • An increase in the oxygen content in the solution allows for a decrease in reaction time • Hydrogen peroxide acts as an inhibitor of glucose oxidase
Source: Food Bioscience
Institution: Institute of Agricultural and Food Biotechnology
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,380
OpenAlex ID: W4414559908