In the pursuit of effective carbon capture technologies, this study presents a novel method for monitoring CO2 absorption in concentrated Monoethanolamine (MEA) solvent systems. Carbon capture is essential for mitigating greenhouse gas emissions, and MEA is a widely used solvent for this purpose. However, real-time and accurate monitoring of CO2 absorption remains a challenge. Here, we introduce a method based on electrical conductivity variations resulting from the interaction between CO2 and MEA. Experimental results demonstrate the feasibility and efficiency of this approach, offering promising prospects for enhanced carbon capture monitoring and process control.

Glucose-transforming enzymes derived from natural microbial sources play a critical role in biochemical energy conversion, metabolic regulation, and industrial biocatalysis. This study provides a comprehensive theoretical and analytical investigation into the catalytic efficiency, thermal stability, and molecular characteristics of such an enzyme system. The research integrates enzyme kinetic theory, thermodynamic constraints, and graph-based reaction modeling to construct a unified interpretative framework for enzymatic glucose transformation.
The catalytic behavior is analyzed through modified Michaelis–Menten kinetics, incorporating parameters such as turnover rate, substrate affinity, and reaction velocity modulation. Thermal properties are evaluated using Arrhenius-based modeling and thermodynamic stability analysis to understand enzyme resilience under varying environmental conditions. Molecular characteristics are interpreted through structural abstraction models, where enzyme–substrate interactions are represented as dynamic interaction networks.
The study further extends into reaction network modeling using hypergraph and bond graph analogies to capture multi-step biochemical transitions and energy flow distribution within enzymatic systems. This allows a deeper understanding of how microbial enzymes optimize glucose oxidation pathways under constrained thermodynamic environments.
Comparative synthesis with prior biochemical studies indicates that microbial-derived glucose-transforming enzymes exhibit adaptive catalytic efficiency influenced by environmental selection pressures and molecular flexibility. The analysis highlights the coupling between molecular structure, thermal stability, and catalytic performance as a unified system rather than independent properties.
Findings suggest that enzyme efficiency is maximized under moderate thermal conditions with optimal substrate availability, while deviations in temperature significantly alter kinetic stability. The study contributes to biochemical engineering, microbial biotechnology, and enzymatic process modeling by providing a structured framework for understanding glucose-transforming enzyme systems.
Overall, this work establishes a theoretical foundation for future experimental validation and biotechnological optimization of microbial enzymatic systems involved in carbohydrate metabolism.