Estimating the structural and spatial variables of allantoinase enzyme critical for protein adsorption.

Abstract

Designing enzyme-based sensors necessitates a comprehensive exploration of macromolecular properties. Integrating enzymes with a suitable transducer involves immobilizing them onto a surface, facilitated through adsorption or entrapment techniques. Allantoin, a stable biomarkers metabolite, holds promise for detecting oxidative stress-related complications through its enzyme. In this study, we examined allantoinase from various taxa, with bacterial origin comprising over 70 % of the dataset. Crucial residues such as Asp, His, and Gly in the active binding site and associated hydrophobic area play a critical role in maintaining binding specificity and sensitivity. In this work, we utilized bioinformatics tools to analyze properties such as pI, solubility index, amino acid hydropathy, stability, disordered regions, solvent-accessible surface area, and hydrodynamic parameters. The stability of allantoinase is assessed through surface Cys residues, hydrophobicity, and thermostability. Furthermore, the compactness and spherical geometry of the enzyme, which are crucial for protein adsorption are evaluated through parameters like spatial conformation, asphericity, and hydrodynamic radius distribution. Among the dataset, bacterial allantoinase demonstrates significant adaptability to environmental changes, as indicated by solvent-accessible surface area and instability index. This study highlights the importance of macromolecular properties underscoring their significance in optimizing, calibrating, and ensuring the stability of enzyme-based sensor design.