Enhancing stability of enzymes for industrial applications: molecular insights and emerging approaches.

The growing demand for robust biocatalysts in industrial bioprocesses has intensified the pursuit of enzymes capable of functioning under extreme physicochemical conditions. This work critically examines the molecular determinants of enzyme stability, including thermostability, pH tolerance, halotolerance, resistance to solvents and oxidative stress, mechanical resilience to shear and pressure, and storage stability. These traits are essential for sustained catalytic performance in sectors such as bioenergy, pharmaceuticals, food, textiles, and environmental remediation. Recent advances in structure-guided engineering, molecular dynamics, and mutational profiling have enabled rational strategies to enhance enzyme resilience. By adopting a multi-parametric lens, this study bridges specific molecular adaptations with industrial challenges, offering a systems-level framework often lacking in single-condition analyses. It also explores emerging frontiers, including AI-assisted enzyme design, metagenomic discovery from extremophiles, and synthetic reconstruction of adaptive pathways, paving the way for next-generation biocatalysts optimised for scalability, performance, and sustainability. The novelty of this work lies in its integrative approach combining molecular insight, environmental origin, and computational tools to guide the development of industrially robust enzymes.