Enzyme stability is the persistence of an enzyme's catalytically competent structure and activity under stated conditions over time. Immobilization can preserve activity by restricting conformational changes, preventing dissociation of subunits, or creating a favorable local environment [1]. Structural stability includes the energetic resistance of the folded protein to unfolding, while kinetic stability concerns the rate of irreversible inactivation. Melting temperature and activity half-life describe different aspects of these properties [2]. Amino acid substitutions can modify packing, interactions among residues, or conformational flexibility and thereby change stability [3]. The support and surrounding solution also participate in stabilization of immobilized preparations. In adsorbed lipases, solvent or detergent exposure can cause desorption, and unfolding can further reduce catalytic activity during operation [4].
- protein conformation
- enzyme inactivation
- thermal stability
- activity retention
References
- Rafael C. Rodrigues; Ángel Berenguer-Murcia; Diego Carballares; Roberto Morellon-Sterling; Roberto Fernandez-Lafuente; Stabilization of Enzymes via Immobilization: Multipoint Covalent Attachment and Other Stabilization Strategies. Biotechnol. Adv. 2021, 52, 107821, 10.1016/j.biotechadv.2021.107821.
- Karen M Polizzi; Andreas S Bommarius; James M Broering; Javier F Chaparro-Riggers; Stability of Biocatalysts. Curr. Opin. Chem. Biol. 2007, 11, 220-225, 10.1016/j.cbpa.2007.01.685.
- Jesse D. Bloom; Sy T. Labthavikul; Christopher R. Otey; Frances H. Arnold; Protein Stability Promotes Evolvability. Proc. Natl. Acad. Sci. 2006, 103, 5869-5874, 10.1073/pnas.0510098103.
- Rafael C. Rodrigues; Jose J. Virgen-Ortíz; José C.S. dos Santos; Ángel Berenguer-Murcia; Andres R. Alcantara; Oveimar Barbosa; Claudia Ortiz; Roberto Fernandez-Lafuente; Immobilization of Lipases on Hydrophobic Supports: Immobilization Mechanism, Advantages, Problems, and Solutions. Biotechnol. Adv. 2019, 37, 746-770, 10.1016/j.biotechadv.2019.04.003.