Enhancing Thermostability of Extremozymes: Strategies and Industrial Applications
摘要
Enzymes are renowned for their high specificity and efficiency, making them valuable in numerous industries. Nonetheless, a significant challenge is thermal instability, which leads to denaturation of the protein structure and subsequent loss of activity at elevated temperatures. This issue imposes considerable constraints on the efficiency and cost-effectiveness of industrial processes. Consequently, enhancing the thermostability of enzymes can yield substantial benefits, such as increased reaction rates, cost savings, improved product quality, enhanced long-term storage stability, and improved hygiene. Several strategies have been developed to enhance enzyme thermostability. These include protein engineering techniques aimed at optimizing the function of existing enzymes, such as rational design, directed evolution, semirational design, and ancestral protein reconstruction (APRC). Additionally, enzyme immobilization techniques, which confine enzymes to specific locations and facilitate continuous reactions and reuse, have been employed. These techniques encompass carrier-binding, crosslinking, and entrapment methods. Other approaches include PEGylation, which involves the attachment of polyethylene glycol (PEG) molecules, and solvent engineering, which modifies the solvent environment of enzymes. Thermostable enzymes are already being applied in various industries, including biofuel and bioethanol production, detergent, food, pharmaceutical, chemical, textile, and environmental biotechnology. By enabling reactions under high-temperature conditions and offering excellent storage stability, these enzymes contribute to the advancement of more efficient and environmentally sustainable “clean and green” technologies. Research and development on thermostable enzymes extend beyond scientific interest to encompass significant economic incentives.